Datasets:

lhallee

/

exp_new_unprocessed

like 0

A0A1S4G9J3

MVVAKKWIYAKPFEGLPKDENFRLEEETLPEPGENEFVAEAVFLSVDPYMRPYMASYPAGTVMIGGQVAKVTASRHPQFPVGATVFGNFGWRTHTLVNPEQGAADSRPYVLPPFGAHPASLGLGVLGMPGNTAYFGFLELCQPKQGETVVVSGAAGAVGSLVGQIAKIKGCRVVGIAGSDDKCGWLRELGFDATINYRQVERDAFADALRAAAPGGVDCYFDNVGGYISEAVLGQMNLYGRISVCGTISNYNAERAQVADPQRLFVFKQLRQEGFIVTRWAKRWMEGIRQNLQWIEEGRLRYQETVTDGFEQMPAAFVSMLTGGNTGKAVVKV

Anopheles gambiae (African malaria mosquito)

1.3.1.48; 1.3.1.74

CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213; Evidence={ECO:0000256|ARBA:ARBA00023498}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374, ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590; Evidence={ECO:0000256|ARBA:ARBA00023548}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133408; Evidence={ECO:0000256|ARBA:ARBA00023544}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586; Evidence={ECO:0000256|ARBA:ARBA00023544}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:79072, ChEBI:CHEBI:133411; Evidence={ECO:0000256|ARBA:ARBA00023543}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594; Evidence={ECO:0000256|ARBA:ARBA00023543}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208, ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133346; Evidence={ECO:0000256|ARBA:ARBA00023517}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209; Evidence={ECO:0000256|ARBA:ARBA00023517}; CATALYTIC ACTIVITY: Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112; Evidence={ECO:0000256|ARBA:ARBA00023553}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738; Evidence={ECO:0000256|ARBA:ARBA00023553}; CATALYTIC ACTIVITY: Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974; Evidence={ECO:0000256|ARBA:ARBA00023496}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205; Evidence={ECO:0000256|ARBA:ARBA00023496}; CATALYTIC ACTIVITY: Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; Evidence={ECO:0000256|ARBA:ARBA00023696}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618; Evidence={ECO:0000256|ARBA:ARBA00023696}; CATALYTIC ACTIVITY: Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH; Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748; Evidence={ECO:0000256|ARBA:ARBA00023504}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782; Evidence={ECO:0000256|ARBA:ARBA00023504}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276; Evidence={ECO:0000256|ARBA:ARBA00024160}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790; Evidence={ECO:0000256|ARBA:ARBA00024160}; CATALYTIC ACTIVITY: Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74; Evidence={ECO:0000256|ARBA:ARBA00023507}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739; Evidence={ECO:0000256|ARBA:ARBA00023507}; CATALYTIC ACTIVITY: Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH; Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455; Evidence={ECO:0000256|ARBA:ARBA00023691}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614; Evidence={ECO:0000256|ARBA:ARBA00023691}; CATALYTIC ACTIVITY: Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH; Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741; Evidence={ECO:0000256|ARBA:ARBA00023530}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786; Evidence={ECO:0000256|ARBA:ARBA00023530}; CATALYTIC ACTIVITY: Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00034052}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778; Evidence={ECO:0000256|ARBA:ARBA00034052}; CATALYTIC ACTIVITY: Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309; Evidence={ECO:0000256|ARBA:ARBA00023545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609; Evidence={ECO:0000256|ARBA:ARBA00023545};

Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome

prostaglandin metabolic process [GO:0006693]

cytoplasm [GO:0005737]

13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)+] activity [GO:0032440]

IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;

3.90.180.10;3.40.50.720;

A0A1S4GMJ4

MCILTLVERKHLKNMVHVRLLVMMHILIIYSTFGAVRRPINIRVLEGNSCDTPQVIGGKCMNISLCDPAFVHSIAYQEHTPVCQQNAFYRVICCQPFLDFCENSKQFQIMHGIEAEPGMFPHLARLGLKSEEDGIAWTCSANIISERFLLTAAHCNPVNIAGLGCAESMQCDQQNTVKSFISNPKYKTSFKYHDIALVELEQNIRFNKRVLPICPYISKTDLHESEDLVIAGWGATESHFQSPRLMFATVRTVLQNDCKDHYASLLKASPNKKLHQGITDEMYCAQGALVDNVTEYIDACSGDSGGPLQTKQNNNLYLIGVISTGFGCGSSSPGLYTRVASYFGWIKETVSATRDN

Anopheles gambiae (African malaria mosquito)

FUNCTION: Probable serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade (PubMed:33045027). In the susceptible strain G3, appears to be dispensable for ookinete elimination which occurs by lysis (PubMed:33045027). {ECO:0000269|PubMed:33045027}.

3.4.21.-

Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen

defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; proteolysis [GO:0006508]

extracellular space [GO:0005615]

serine-type endopeptidase activity [GO:0004252]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph (PubMed:33045027). Recruited by CLIPA8 to microbial surfaces where it is cleaved into the two chain active form (PubMed:33045027). {ECO:0000269|PubMed:33045027}.

PTM: Secreted as a full-length protein (PubMed:12364791). Following bacterium E.coli infection, proteolytically cleaved into two chains, p12 and p30, which remain covalently linked (PubMed:12364791). {ECO:0000269|PubMed:12364791}.

DOMAIN: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.

IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;

2.40.10.10;

A0A1S4GYC7

MKTVTNCSEPIDSENSIVISGISGKYPRSDNVQEFANNLYSKVDLVDDKEERWRHTHPDIPKRLGKLNHLEKFDADFFGYSPKEAHTMDPQHRLLLEHCYEAVMDAGLHLDDLRGSKTGVFIGISMSETETYWTYKKTQMPYRRVMLGFTRSMTALKIAYALDLKGPAMTVDTACSSSMYALDWACKAIRQGQCDAAIVAGTNLTLHPYITLQFALLGVLAADGYCRPFDKNASGYSRSEANAVILLQKAKDAKRIYAHVVNTKTNCDGYKLEGITFPSNKIQKQLLDELYSEVPYDPKDISYVEAHSTGTVVGDPEECDAIDKVFCPNRTSPLLVGSVKSNIGHSEPAAGLCSLTKCIIAMQTGLIPPNIHYTEPRKDVPSLLNGHLKVVDEATPLGGPLVAVNSFGFGGANAHALLHAHTRKKDHNIRPHGDLPRLVVWSGRTIEAVDQFLEGIAKHSFDPELYALTHNIQRKELAKMTSRGYAVLARGGDGSTTILQKNISKANKTLPPFAIVFGQMDYEWQATLQAFKKFPLFKASVEQCLALLKEPEYDCIFSKDNYATILQRAVWTLIIQIGVYQMLKSIGVKVDQYGGYSIGQITCAYIDGVLSLADAIRVAFTHGVLLSSYQNPETVNYRDIITNKELNSKLTSILESFLFAKATDRWKTATSVLSFRIYDPKSATQMFNRIDSNAIVLQPLPSIQSTDSLVNSFLASIGRAFIHGQHCQLLDLYPKVTFPVSLETPMIGPLIRWNHSVDWHVANFQTKKMVDQGSNKHSVTLAEQEYIAGHCIDGRVLIPATEYLYLVWDSFTSKTGTIPNEVAVQFTEVEFLRATTIAPGQVITLFVEINDISGHFEVSEGSTLVVKGCIQRLDHFQRQPIEQRNQPAITLPTQDFYKELRLRGYHYGGFFKSVMESAADGSHAKIEWKGNWTALLDCMLQVAIIAVDTRSLMIPTRIESIKIDPVRQKMSQQVNEQGVPHYGVCFDPDLNLLQSSGIEIRGLNASTIARRLPPGVPVLESYKFHPYFSQQLLQPAQAASIVLQTILDNQTTLVCSVTEIHSKTRDPIISLFGDAIGDLPLVKAHLTLLSTAKPEPIPNVTISEDKLMKQRNVLLLICENLFADDEFISDAINCLSDQGFILLRESPEYRLQDGHRRLQLVSTMSIEGETFLLLQQKKSAMNTSVDAHVIKVCSNDTTHNWLLELKQEVKTKPVILYAQHDPSSGIIGLVNCIRKEPNIQTVSCFFIDDPSAPAFDASNPFYKEKIELGLAINVYREGQWGSYRHFKLQEEPRYEPSTKHCFANCVKPGDLSSFTWMVGPLNEQSPSSPLARVVYSSLNFKDVMLATGRLTVETSFTNRLQQECVLGFEYSGVTTTGKRVMGMIPAGSMATMIETDRHFTLDVPDHISLEQAATIPTVYATVYASFFICSHIRKGNSILIHAGTGGVGLAAIRVCLAYGLEVFTTVSTKEKRDFLLSYFPDLNPNNIGNSRDISFETLIKERTNGRGVDFVLNSLSEEKLQASIRCLARGGHFLEIGKYDMMKDSKLAMTFFQRGITFTAVLVDLLFQEKRDFLLELHKLIMKDLAKGIILPLPTTVFQAHEIEQAFRYLATAKHIGKVVLKIRDNEDDLASVPISYLPRVYCNTEQSFVIAGGLGGFGLELADWLIIRGCRKLLLSSSRGITKPYQQYRINTWRTYGVQVTISTEDISTYDGCRRLLQQAIQMGPIAGIFNLAVQLRDAIIENQSVDKFAECLAPKATATHHLDALSRELCPMLKHFVVFSSVSCGRGNAGQSNYGMANSIMERIIEHRVVHGLPGKAIQWGAIGEVGIVADMQEDKIDMEIGGTLQQRLSSCIQVLDQLLTTSEPIVASMVVAEKRSSSGGAKNIVEAVMNIMNIRDMKSVSVESTLADIGMDSLMAVEIRQVLERDFDIILTPQDLRTLTFSKLQKLADAKTESETAEATTQQLQLQDLLASFGDETASHHTVLRLPSKCNDLEYDRPVLIIPGIESVSSPAWTKIASEINAPTFVLQTFAKGSDEQTIPGIVDSVFDEMFDTVFAKAEQFLVIGYSFGSLLALEVVKRLEARSLRGKLMLIDGSPLYLQRFASHHLSGFDDEHLQMLILTLVISFIFPTATQDVIKPVMDQPTYSDRVEKLMAVAHDSNPFSDQYARKMMRVLFYRLKVAMNMSTEVKEKIESPLVLVRSATIVDVEEDYGLNEFTVASLIVKIIDGTHQTMLANPELIEIINKDTL

Anopheles gambiae (African malaria mosquito)

FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000256|ARBA:ARBA00023442}.

CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000256|ARBA:ARBA00023357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813; Evidence={ECO:0000256|ARBA:ARBA00023357}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; Evidence={ECO:0000256|ARBA:ARBA00023387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865; Evidence={ECO:0000256|ARBA:ARBA00023387}; CATALYTIC ACTIVITY: Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65264, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881; Evidence={ECO:0000256|ARBA:ARBA00023385}; CATALYTIC ACTIVITY: Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; Evidence={ECO:0000256|ARBA:ARBA00023345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913; Evidence={ECO:0000256|ARBA:ARBA00023345}; CATALYTIC ACTIVITY: Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78458, ChEBI:CHEBI:78459; Evidence={ECO:0000256|ARBA:ARBA00023359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833; Evidence={ECO:0000256|ARBA:ARBA00023359}; CATALYTIC ACTIVITY: Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) + octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495; Evidence={ECO:0000256|ARBA:ARBA00023376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929; Evidence={ECO:0000256|ARBA:ARBA00023376}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP]; Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78462, ChEBI:CHEBI:78463; Evidence={ECO:0000256|ARBA:ARBA00023420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849; Evidence={ECO:0000256|ARBA:ARBA00023420}; CATALYTIC ACTIVITY: Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) + tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477; Evidence={ECO:0000256|ARBA:ARBA00023368}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897; Evidence={ECO:0000256|ARBA:ARBA00023368}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627, ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453; Evidence={ECO:0000256|ARBA:ARBA00023402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809; Evidence={ECO:0000256|ARBA:ARBA00023402}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|ARBA:ARBA00023388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861; Evidence={ECO:0000256|ARBA:ARBA00023388}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643, ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877; Evidence={ECO:0000256|ARBA:ARBA00023351}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651, ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481; Evidence={ECO:0000256|ARBA:ARBA00023401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909; Evidence={ECO:0000256|ARBA:ARBA00023401}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631, ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458; Evidence={ECO:0000256|ARBA:ARBA00023373}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829; Evidence={ECO:0000256|ARBA:ARBA00023373}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655, ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489; Evidence={ECO:0000256|ARBA:ARBA00023399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925; Evidence={ECO:0000256|ARBA:ARBA00023399}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635, ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462; Evidence={ECO:0000256|ARBA:ARBA00023332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845; Evidence={ECO:0000256|ARBA:ARBA00023332}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647, ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475; Evidence={ECO:0000256|ARBA:ARBA00023398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893; Evidence={ECO:0000256|ARBA:ARBA00023398}; CATALYTIC ACTIVITY: Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451; Evidence={ECO:0000256|ARBA:ARBA00023413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805; Evidence={ECO:0000256|ARBA:ARBA00023413}; CATALYTIC ACTIVITY: Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466; Evidence={ECO:0000256|ARBA:ARBA00023418}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857; Evidence={ECO:0000256|ARBA:ARBA00023418}; CATALYTIC ACTIVITY: Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470; Evidence={ECO:0000256|ARBA:ARBA00023416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873; Evidence={ECO:0000256|ARBA:ARBA00023416}; CATALYTIC ACTIVITY: Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480; Evidence={ECO:0000256|ARBA:ARBA00023390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905; Evidence={ECO:0000256|ARBA:ARBA00023390}; CATALYTIC ACTIVITY: Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457; Evidence={ECO:0000256|ARBA:ARBA00023346}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825; Evidence={ECO:0000256|ARBA:ARBA00023346}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488; Evidence={ECO:0000256|ARBA:ARBA00023419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921; Evidence={ECO:0000256|ARBA:ARBA00023419}; CATALYTIC ACTIVITY: Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461; Evidence={ECO:0000256|ARBA:ARBA00023364}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841; Evidence={ECO:0000256|ARBA:ARBA00023364}; CATALYTIC ACTIVITY: Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473, ChEBI:CHEBI:78474; Evidence={ECO:0000256|ARBA:ARBA00023367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889; Evidence={ECO:0000256|ARBA:ARBA00023367}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487; Evidence={ECO:0000256|ARBA:ARBA00023365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917; Evidence={ECO:0000256|ARBA:ARBA00023365}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000256|ARBA:ARBA00023361}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000256|ARBA:ARBA00023361}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000256|ARBA:ARBA00023414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000256|ARBA:ARBA00023414}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00023341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000256|ARBA:ARBA00023341}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP]; Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933; Evidence={ECO:0000256|ARBA:ARBA00023378}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124; Evidence={ECO:0000256|ARBA:ARBA00023410}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000256|ARBA:ARBA00023333}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399; Evidence={ECO:0000256|ARBA:ARBA00023333}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|ARBA:ARBA00023394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098; Evidence={ECO:0000256|ARBA:ARBA00023394}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023381}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566; Evidence={ECO:0000256|ARBA:ARBA00023381}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000256|ARBA:ARBA00023389}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85; Evidence={ECO:0000256|ARBA:ARBA00023370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994; Evidence={ECO:0000256|ARBA:ARBA00023370}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000256|ARBA:ARBA00023397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789; Evidence={ECO:0000256|ARBA:ARBA00023397}; CATALYTIC ACTIVITY: Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; Evidence={ECO:0000256|ARBA:ARBA00023352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801; Evidence={ECO:0000256|ARBA:ARBA00023352}; CATALYTIC ACTIVITY: Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; Evidence={ECO:0000256|ARBA:ARBA00023403}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; Evidence={ECO:0000256|ARBA:ARBA00023403}; CATALYTIC ACTIVITY: Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000256|ARBA:ARBA00023396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000256|ARBA:ARBA00023396}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000256|ARBA:ARBA00023348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000256|ARBA:ARBA00023348};

Phosphopantetheine;Phosphoprotein;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase

fatty acid biosynthetic process [GO:0006633]

(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity [GO:0047117]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; phosphopantetheine binding [GO:0031177]

IPR029058;IPR001227;IPR036736;IPR016035;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR036291;IPR032821;IPR020841;IPR042104;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR001031;IPR016039;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;

A0A1S4H145

MVNDDDRRWPRGLYDLPTRIGKIKDEDLMKLDAEFFKIHQKQAECMDPQLRMLLECTHEAIIDAGINPQEIRGSRTGVYIGCSNSETEQHWCADPDLVNGYGLTGCARAMFANRISFTFDFKGPSYAVDTACSSSLFALSQAFADMRAGHCDAAIVAGCGLILKPTMSLQFKRLNMLSKDGMCKAFDESGNGYVRSDGCVVTFLQRAANSRRIYASVLNVRTNTDGYKDQGITYPIGEMQKRLIRETYEEIGLSPADVTYVEAHGTGTKVGDPQEVNAITDFFCKDRKAPLLIGSVKSNMGHSEPASGVCSIAKILIAMEEGVIPGNLHYNSPNKDLYGLMDGRLKVVDRNLPWNGGIIGLNSFGFGGANAHVILKSNPKPKPISPKDGGFPKLMVASGRTTEAVEAFLDQAAKSKDDEEFVGLVNEIHSRNIPLHNHRGYTVVAGDGQSQTVREVLEVNADEKRPVWFIYSGMGSQWASMAKDLMQLEVFHNSIYRCAEALRPEGVDLIDVLTKSDETKFDNILNSFISIAAVQVALTDVLTHVGITPDGMVGHSVGELGCAYADGCFTPEQTVLAAYWRGRSILDTDLIAGQMAAVGLSWEECKQKLPKDVIPACHNSADSVTISGPVSSVSKVIADLNAQGIFAKGVKSSGIAFHSRYIADAAPKLRKSLDRIIPNPKNRTPRWISTSIPEESWPTALAQQSSSAYHVNNLLSPVLFAEGLKHVPANAICIEIAPHGLLQAILKRALGKDATNLSLMKRDHANNMIFLLSNLGKLYSSGAQPQVQKLYRPITYPVGRGTPMLNSLVKWDHSINWFLAKIGVENKSGETIIDVNLGKDEDAYLAGHTIDGRVLFPATGYLTLAWRTYAKMQGADIEKTPVVIENAVFHRATILPKDGSVKFGINFFDGTGAFEICEGGTLAVSGKLTIPEKIEQEELPLNKLEADKSGLPLNMSDVYKELRLRGYDYADMFRGVTRSDGRAITGELQWRDNWVSFMDTMLQFSILGKDLRELYLPTRIEKIVINPTRHLEMVANLTQTGDDRTLPVYMYREINVIKSGGVEMRGLRATLAPRRQGTQAPPTLEKYVFVPNANEKELAEGNSEKARLRAITAAVHLVIENSAGALKIKVAEASFERSPENTMAGTVQAIIEGEPTLASDVAVATTHQPDSLVQHYGESGVRVLSKDVAAGAIEQNCHLAIGYDTFGRADPDTILRNLRDSVKADGFVLLEESRSTFDARCRAALAKAGFTLVSTQVCEKKVFVLVRPTIAELAQRKSVVIALTERSFGWVEELKAALAKAEATGTYVYIVCQGEELCGAQGLMNCVKNEVGGKFARLYFIQDRKADKFSLTGAMYKEQLAKDLICNVLRPANGTPAPAWGTFRHLRLDNQSNAPSLPVEHAYINALTKGDLASLKWIESSLSRERPDPSARDARTELCTVYYAPINFRDVMLSSGKLGADALPGDLATQDCILGLEFAGRDSNGRRIMAMVQAKSLATTCVAQRNMIWEIPDGWTMEQASTVPCVYSTVYYALVMRGRMKRGESILIHAGSGGVGQAAISVALAAGVTVYTTVGSKEKREFLKRTFPQLTDRNIGNSRDCSFEQLVMRETQGRGVDLVLNSLAEEKLQASIRCLGLNGRFLEIGKFDLNNNSPLGMSVFLKNTSFHGILLDSVMEGDDETIAEVVKLVADGIKSGAVRPLPTSVFTEQQVEQAFRFMASGKHIGKVVVRVREEEKAKIVQPAPKLISAIPRTYMHAEKVYILIGGLGGFGLELSNWLVSRGAKIIVLTSRSGVRTGYQSLMIRRWTERGVKVVIDTNDVTTLKGAQKLLTDAARHGPVGGVFNLAAVLRDGLLENSTEADFRAVCVPKVDGTKNLDVATRELCPELDYFICFSSVSCGRGNQGQVNYGLANSAMERICEARHAVGLPATAIQWGAIGDTGLVLENLGDNDTVVGGTLPQRMPSCLQTMDLFMQQPSPVLASMVIAEKRKTDTGGVSLVGCIANILGLKDTKNVSDGATLADLGMDSLMGAEIKQTLERSFDLVLSAAEIRLLTFGKLRSFEKGGAAVAGDVGAAAGGSPAAAAASENAIGDGTQVKFSAELMPKECLVRMESAAPAGSKARPVFAVHAIEGVITALIPLAQTLPVPVYGLQCDEAAPLESLVLLAGYYIKQIRTVQPRGPYTIVGYSFGASIAYEMVAQLEKAGDTCQLLLVDGSPRYVSWYTEAQKQRNANGEVVQAEDEAYALAYFAMVCGSLDYGRTAKELVEAKSWEERVAKCAEMVHAKAPQYSLKLLATTAKSFVGKIVASHMYKPASKIKATVKLVKPTENYAKLQGDYGLSDLCQQKVELFTVEGDHRSMLLGDSMKKISDVLQKLL

Anopheles gambiae (African malaria mosquito)

FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000256|ARBA:ARBA00023442}.

1.1.1.100; 1.3.1.39; 2.3.1.41; 2.3.1.85; 3.1.2.14

CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000256|ARBA:ARBA00023357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813; Evidence={ECO:0000256|ARBA:ARBA00023357}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; Evidence={ECO:0000256|ARBA:ARBA00023387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865; Evidence={ECO:0000256|ARBA:ARBA00023387}; CATALYTIC ACTIVITY: Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65264, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881; Evidence={ECO:0000256|ARBA:ARBA00023385}; CATALYTIC ACTIVITY: Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; Evidence={ECO:0000256|ARBA:ARBA00023345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913; Evidence={ECO:0000256|ARBA:ARBA00023345}; CATALYTIC ACTIVITY: Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78458, ChEBI:CHEBI:78459; Evidence={ECO:0000256|ARBA:ARBA00023359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833; Evidence={ECO:0000256|ARBA:ARBA00023359}; CATALYTIC ACTIVITY: Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) + octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495; Evidence={ECO:0000256|ARBA:ARBA00023376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929; Evidence={ECO:0000256|ARBA:ARBA00023376}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP]; Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78462, ChEBI:CHEBI:78463; Evidence={ECO:0000256|ARBA:ARBA00023420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849; Evidence={ECO:0000256|ARBA:ARBA00023420}; CATALYTIC ACTIVITY: Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) + tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477; Evidence={ECO:0000256|ARBA:ARBA00023368}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897; Evidence={ECO:0000256|ARBA:ARBA00023368}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627, ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453; Evidence={ECO:0000256|ARBA:ARBA00023402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809; Evidence={ECO:0000256|ARBA:ARBA00023402}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|ARBA:ARBA00023388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861; Evidence={ECO:0000256|ARBA:ARBA00023388}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643, ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877; Evidence={ECO:0000256|ARBA:ARBA00023351}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651, ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481; Evidence={ECO:0000256|ARBA:ARBA00023401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909; Evidence={ECO:0000256|ARBA:ARBA00023401}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631, ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458; Evidence={ECO:0000256|ARBA:ARBA00023373}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829; Evidence={ECO:0000256|ARBA:ARBA00023373}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655, ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489; Evidence={ECO:0000256|ARBA:ARBA00023399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925; Evidence={ECO:0000256|ARBA:ARBA00023399}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635, ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462; Evidence={ECO:0000256|ARBA:ARBA00023332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845; Evidence={ECO:0000256|ARBA:ARBA00023332}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647, ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475; Evidence={ECO:0000256|ARBA:ARBA00023398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893; Evidence={ECO:0000256|ARBA:ARBA00023398}; CATALYTIC ACTIVITY: Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451; Evidence={ECO:0000256|ARBA:ARBA00023413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805; Evidence={ECO:0000256|ARBA:ARBA00023413}; CATALYTIC ACTIVITY: Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466; Evidence={ECO:0000256|ARBA:ARBA00023418}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857; Evidence={ECO:0000256|ARBA:ARBA00023418}; CATALYTIC ACTIVITY: Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470; Evidence={ECO:0000256|ARBA:ARBA00023416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873; Evidence={ECO:0000256|ARBA:ARBA00023416}; CATALYTIC ACTIVITY: Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480; Evidence={ECO:0000256|ARBA:ARBA00023390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905; Evidence={ECO:0000256|ARBA:ARBA00023390}; CATALYTIC ACTIVITY: Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457; Evidence={ECO:0000256|ARBA:ARBA00023346}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825; Evidence={ECO:0000256|ARBA:ARBA00023346}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488; Evidence={ECO:0000256|ARBA:ARBA00023419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921; Evidence={ECO:0000256|ARBA:ARBA00023419}; CATALYTIC ACTIVITY: Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461; Evidence={ECO:0000256|ARBA:ARBA00023364}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841; Evidence={ECO:0000256|ARBA:ARBA00023364}; CATALYTIC ACTIVITY: Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473, ChEBI:CHEBI:78474; Evidence={ECO:0000256|ARBA:ARBA00023367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889; Evidence={ECO:0000256|ARBA:ARBA00023367}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487; Evidence={ECO:0000256|ARBA:ARBA00023365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917; Evidence={ECO:0000256|ARBA:ARBA00023365}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000256|ARBA:ARBA00023361}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000256|ARBA:ARBA00023361}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000256|ARBA:ARBA00023414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000256|ARBA:ARBA00023414}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00023341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000256|ARBA:ARBA00023341}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP]; Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933; Evidence={ECO:0000256|ARBA:ARBA00023378}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124; Evidence={ECO:0000256|ARBA:ARBA00023410}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000256|ARBA:ARBA00023333}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399; Evidence={ECO:0000256|ARBA:ARBA00023333}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|ARBA:ARBA00023394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098; Evidence={ECO:0000256|ARBA:ARBA00023394}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023381}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566; Evidence={ECO:0000256|ARBA:ARBA00023381}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000256|ARBA:ARBA00023389}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85; Evidence={ECO:0000256|ARBA:ARBA00023370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994; Evidence={ECO:0000256|ARBA:ARBA00023370}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000256|ARBA:ARBA00023397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789; Evidence={ECO:0000256|ARBA:ARBA00023397}; CATALYTIC ACTIVITY: Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; Evidence={ECO:0000256|ARBA:ARBA00023352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801; Evidence={ECO:0000256|ARBA:ARBA00023352}; CATALYTIC ACTIVITY: Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; Evidence={ECO:0000256|ARBA:ARBA00023403}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; Evidence={ECO:0000256|ARBA:ARBA00023403}; CATALYTIC ACTIVITY: Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000256|ARBA:ARBA00023396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000256|ARBA:ARBA00023396}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000256|ARBA:ARBA00023348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000256|ARBA:ARBA00023348};

Hydrolase;Lipid metabolism;Phosphopantetheine;Phosphoprotein;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase

fatty acid biosynthetic process [GO:0006633]

cytoplasm [GO:0005737]

(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity [GO:0047117]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; phosphopantetheine binding [GO:0031177]

IPR029058;IPR001227;IPR036736;IPR014043;IPR016035;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR001031;IPR016039;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;

A0A1S4HE27

MHPSTSSTSSATTAAAAAPGTKCTPITADDSIVISGIAGKYPRSDSVEHFADNLYNKVDLVDDKEDRWRHLYAGIPKRLGKLNKLGKFDAEFFGSGFQETHTMDPQQRLLLEHCYEALLDAGLHPDDIRGTRTGVFVGVSIAETEIYWTYKKTKSPYNRSILGFVRSMLATKIAYALDLKGPSMAVDTACSSSMYALDWACKAIRQGQCDAAIVAGTNLTLHPYITLQFALLGVLAADGYCRPFDKNASGYSRSEANAVILLQKAKDAKRIYAHVVNTKTNCDGYKLEGITFPSNKIQKQLLDELYSEVPYDPKDISYVEAHSTGTVVGDPEECDAIEKVFCPDRTEPLLVGSVKSNIGHSEAAAGICSVTKCVIAMQNRIIPPNINYTEPRTDVPSLLNGKLKVVDQCTPLGGPLVAVNSFGFGGANAHALLHNCTKQKINGGYPKDGLPRLVVWSGRTIEAVDHFLDSLKGKSYDAEFYALTHNIQRSEIPKMTTKGYAIFGGRQDGTAELLYKAASNKIPKKYKLPPVTLAFGQLEGNWKATVQAFNQFPEFANGIAECLQAIKDCGFDAFDQTMQANDPIQHILWTFMAQVGVYRLLTASGVTIDQYAGYAVGQITCAYLDGVLSLHDALRVAYAHGYIIRAHHTEKSANYGSGVSSNKQLTVKLATALKPLRLQAATPKWFNPCQLKTFEMYDPKVMTTLFHTLGANEAIVLQPLNASKDVLMHFLKSLGEVFLKGHPVNLLPVYPAIQFPVSQGTGMISSLLEWDHSADWHVTNFRTTRMVDQSTSEYTISLSEQDYISGHCIDGRILIPATGYLFYVWDSFSGRMGIIPEEMPVEFSDIEFLRATTLVGDQQVTLTVDLNEVTGSFEVSEGTALVVKGRIQALTNYTPPETKHRQSDAVMMPSKDFYKELRLRGYHYGGYFKSVMESRTDGSYAKIEWKYNWTALLDCILQVAIIAVDSRSLVIPTRIESIKIDPIQHKLTDQATGNEVPSYNVCFDPDLNLLQCGAIEIRGLNASTIARRLPPGVPVLESYKFHPYYPQHTMAPSSAVSTIVQTILENQATIFFTVTEIHSKTKDPIISLFGDAIGDLPLVKAHLTLLSTAKPEPIPNVTISEDKLMKQRNVLLLICENLFADDEFISDAINCLSDQGFILLRESPEYRLQDGHRRLQLVSTMSIEGETFLLLQQKKSAMNTSVDAHVIKVCSNDTTHNWLLELKQEVKTKPIILYAQNDPSSGIIGLVNCIRKEPNIQTVSCFFIDDPSAPAFDASNPFYKEQIELGLAINVYRKGQWGSYRHFKLQEEPRYEPATKHCFANCVKPGDLSSFTWMVGPLSEQPPSSPLARVVYSSLNFKDVMIATGRLTVETFCTDRLQQECILGFEYSGVTTTGKRVMGIIGAGSMATIVESDPIFTLDVPDNISLEQAATIPTVYTTVYASFFVCAQIRKGNSILIHAGTGGVGLAAIRVCLAYGLEVFTTVSTKEKRDFLLSYFPDLNPNNIGNSRDISFETLIKERTNGRGVDFVLNSLSEEKLQASIRCLARGGHFLEIGKYDMMKDSKIAMTFFQRGITFTAVLVDLLFQEKRDLLVELHKLIMKDLAKGIIQPLPTTVFQAHEIEQAFRYLATAKHIGKVVLKIRDNEDDLASVPISYLPRVYCNPEQTFVIAGGLGGFGLELADWLIIRGCRKLLLSSSRGITKPYQQYRINTWRTYGVQVTVSTEDISTYDGCRRLLQQAIQMGPIAGIFNLAVQLRDAIIENQSVDKFAECLAPKATATHHLDALSRELCPMLKHFVVFSSVSCGRGNAGQSNYGMANSIMERIIEHRVVHGLPGKAIQWGAIGEVGIVADMQEDKIDMEIGGTLQQRLSSCIQVLDQLLTTSEPIVASMVVAEKRSSSGGAKNIVEAVMNIMNIRDMKSVSVESTLADIGMDSLMAVEIRQVLERDFDIILTPQDLRTLTFSKLQKLADAKTESETAEATTQQLQLQDLLASFGDETASHHTVLRLPSKCNDLEYDRPVLIIPGIESVSSPAWTKIASEINAPTFVLQTFAKGSDEQTIPGIVDSVFEEMFETVFAKAEQFLVIGYSFGALLALEVVKRLEARPLRGKLMLIDGSPLYLQRFASHHLSGFDDEHLQMAILTLVLRFSLPSVSNEILSSIMGEATYENRVTKMLDIGRESNPFSEEYTRKMMRVLLFRLKAAMNMSTEVKEKLASPLVLVRSGTIGDIEEDYGLTEFTSSSMIVKIIDGTHQTMLANMELLEIINKDTL

Anopheles gambiae (African malaria mosquito)

FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000256|ARBA:ARBA00023442}.

CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000256|ARBA:ARBA00023357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813; Evidence={ECO:0000256|ARBA:ARBA00023357}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; Evidence={ECO:0000256|ARBA:ARBA00023387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865; Evidence={ECO:0000256|ARBA:ARBA00023387}; CATALYTIC ACTIVITY: Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65264, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881; Evidence={ECO:0000256|ARBA:ARBA00023385}; CATALYTIC ACTIVITY: Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; Evidence={ECO:0000256|ARBA:ARBA00023345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913; Evidence={ECO:0000256|ARBA:ARBA00023345}; CATALYTIC ACTIVITY: Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78458, ChEBI:CHEBI:78459; Evidence={ECO:0000256|ARBA:ARBA00023359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833; Evidence={ECO:0000256|ARBA:ARBA00023359}; CATALYTIC ACTIVITY: Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) + octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495; Evidence={ECO:0000256|ARBA:ARBA00023376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929; Evidence={ECO:0000256|ARBA:ARBA00023376}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP]; Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78462, ChEBI:CHEBI:78463; Evidence={ECO:0000256|ARBA:ARBA00023420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849; Evidence={ECO:0000256|ARBA:ARBA00023420}; CATALYTIC ACTIVITY: Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) + tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477; Evidence={ECO:0000256|ARBA:ARBA00023368}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897; Evidence={ECO:0000256|ARBA:ARBA00023368}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627, ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453; Evidence={ECO:0000256|ARBA:ARBA00023402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809; Evidence={ECO:0000256|ARBA:ARBA00023402}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|ARBA:ARBA00023388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861; Evidence={ECO:0000256|ARBA:ARBA00023388}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643, ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877; Evidence={ECO:0000256|ARBA:ARBA00023351}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651, ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481; Evidence={ECO:0000256|ARBA:ARBA00023401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909; Evidence={ECO:0000256|ARBA:ARBA00023401}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631, ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458; Evidence={ECO:0000256|ARBA:ARBA00023373}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829; Evidence={ECO:0000256|ARBA:ARBA00023373}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655, ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489; Evidence={ECO:0000256|ARBA:ARBA00023399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925; Evidence={ECO:0000256|ARBA:ARBA00023399}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635, ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462; Evidence={ECO:0000256|ARBA:ARBA00023332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845; Evidence={ECO:0000256|ARBA:ARBA00023332}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647, ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475; Evidence={ECO:0000256|ARBA:ARBA00023398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893; Evidence={ECO:0000256|ARBA:ARBA00023398}; CATALYTIC ACTIVITY: Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451; Evidence={ECO:0000256|ARBA:ARBA00023413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805; Evidence={ECO:0000256|ARBA:ARBA00023413}; CATALYTIC ACTIVITY: Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466; Evidence={ECO:0000256|ARBA:ARBA00023418}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857; Evidence={ECO:0000256|ARBA:ARBA00023418}; CATALYTIC ACTIVITY: Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470; Evidence={ECO:0000256|ARBA:ARBA00023416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873; Evidence={ECO:0000256|ARBA:ARBA00023416}; CATALYTIC ACTIVITY: Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480; Evidence={ECO:0000256|ARBA:ARBA00023390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905; Evidence={ECO:0000256|ARBA:ARBA00023390}; CATALYTIC ACTIVITY: Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457; Evidence={ECO:0000256|ARBA:ARBA00023346}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825; Evidence={ECO:0000256|ARBA:ARBA00023346}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488; Evidence={ECO:0000256|ARBA:ARBA00023419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921; Evidence={ECO:0000256|ARBA:ARBA00023419}; CATALYTIC ACTIVITY: Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461; Evidence={ECO:0000256|ARBA:ARBA00023364}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841; Evidence={ECO:0000256|ARBA:ARBA00023364}; CATALYTIC ACTIVITY: Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473, ChEBI:CHEBI:78474; Evidence={ECO:0000256|ARBA:ARBA00023367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889; Evidence={ECO:0000256|ARBA:ARBA00023367}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487; Evidence={ECO:0000256|ARBA:ARBA00023365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917; Evidence={ECO:0000256|ARBA:ARBA00023365}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000256|ARBA:ARBA00023361}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000256|ARBA:ARBA00023361}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000256|ARBA:ARBA00023414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000256|ARBA:ARBA00023414}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00023341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000256|ARBA:ARBA00023341}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP]; Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933; Evidence={ECO:0000256|ARBA:ARBA00023378}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124; Evidence={ECO:0000256|ARBA:ARBA00023410}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000256|ARBA:ARBA00023333}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399; Evidence={ECO:0000256|ARBA:ARBA00023333}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|ARBA:ARBA00023394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098; Evidence={ECO:0000256|ARBA:ARBA00023394}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023381}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566; Evidence={ECO:0000256|ARBA:ARBA00023381}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000256|ARBA:ARBA00023389}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85; Evidence={ECO:0000256|ARBA:ARBA00023370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994; Evidence={ECO:0000256|ARBA:ARBA00023370}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000256|ARBA:ARBA00023397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789; Evidence={ECO:0000256|ARBA:ARBA00023397}; CATALYTIC ACTIVITY: Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; Evidence={ECO:0000256|ARBA:ARBA00023352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801; Evidence={ECO:0000256|ARBA:ARBA00023352}; CATALYTIC ACTIVITY: Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; Evidence={ECO:0000256|ARBA:ARBA00023403}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; Evidence={ECO:0000256|ARBA:ARBA00023403}; CATALYTIC ACTIVITY: Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000256|ARBA:ARBA00023396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000256|ARBA:ARBA00023396}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000256|ARBA:ARBA00023348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000256|ARBA:ARBA00023348};

Phosphopantetheine;Phosphoprotein;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase

fatty acid biosynthetic process [GO:0006633]; toxin biosynthetic process [GO:0009403]

(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity [GO:0047117]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; phosphopantetheine binding [GO:0031177]

IPR029058;IPR001227;IPR036736;IPR014043;IPR016035;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR036291;IPR032821;IPR020841;IPR042104;IPR049551;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR001031;IPR016039;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;

A0A1S5RW73

MSFATSLPRPTTTGAAGFGLPLATCISLSVSHSFSPKFGICNNTSLRLKSKAGSGCYEGIHRSQLAASTILEGHTPINPEVESEKIRLIERIRLMFRSMDDGEISVSPYDTAWVALVEDIGGSGGPQFPTSLEWISNNQLDDGSWGDRKFVLYDRILNTLACVVALTTWKMHPNKCEKGLRFISDNIEKLADEDEELMPVGFEIALPSLIDLAKRLCIEIPDNSASIKNIYAKRDSKLKRIPMDLMHKKPTSLLFSLEGMEGLNWDKLLDFQSEGSFLSSPSSTAYALHHTKDELCLEYLLKAVKKFNGGVPNAYPVDMFEHLWSVDRLRRLGISRYFQVEIDECLDYVYRYWTNKGICWARNMCVQDSDDSSMGFRLLRLYGYDVSIDVFKQFEEGGQFCSIPGQMTHAITGMYNLYRASQLMFPQEHILADARNFTANLLHQKRVTNSIVDKWIITKDLPGEVAYALDVPFYASLPRLEARFFLEQYGGDDDVWIGKTLYRMLYVNCNTYLELAKLDYKHCQTVHQLEWNSMQTWYRECNLGEFGLSERSLLLAYYIAASTAFEPEKSSERLAWAITTILVETIMSQELSDEQKREFVDEFVNISIINNQNGGRYKPGNRLVEVLINTVTLMAEGRGTDQQLSNAWKNWLKTWEEGGDLGEAEARLLLHTIHLSSGLDESSFSHPKYQQLLEATSKVCHQLRLFQNLKANDAQGSTSRLVTVTTFQIEAGMQELVKLIFTKTLEDLTSATKQSFFNIARSFYYTAYCPADTIDSHINKVLFEKIV

Salvia divinorum (Maria pastora) (Diviner's sage)

FUNCTION: Involved in the biosynthesis of clerodane diterpenoids natural products, including salvinorin A with potent agonistic activity on brain kappa-opioid receptors, thus conferring hallucinogenic properties (PubMed:30468448). Diterpene synthase that catalyzes the formation of (-)-kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP) as the first reaction in salvinorin A biosynthesis (PubMed:27865008, PubMed:28204567). {ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567, ECO:0000303|PubMed:30468448}.

5.5.1.28

CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl diphosphate; Xref=Rhea:RHEA:54684, ChEBI:CHEBI:58756, ChEBI:CHEBI:138310; EC=5.5.1.28; Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54685; Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28204567};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for geranylgeranyl diphosphate {ECO:0000269|PubMed:28204567}; Note=kcat is 0.88 sec(-1) with geranylgeranyl diphosphate as substrate. {ECO:0000269|PubMed:28204567};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:28204567};

Chloroplast;Isomerase;Magnesium;Metal-binding;Plastid;Transit peptide

diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]

chloroplast [GO:0009507]

isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity through binding to Mg(2+). {ECO:0000305|PubMed:28204567}.

IPR008949;IPR001906;IPR036965;IPR008930;

1.50.10.160;1.10.600.10;1.50.10.130;

A0A1S6M251

MRVRRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNMRTIGAQVYEQVVRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDTIHELFSKDPAIKLGGHWKPSDCVPRWKVAILIPFRNRHEHLPVLLRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLVFHDVDHIPENDRNYYGCGQMPRHFATKLDKYMYLLPYNEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPYHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVTEY

Sus scrofa (Pig)

FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (By similarity). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity). Plays a role in the glycosylation of BMPR1A and regulation of its protein stability (By similarity). Essential for extraembryonic development during early embryogenesis (By similarity). {ECO:0000250|UniProtKB:Q9JMK0}.; FUNCTION: (Microbial infection) May play a role in the glycosylation of porcine reproductive and respiratory syndrome virus GP5 protein and may be involved in the regulation of viral proliferation. {ECO:0000269|PubMed:29546034}.

2.4.1.-; 2.4.1.274

CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.274; Evidence={ECO:0000250|UniProtKB:Q9JMK0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496; Evidence={ECO:0000250|UniProtKB:Q9JMK0};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBX8};

PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Sphingolipid metabolism.

Disulfide bond;Glycoprotein;Glycosyltransferase;Golgi apparatus;Lipid biosynthesis;Lipid metabolism;Manganese;Membrane;Metal-binding;Reference proteome;Signal-anchor;Sphingolipid metabolism;Transferase;Transmembrane;Transmembrane helix

carbohydrate metabolic process [GO:0005975]; central nervous system myelination [GO:0022010]; central nervous system neuron axonogenesis [GO:0021955]; ganglioside biosynthetic process via lactosylceramide [GO:0010706]; glycoprotein biosynthetic process [GO:0009101]; glycosylation [GO:0070085]; neuron maturation [GO:0042551]; positive regulation of embryonic development [GO:0040019]; protein glycosylation [GO:0006486]; regulation of protein stability [GO:0031647]

Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]

metal ion binding [GO:0046872]; UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity [GO:0008489]

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000269|PubMed:29546034}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.

IPR003859;IPR027791;IPR027995;IPR029044;

A0A1S7LCW6

MKLKGTTIVALGMLVVAIMVLASMIDLPGSDMSATPAPPDTPRGAPIVGGQGQAMGLPVAMQRRRGEQRAPVPALSDANGGFVAPNVQFSEAHWQGMEALPLSIELKRKLKLPLDLEGLLIDETSLNAAVSGLLAGDVLVAINGRKVKTLKKMQKETRRVQMDRRASLTVYRKGRLLTLTLSEEKNLGLAQVETAPMILPGDIMPHPYRGPCTQCHAIGTTGHITPDPDGIVLPPGPIRAGAKMPHRDRGPCAACHAIIQ

Magnetococcus massalia (strain MO-1)

FUNCTION: Oxidizes Fe(2+) at alkaline pH; successively forms ferrihydrite (Fe(3+)(2)O(3) 0.5 H(2)O) then magnetite (Fe(3)O(4)) from an Fe(2+) solution. {ECO:0000269|PubMed:24097349}.

1.-.-.-

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:24097349}; Note=Binds 2 heme groups via the magnetochrome (MCR) motifs. {ECO:0000269|PubMed:24097349};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for oxidation of Fe(2+). {ECO:0000269|PubMed:24097349};

3D-structure;Biomineralization;Cell inner membrane;Cell membrane;Heme;Iron;Membrane;Metal-binding;Oxidoreductase;Transmembrane;Transmembrane helix

plasma membrane [GO:0005886]

metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]

SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q2W8Q1}; Single-pass membrane protein {ECO:0000305|PubMed:24097349}. Note=Not seen in magnetosome membranes. {ECO:0000250|UniProtKB:Q2W8Q1}.

PTM: Subject to proteolytic cleavage which requires both MamE and MamO. {ECO:0000250|UniProtKB:Q2W8Q1}.

DOMAIN: The dimer forms a pocket of about 8 X 15 Angstroms, lined with acidic residues, which may bind 2 Fe(2+) ions. {ECO:0000269|PubMed:24097349}.

IPR040963;IPR001478;IPR036034;

2.30.42.60;

A0A1U8QK63

MALEEVPSVSRDLDHSALRALSSASPSSLPSSCSRSTTSLLFQSKGIEFRLSIPDTFLSLVEPHRNAFLASYSTQGNTQSPLELALSFLYFLLDQKVSPLVLSSVLRAFNLEFLGNRSEIHSLIADLTPIPKQRQRWLGIYYRFLEASDDKRAEIPLSSIFQHARTNEFQLMAVFGGQGECSRTCLNEFAELYSSYEPMLRRLVGVIGPCLYNLSTSDEYSSYYRNQPLDLKAWITDENHVPDLGFVASAPVSVPVIGALSLARYCVTCHITGCNPGLMRSMLRTATGHSQGLLAAIVVAVSHSWDSFYQATEEVIELLFRLGWECHHAAPCSMVPAANYADVDGANGPSYMLSLRGLKRQETEATIDHVNASLPEDKRLYLALINAYDQFVVAGPVASLLRLESHLVEITSKDIDQSRIPFRDRKPYIQHSFLPVSTPFHTPYLTRAAARVKKQFAARPIPTRRLAIPVYHTHTGLDLRKQGGCALSIAIDAIASEPCNWPCAVASYHASHILTFDRGGLAPLIKRVREGCGVRVVQVADLDTRDSEMATMRDLFATKLLPTSTKLQSWGQQFRPGLASGPKIQLETRLNRVLGAPPIMVAGMTPTTVHPDFVAAIMNAGYHAELAGGGYHNASAMEAAIYDLVSSIPKERGITCNLIYANPRSISWQIELLRRLSNGNVRIDGLTIGAGVPSLTVASEYIETLGLRHISFKPGSVAAIRKVVEIAREHPDFPVILQWTGGRGGGHHSFEDFHAPIIATYGIIRQEPNVYLVAGSGFGDSDSVYPYLTGSWSVAMGHPAMPFDGILLGSRMMVAKEAHTSPAVRRIIAATPGVSDSEWEKTYSGPAGGVITVTSEMGEPIHKIATRGVCLWADLDKTVFSLSRRDRLTYLAQHRRSIIQRLNADFAKPWFGCNSDGEAVDLEDMTYLEVLKRLTALMFVPNKQWIDASYIEFTMTIAQRWLQRLQFDSEAAASLTISLLRKAPDRFLAIFADVCPTAEGDLLNPEDISFFLMQCKTPGRKPVNFIPALDDDFEFYFKKDSLWQAEDVDAVLDQDAERVCILHGPIAARYSKSDSEPAGYILDSILNGVVARLRETSTAEMLLPKLERGHTTPASWSTLSLTERDTSEETSDTSITSLSELIENHSFSSGGVDSVPRPSHPLWMRALLEDDVVLQGTLRQKNPFRDLIQSSPNTVVNYNQDSSELMVTAQEPYHISSFMRAVCHDGVMDKRNERIKSFYSLLWFGHDCDTSQSLNGVFYGPDITLTEDLLDEYNATIGPAYSDHRQMVPSTDVLPISMGIIIAWDVISRPLILRQIGGDLLRLVHRSNTFEYYSDTRLRLGDSVSSRSEVQAVYDDDGGRVVIVEAQILRSRVPVMTVTSTFLFRGSKGTTVPAFRRAREQKWTYDVTSEFEESILLSRNWFRPCDPSLTLVGKSMIFDLNSLVKYHDDGNMELHVQGTAMSQTNGQQQKLAIVDFRNTCTGNPVLDFLQRRGKLAEPRTEFKIPGWAGKSTMDIQMPPSNEPYAQLSKDFNPIHTSPIFSSLAGVPGTLCHGMCTSAIAERVLEHLGLGGDRERLRRFEARFTDMVMPLEKLVVEIKHTGMVDGRMCFSILAKRKETDERVLEGDAEVEQPRTAYLFTGQGSQSKGMGMDLYKTSTGQFLLTNKGGLFWTSCKTTQSPLPIRQKYLDITTEVVLPNGKRVQKPVFPGLTPTSTSYTFRHPRGLLYSTQFAQPAILLFEAAAFAELRAKGYVSHGAVYAGHSLGEFGALSALSRSVPTGALVELAFYRGSVMQASVASDNDGGTTYGMVAMNPKRVGTFFTQTTLDRLVSQIAAQSQELLEIVNFNIEGEQYVCSGTIDRPISGGTWPSLSG

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

FUNCTION: Fatty acid synthase beta subunit; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then transferred directly from the FAS to the SAT domain of the non-reducing polyketide synthase pkiA (PubMed:22510154). PkiA condenses the decanoyyl starter unit with 4 malonyl-CoA units and performs one methylation step to yield 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). {ECO:0000269|PubMed:22510154}.

1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; Evidence={ECO:0000250|UniProtKB:P07149}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000250|UniProtKB:P07149}; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000250|UniProtKB:P07149}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000250|UniProtKB:P07149}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; Evidence={ECO:0000250|UniProtKB:P07149}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000250|UniProtKB:P07149};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:22510154}.

Hydrolase;Lyase;Multifunctional enzyme;NAD;NADP;Oxidoreductase;Reference proteome;Transferase

long-chain fatty acid biosynthetic process [GO:0042759]

fatty acid synthase complex [GO:0005835]

(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; fatty-acyl-CoA synthase activity [GO:0004321]

IPR001227;IPR014043;IPR016035;IPR013785;IPR016452;IPR013565;IPR003965;IPR029069;IPR039569;IPR002539;IPR032088;

1.20.1050.120;1.20.930.70;3.30.1120.100;3.30.70.3320;6.10.60.10;3.20.20.70;3.10.129.10;3.40.366.10;

A0A1U8QLG8

MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEGAKNRTALLHMLRLKTDDMKIKQEAVCILDNAGSLDYTREVLYGLDRKARSLLREFKTPNPFMEALLDAMLSSLQACH

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable). {ECO:0000269|PubMed:22506079, ECO:0000269|PubMed:27098256, ECO:0000305|PubMed:22506079}.

2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29

CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:22506079}.

Isoprene biosynthesis;Magnesium;Metal-binding;Reference proteome;Transferase

alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; terpenoid biosynthetic process [GO:0016114]; ubiquinone biosynthetic process [GO:0006744]

mitochondrion [GO:0005739]; transferase complex [GO:1990234]

dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659]

IPR008949;IPR000092;IPR033749;

1.10.600.10;

A0A1U8QNG8

MDALLPRSSPQLKFYLNGTPISLTSPHPRWTLLDFIRSQDGLKGTKLGCGEGGCGALSGKHVITIEGLGTVDHPHPLQERIAQLHGSQCGFCTPGIVMSLYAMIRNAYDPVTGKFQLSADDIESKGHLDGNLCRCTGYKPILNAARTFIEDDLGSVPSIVESELVGTEEETESDMGAHSGSGDTGSRSSGSCGRPGGCCKDSPGISSCSSRETDMTTPSLPDSPVLKQYDFIPYTPTTELIYPPGLAKFVPELLCYGDAEQAWVKPRSVQEALEILSQCPSATLVTGASEVQVDVRFKDFRPSVSVFVGDITEMTGISWSEDMKTLYIGGSASLSDIEAECLRCIPLLKAVNLGSESVLSAIARTLRYFAGRQIRNAACLAGNIATASPISDMNPLLLAVGATVHARTSAEETTIPMSEMFKGYRKTALPSGSLITKIAVPMPSKDQIEIVNAYKQAKRKDDDIAIVTAAFRVRIAPGPDYTVQEASLAFGGMAPTTVLAHKTASALEGKRWGDEAVLDIVLTSLGEEFNLPYSVPGGMATYRRTLTLSLFVRFWNYVNQKLGLEYDSDLIEEIHRGISTGTRDDDNPHAQRVVGQQIPHLSGLKHATGEAEYVDDMPPLHRELHGALVLSERAHAKILSVNWTPALERGAVGYVDHTSLPEEKNHWGPVVHDEPVFAKGEVHAHGQPIGLVYADDAMTAQIAAKAVIVTYEDLPAILTIDEAIEARSFFNYGKELRRGAPPEEIRKELDDCEYTLSGTTKIGGQEHFYLETNAAIAVPHTEDGSMDVWSSTQNTMETQDFLSQVTNVPRHKINARVRRMGGAFGGKESRSVPIACIVAVAAKKARRPVRIMLNRDEDMMTSGQRHPVQCRWKVGFNREGKLLVLDADTYNNAGYSVDMSAAVMDRCLTHIENCYYIPNVWLRGWVCKTNTHSNTAFRGFGAPQAMYITESIISAVAEKVGIDVDEIRRRNLYQVGQRTPFNQVLDEDWHVPLLLEQVREEADYDARKKEIERFNSEHRWRKRGIALIPTKFGISFATALHLNQASAAVRVYTDGSVLLNHGGTEMGQGLYTKMVQVAAQELRVPVDQVYTQDTSSYQTANASPTAASSGSDLNGMAIKHACDQINERLRPYREKYGEDADLGTIAKAAYRDRVNLSAAGYYKMPTIGYEWGNYSENVKPMYFYFTQRQGVACTEVELDLLTGTHTVLRADLKMDIGRSINPAIDYGQIEGAFVQGQGLFTMEESLWTRSGQLATRGPGTYKIPGFADIPQVFNSSKGIGEPPLFMGSSVLFALRDALSHARRERGVSEPLVLDSPATVERLRLAVGDDLVHRAQVQRKDGEQGFFVAVA

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

FUNCTION: Nicotinate hydroxylase, part of the hnx cluster involved in the purine degradation (PubMed:4581274). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:4581274). HnxS accepts also hypoxanthine, but not xanthine, as a substrate (PubMed:29212709, PubMed:363427, PubMed:4581274). The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid (PubMed:4581274). {ECO:0000269|PubMed:29212709, ECO:0000269|PubMed:363427, ECO:0000269|PubMed:4581274}.

1.-.-.-

COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P80457}; Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250|UniProtKB:P80457}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P80457}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:P80457}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250|UniProtKB:P80457};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90.4 uM for hypoxanthine {ECO:0000269|PubMed:363427}; KM=36.15 uM for 2-hydroxypurine {ECO:0000269|PubMed:363427}; KM=524.5 uM for 6,8-dihydroxypurine {ECO:0000269|PubMed:363427}; KM=188.6 uM for nicotinate {ECO:0000269|PubMed:363427};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. {ECO:0000269|PubMed:363427};

2Fe-2S;FAD;Flavoprotein;Iron;Iron-sulfur;Metal-binding;Molybdenum;Oxidoreductase;Reference proteome

2 iron, 2 sulfur cluster binding [GO:0051537]; FAD binding [GO:0071949]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; xanthine dehydrogenase activity [GO:0004854]

IPR002888;IPR036884;IPR036010;IPR000674;IPR036856;IPR016208;IPR008274;IPR046867;IPR037165;IPR012675;IPR005107;IPR036683;IPR016166;IPR036318;IPR016167;IPR016169;IPR002346;

3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10;

A0A1U9X797

MWLTWPFCFLTITLREEGVCHLESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW

Homo sapiens (Human)

FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly. {ECO:0000256|HAMAP-Rule:MF_03130}.

2.3.1.108

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-acetyl-L-lysyl-[alpha-tubulin]; Xref=Rhea:RHEA:15277, Rhea:RHEA-COMP:11278, Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.108; Evidence={ECO:0000256|HAMAP-Rule:MF_03130};

Acetylation;Acyltransferase;Cell junction;Cell projection;Coated pit;Cytoplasm;Cytoskeleton;Membrane;Signal;Transferase

neuron development [GO:0048666]; regulation of microtubule cytoskeleton organization [GO:0070507]

axon [GO:0030424]; clathrin-coated pit [GO:0005905]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; spindle [GO:0005819]

tubulin N-acetyltransferase activity [GO:0019799]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03130}. Membrane, clathrin-coated pit {ECO:0000256|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion {ECO:0000256|HAMAP-Rule:MF_03130}. Cell projection, axon {ECO:0000256|HAMAP-Rule:MF_03130}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03130}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03130}.

PTM: Autoacetylation strongly increases tubulin acetylation. {ECO:0000256|HAMAP-Rule:MF_03130}.

IPR038746;IPR007965;

3.40.630.30;

A0A1V0E492

MACVSDLVAFTQPLIIGAKPLEIVRRSAAFHPNVWGDYFLKLSQDEKKLESMRERAKVLKEKVLKKLSTIEGGERLELIDTLYHLGVAYNFEKEIEEALEKIYKAYDEDATQDNLCTLALRFRLLRQHGWNASSDVFNKFKETKNGNFKESVASDVLGMLSLYEASYVGTKEDKILEEAISFTTRNLSAALPNMEPLLAERVAHSLELPLHKRLQRLEARYFITMYEKNNAHDEMLLEYAKLDYNLLQALHQNEMKELTKWWTKIDLVGKMKFPRDRVTECYFWPLGAFFEPQHSRGRIFATKITQLTSIIDDLYDVYGTQEELQLFTDVIQRWDMNAKKSLPDYIKPLYEALLSTLKDFEEELSLEGNAYRASFMQQAMKNICMAYFDEAKWYNRGTTPKVEEYLNSAEISCGYPVVATACFTGAGEITTKKLLEWIQSQPKYMKDTCRLCRIVDDIKTYKFEEERGHVASVVACYMEEHKCNEDEALEKLNEDVMNTWKDINKACMRPTPFPMVVMNIIRNLSRVMEILYQFGDGYTFADTVTKERLNLLLKDPIPV

Piper nigrum (Black pepper)

FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-caryophyllene and, as a minor compound, into alpha-humulene (PubMed:29248443). {ECO:0000269|PubMed:29248443}.

4.2.3.104; 4.2.3.57

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:29248443};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.455 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}.

Lyase;Magnesium;Metal-binding

beta-caryophyllene biosynthetic process [GO:1901937]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762]

alpha-humulene synthase activity [GO:0080017]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:Q40577}.

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR005630;IPR008930;IPR019734;

1.10.600.10;1.50.10.130;

A0A1V0E4A6

MDAVSCAINALSAQAPPKHLGGNNVGRKSVTFPKDIWGDYFLKISPNEEKLDSWRVRAKELKEKVFDILSCAKGAEQVHIIDALYHLGVSYQFEKEIEEALKNMLTTYNDDTSTEDDLYTLALRFRLLRQNGFHASTKALNKFKDAHGSFREDLASDVMGLLSLYEASYAGTVDDLILDEALAFTKIHLKAALPHLDSHLAQRVSHSLELPLHKRIQRLEAREFISLCEKDDSIVIKELLEFAKLDYNILQALHQWELKELTKWWKKLNLVGKMTFARDRMTEIYFYVSGFFFEPQYSRGRIISSKILAICSVVDDEYDVYGTLDELQVFTDAICRLDVAAMENLPEYVKPLYEAIFFSLKEFEEELAREGNAYRVNYLREEVKNLCKSYLQETKWLHQRYIPTLEEYLLVSEISSTYTVIFNGCFVGCGEIATKEVFEWFQAFPKLLSDSARIGRIADDIMSCKFEQSRGHCPSAVECCMEEHQCTKEVALGNLDGVLGRAWKDMNKACMRPTPFPMEVLRPIVNLARMAEISYQYEDGYTFSGGKTKERISMLYKDPIPV

Piper nigrum (Black pepper)

FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-cadinene, delta-cadinene and delta-cadinol (PubMed:29248443). {ECO:0000269|PubMed:29248443}.

4.2.3.-

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate; Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-cadinene + diphosphate; Xref=Rhea:RHEA:69444, ChEBI:CHEBI:33019, ChEBI:CHEBI:80749, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69445; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = (-)-delta-cadinol + diphosphate; Xref=Rhea:RHEA:69448, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:156223, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69449; Evidence={ECO:0000269|PubMed:29248443};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.4 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.694 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}.

Lyase;Magnesium;Metal-binding

cadinene biosynthetic process [GO:1901928]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762]

(+)-delta-cadinene synthase activity [GO:0047461]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:Q40577}.

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR005630;IPR008930;

1.10.600.10;1.50.10.130;

A0A1W2Q5Z7

MVNMRKRTLKYLTFFLLFIFLTSFVLNYSNSGVPSAWFPKQMVLEFSENFRKFIKSQPCTCRHCISQGKVSYWFDQRFNKTMQPLLTAHNALMEEDTYRWWLRLQRERKPNNLSDTVKELFRLVPGNVDPMLNKRLVGCRRCAVVGNSGNLKDSSYGPEIDSHDFVLRMNRAPTVGFEADVGSRTTHHLVYPESFRELGENVNMVLVPFKITDLQWVISATTTGTITHTYVPVPPKIKVKQEKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSIHICDEVWTYMALGQTAKEIGTITGRTTHQQVHSERRGFMMATSSTMSQLPWQPSTKSASSRGDDAAT

Rattus norvegicus (Rat)

2.4.3.2; 2.4.3.4

CATALYTIC ACTIVITY: Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+); Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153; Evidence={ECO:0000256|ARBA:ARBA00036879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249; Evidence={ECO:0000256|ARBA:ARBA00036879}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.3.4; Evidence={ECO:0000256|ARBA:ARBA00036292}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617; Evidence={ECO:0000256|ARBA:ARBA00036292}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GM1b (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:47560, ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78568; Evidence={ECO:0000256|ARBA:ARBA00043673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561; Evidence={ECO:0000256|ARBA:ARBA00043673}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 + CMP-N-acetyl-beta-neuraminate = a ganglioside GM1b + CMP + H(+); Xref=Rhea:RHEA:48244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:88069, ChEBI:CHEBI:90151; Evidence={ECO:0000256|ARBA:ARBA00043816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245; Evidence={ECO:0000256|ARBA:ARBA00043816}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD1a (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:18021, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.3.2; Evidence={ECO:0000256|ARBA:ARBA00043773}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022; Evidence={ECO:0000256|ARBA:ARBA00043773};

PATHWAY: Glycolipid biosynthesis. {ECO:0000256|ARBA:ARBA00004934}.; PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922}.

Glycoprotein;Golgi apparatus;Membrane;Proteomics identification;Reference proteome;Secreted;Signal-anchor;Transferase;Transmembrane;Transmembrane helix

ganglioside biosynthetic process via lactosylceramide [GO:0010706]; memory B cell differentiation [GO:0002319]; negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process [GO:1905403]; protein glycosylation [GO:0006486]; sialylation [GO:0097503]

extracellular region [GO:0005576]; Golgi medial cisterna membrane [GO:1990675]; Golgi trans cisterna membrane [GO:1990676]; membrane [GO:0016020]; trans-Golgi network membrane [GO:0032588]

beta-galactoside (CMP) alpha-2,3-sialyltransferase activity [GO:0003836]

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Secreted {ECO:0000256|ARBA:ARBA00004613}.

IPR001675;IPR038578;IPR012163;

3.90.1480.20;

A0A1W2Q671

MATDSGEPASTEDSEKPDGVSFQSRVARAVAPLTVEARIKEKYSTFSASGETIERKRFFRKSVEMTEDDKVAQSSRRDERKVATNISRVEKVPTNVLRGGQEVKYEQCSKATSESSKDCFKEKTEKEMEEEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESILKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAEDTGLRVELAEEDDCSNSSLALRLWVEDPKKLKGKHKDNEAIEFSFNLEADTPEEVAYEMVKSGFFHESDSKAVAKSIRDRVTLIKKIREKKPAGCLEERRDSQCKHARNVNPQQQTATLRPAPGPHNAAECEETEVDQHVRQQLVQGKAQQQPSSVRGDTSSEPAAGPVLHSDTSSHPTVAYSSNQATSSQLQEQPKLTRSPVLPVVQGQSSVMPIYAAGPAVASQSQISPLTIQKVSQIKPVSQPIGAEQQATPPNPDFVRSLNQDVTSVKENTNSPDTPSGNGKQDRIKQRRASCPRPEKGTKFQLTVLQVSVSGDNMVECQLETHNNKMVTFKFDVDGDAPEDIADYMVEDNFVLENEKEKFVEELRAIVGQAQEILHVHSAAEKSIGVDSVALESNSNQTGSSEQVLINSASTQTSNESAPQSSPVGRWRFCINQTIKNREAQSPPSLQPSVAMVPGLHPFPNNTSNQEISQDTLFTVPGHHVVFTSKLDGKIGERASVETEQTSVPYQAEDDKLKAPATDTSNYSATLVCPDPAGCEALTSQAGMFIPTYPCQQAAVPADVLMSHPGESVQIGSNAVVTSVLVSSDQKPQSLSVQQPTIDAEFISQEGETTVNSETSSPKAVGATQTPGFEPTVLLPATILESDGERPPKMEFTDNRIKTLDEKLRNLLYQEHSISTICPESQKDTQSIDSPFSSSAEDILSSPMPEVIAISHCGIQDSQAQSPNFQPTGSKILSNVAASQPAHIPVLKRDLNVITSVPSELCLHEMSPDASLPGDPEAYPAAVSSDGTIHLQTGGGYFGLSFTCPSLKNPISRKSWTRKLKSWAYRLRQSTSFFKRSKVRQVETEDKRSAIASDPIPLTREFSADTRALSRCKAMSGSFQRGRFQVITVPQQQPVKMMSFGKEHRPPSKKTTAQSNEQALTFTEAAVTQLIEVEPAIPTHKASVSSQKLRTLYETFKEDKGDPEQGDILSLSTARETSVSSVTTEKNVEETSTTGISVQSGSEMLDKEKDESTPGKQTCTNEFSATPAGSGKSVAKAAPKSGQHLPARAQTQSSLFYSPSSPMSSDNESEIEDEDLKAELQRLREKHIQEVVSLQTQQNKELQELYERLRATKDSKAQSSEVPMPPASPRRPRSFKSKLRSRPQSLTHSDNLVVVKDVQRAESNTAPRQQSPASKKGMFTDDLHKLVDDWTRETVGNFPSKPSLNQLKQSQQKSEAENWNKLHESTPSTVGYTSTWISSLSQIRGAAPSSLPHGLPLPSFPGPLASYGMPHACQYNPVGAASYPVQWVGISGAAQQSVVLPTQSGGLFQPGMNLQSFPAPPVQNPPSIPPGPK

Rattus norvegicus (Rat)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Transferase

cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; intracellular signal transduction [GO:0035556]; maintenance of blood-brain barrier [GO:0035633]; monoatomic ion homeostasis [GO:0050801]; negative regulation of apoptotic process [GO:0043066]; negative regulation of pancreatic juice secretion [GO:0090188]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of sodium ion transport [GO:0010766]; non-membrane-bounded organelle assembly [GO:0140694]; osmosensory signaling pathway [GO:0007231]; phosphorylation [GO:0016310]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of potassium ion import across plasma membrane [GO:1903288]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of sodium ion transport [GO:0010765]; protein localization to plasma membrane [GO:0072659]; regulation of calcium ion import [GO:0090279]; regulation of monoatomic cation transmembrane transport [GO:1904062]

adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]

ATP binding [GO:0005524]; molecular condensate scaffold activity [GO:0140693]; potassium channel inhibitor activity [GO:0019870]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR024678;IPR000719;IPR008271;

1.10.510.10;

A0A1W2Q672

MPRVGPGGAHWRPALALALLGLAATLGASPTSGQRWPVPYKRFSFRPKTDPFCQAKYTFCPTGSPIPVMKDNDVIEVLRLQAPVWEFKYGDLLGHFVRMHLDLKIMHDAIGFRSTLTGKNYTVEWYELFQLGNCTFPHLRPEVNAPFWCNQGAACFFEGIYDKHWKENGTLSLVATVSGNTFNKVAEWVKQDNETGIYYETWTVRASPGKGAQTWFESYDCSNFVLRTYEKLAEFGTDFKKIETNYTKIFLYSGEPIYLGNETSIFGPKGNKTLALAIKKFYGPFKRYSSTKDFLLNFLKIFDTVIMHREFYLFYNFEYWFLPMKPPFVKITYEETPLPTQHTTFTDL

Rattus norvegicus (Rat)

FUNCTION: Exhibits palmitoyl protein thioesterase (S-depalmitoylation) activity in vitro and most likely plays a role in protein S-depalmitoylation. {ECO:0000256|ARBA:ARBA00044494}.

3.1.2.22

CATALYTIC ACTIVITY: Reaction=2 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77599, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152, ChEBI:CHEBI:197411; Evidence={ECO:0000256|ARBA:ARBA00044481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77600; Evidence={ECO:0000256|ARBA:ARBA00044481}; CATALYTIC ACTIVITY: Reaction=2 3-hexadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-hexadecanoyl-sn-glycero-1-phospho-(3'-hexadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77607, ChEBI:CHEBI:44859, ChEBI:CHEBI:197411, ChEBI:CHEBI:197415; Evidence={ECO:0000256|ARBA:ARBA00044455}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77608; Evidence={ECO:0000256|ARBA:ARBA00044455}; CATALYTIC ACTIVITY: Reaction=2 3-octadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-octadecanoyl-sn-glycero-1-phospho-(3'-octadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77603, ChEBI:CHEBI:197411, ChEBI:CHEBI:197412, ChEBI:CHEBI:197414; Evidence={ECO:0000256|ARBA:ARBA00044460}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77604; Evidence={ECO:0000256|ARBA:ARBA00044460}; CATALYTIC ACTIVITY: Reaction=2 3-tetradecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-tetradecanoyl-sn-glycero-1-phospho-(3'-tetradecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77611, ChEBI:CHEBI:197411, ChEBI:CHEBI:197413, ChEBI:CHEBI:197416; Evidence={ECO:0000256|ARBA:ARBA00044453}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77612; Evidence={ECO:0000256|ARBA:ARBA00044453}; CATALYTIC ACTIVITY: Reaction=2 a 3-acyl-sn-glycero-1-phospho-(1'-sn-glycerol) = a 3-acyl-sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77619, ChEBI:CHEBI:77717, ChEBI:CHEBI:197411, ChEBI:CHEBI:197425; Evidence={ECO:0000256|ARBA:ARBA00044472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77620; Evidence={ECO:0000256|ARBA:ARBA00044472}; CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000256|ARBA:ARBA00037021}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000256|ARBA:ARBA00037021};

Glycoprotein;Reference proteome;Signal

brain development [GO:0007420]; glycosylation [GO:0070085]; lysosomal lumen acidification [GO:0007042]; lysosome organization [GO:0007040]; neurogenesis [GO:0022008]; retrograde transport, endosome to Golgi [GO:0042147]; signal peptide processing [GO:0006465]; visual perception [GO:0007601]

cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; vacuolar lumen [GO:0005775]

bis(monoacylglycero)phosphate synthase activity [GO:0160121]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; mannose binding [GO:0005537]

IPR026138;

A0A1W5BM90

MVRSKYFTKAQEFDGMPKLTDFKIIDEEIDDNLKEGEVVGEALCASVDPFIRAYPVPPGAPIIGFQVLKVTKSMNKKYPVGCKVMGFSGWRTICKLSDADVWYKVNEGQNPTVSLGALGMPGMTAYCGFLDICKPQAGETVMVNGCAGAVGNLVGQIAKIKGCKVIGCCGSDEKVKFAKSLGFDQVFNYKTCKFYPKTLKELAPDGIDCFFDNVGGQLSSDIMGCMNKGGRIAVCGAITSYNSKQPPMATMVQGLMVFKLLTMRGFLVQQYKDKFPEALVEMQQWIKEGKIKIHETPSSGFENIPRSFIDMLSGGNIGKAVVVMS

Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)

1.3.1.48; 1.3.1.74

CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213; Evidence={ECO:0000256|ARBA:ARBA00023498}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374, ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590; Evidence={ECO:0000256|ARBA:ARBA00023548}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133408; Evidence={ECO:0000256|ARBA:ARBA00023544}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586; Evidence={ECO:0000256|ARBA:ARBA00023544}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:79072, ChEBI:CHEBI:133411; Evidence={ECO:0000256|ARBA:ARBA00023543}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594; Evidence={ECO:0000256|ARBA:ARBA00023543}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208, ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133346; Evidence={ECO:0000256|ARBA:ARBA00023517}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209; Evidence={ECO:0000256|ARBA:ARBA00023517}; CATALYTIC ACTIVITY: Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112; Evidence={ECO:0000256|ARBA:ARBA00023553}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738; Evidence={ECO:0000256|ARBA:ARBA00023553}; CATALYTIC ACTIVITY: Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974; Evidence={ECO:0000256|ARBA:ARBA00023496}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205; Evidence={ECO:0000256|ARBA:ARBA00023496}; CATALYTIC ACTIVITY: Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; Evidence={ECO:0000256|ARBA:ARBA00023696}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618; Evidence={ECO:0000256|ARBA:ARBA00023696}; CATALYTIC ACTIVITY: Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH; Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748; Evidence={ECO:0000256|ARBA:ARBA00023504}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782; Evidence={ECO:0000256|ARBA:ARBA00023504}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276; Evidence={ECO:0000256|ARBA:ARBA00024160}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790; Evidence={ECO:0000256|ARBA:ARBA00024160}; CATALYTIC ACTIVITY: Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74; Evidence={ECO:0000256|ARBA:ARBA00023507}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739; Evidence={ECO:0000256|ARBA:ARBA00023507}; CATALYTIC ACTIVITY: Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH; Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455; Evidence={ECO:0000256|ARBA:ARBA00023691}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614; Evidence={ECO:0000256|ARBA:ARBA00023691}; CATALYTIC ACTIVITY: Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH; Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741; Evidence={ECO:0000256|ARBA:ARBA00023530}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786; Evidence={ECO:0000256|ARBA:ARBA00023530}; CATALYTIC ACTIVITY: Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00034052}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778; Evidence={ECO:0000256|ARBA:ARBA00034052}; CATALYTIC ACTIVITY: Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309; Evidence={ECO:0000256|ARBA:ARBA00023545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609; Evidence={ECO:0000256|ARBA:ARBA00023545};

Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome

prostaglandin metabolic process [GO:0006693]

cytoplasm [GO:0005737]

13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)+] activity [GO:0032440]

IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;

3.90.180.10;3.40.50.720;

A0A1W6QDI7

MSLAFNLRVIPFSGHTIQSRRGLFPVHESPMITTKPFAAVKCSLTTSTDLMGKIKEKFNGKVHTSLPAITTHSADTPSNLCIIDTLQRLGVDRYFQSEIDSILDDTYRLWQLKKEDIFSDITTHAMAFRLLRVKGYQVSSEELAPYADQEHVNLQEIDVPTVIELYRAAQERVTEEDSTLKKLYVWTSTFLKQQLLTDAIPDKKLHEQVDYYLKNYHGILDRMGVRRSLDLYDVGHYKTLKAADGFSNLCNEDFLAFARQDFNISQAQHQKELQQLQRWYSDCRLDTLKFGRDVVRVSNFLTSAMSGDPELSDVRLAFAKHIVLVTRIDDFFDHGGSKEESYKILELVKEWKEKPAGEYGSEEVEILFTAVYNTVNELAEMAHIEQGRSVKDLLIKLWVEILSMFKIELDTWSDDTALTLDEYLSSSWVSIGCRICILISMQFLGVKLTDEMLLSEECTDLCRHVSMVDRLLNDVQTFEKERKENTGNSVSLLLAAHKDERAINEEEAITKAKDLAEYNRRKLMQIVYKTGTIFPRKCKDMFLKVCRIGCYLYSSGDEFTTPQQMMEDMKSLVYEPLTIHPPEANNVVGKKTELCQQLVKPYVCHTFCKKYTVSRPSNVMMTCYID

Isodon rubescens (Rabdosia rubescens)

FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities (PubMed:28381502, PubMed:28445526). Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to miltiradiene (PubMed:28381502, PubMed:28445526). {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}.

4.2.3.131

CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635, ChEBI:CHEBI:65037; EC=4.2.3.131; Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984; Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}.

Alternative splicing;Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide

gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946]; terpenoid biosynthetic process [GO:0016114]

chloroplast [GO:0009507]

magnesium ion binding [GO:0000287]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000305}.

IPR008949;IPR001906;IPR036965;IPR005630;IPR008930;

1.10.600.10;1.50.10.130;

A0A1W7HCY1

MSGHSFFEHLFEHSQHVTPYLHGAIKPRPERCAEHGFIHIEHASSDHIRALYESLKLAHPEAGAAYWLTRTWTLLCWQPLYVAFIAIYSCQGLPKLSSMGQHVQPRFVSGYQFDDDEYRQGSEQELIAHAGKELCALFDYFRQEMSLWTRIRPGFTQHLFADGVFGCLVKLSQFYPTLSGDYFLEQARLWLAACQLPEKLIQSLRYDETSRQLSLVRTSCCLVYKCQGRELCRDCPRHPDNKRE

Vibrio vulnificus

FUNCTION: Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB (PubMed:28150143, PubMed:32681432). Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)-enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)-nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Catalyzes also reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor (PubMed:32681432). {ECO:0000269|PubMed:28150143, ECO:0000269|PubMed:32681432, ECO:0000305}.

1.16.1.10

CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:32681432}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15063; Evidence={ECO:0000269|PubMed:32681432}; CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:32681432}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28797; Evidence={ECO:0000269|PubMed:32681432};

COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P39405}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P39405};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=6.83 nmol/min/mg enzyme with Fe(3+)-aerobactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=2.32 nmol/min/mg enzyme with Fe(3+)-vulnibactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=1.44 nmol/min/mg enzyme with ferrioxamine B as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=1.1 nmol/min/mg enzyme with Fe(3+)-vibriobactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=10.98 nmol/min/mg enzyme with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor and glutathione (GSH) as electron donor (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=14.24 nmol/min/mg enzyme with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor and simultaneous presence of glutathione (GSH) and NADPH as electron donors (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:32681432};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor. {ECO:0000269|PubMed:32681432};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor. {ECO:0000269|PubMed:32681432};

2Fe-2S;Cytoplasm;Iron;Iron-sulfur;Metal-binding;NAD;NADP;Oxidoreductase

cellular response to iron ion starvation [GO:0010106]

cytoplasm [GO:0005737]

2 iron, 2 sulfur cluster binding [GO:0051537]; ferric-chelate reductase (NADH) activity [GO:0140618]; ferric-chelate reductase (NADPH) activity [GO:0052851]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28150143}.

IPR023998;IPR024726;

A0A1Y1IH42

MEPKSVIDGLGEEITAIVTPVSICMLVVVCLVHGLTPHGSDSGVSPFIATSFYHEKSTDSAETKLGGALLNALIFIVAVAAITFVLVALFYFRCTKVIWGYMGFSGFTILALLGGILGIQIIQAASIPLDIITFSIVLWNFSVVGVLAVFFWKMPIFLKQGYLVFIGAVVAFWFTKLPEWTTWTVLAAMALYDLAAVLAPGGPLKLLVEMSIERDEDIPALIYEARPTSLSRGEAMTGRGRQNESEAAPGRRRRQQRSGGADDGIEQLAVATRDSGASDPRPSSSSANGAQLSSTSNNNRAAGSGSQGLLAETNAPESQELTRLGAGTSSSRGQVRAEQSAVSGRLRGRRTGSERTANEGLPGSGSQGEIDEGESAPLVGGTQRGGAEGGEEEARSSGEGEDGLGYDEEEWGLPDAIKLGLGDFIFYSLLVGRAAMYDLMTVYACYLAIIAGLGATLVLLAVYRHALPALPISVALGMVFYFMTRIVVEPLVVGLATNLLFF

Klebsormidium nitens (Green alga) (Ulothrix nitens)

FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. {ECO:0000256|RuleBase:RU361148}.

3.4.23.-

Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Protease;Reference proteome;Transmembrane;Transmembrane helix

amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta metabolic process [GO:0050435]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485]

apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]

aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000256|RuleBase:RU361148}.

IPR001108;IPR006639;IPR042524;

1.10.472.100;

A0A1Y3DYH2

MNILQEPIDFLKKDELKNIDLSQMDKKERYKIWKRIPKCELHCHLDLCFSADFFLSCVRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFQDYEMIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKHNLDIELIHQAIVKGIKEVVELLDHKIDVTLLCIGDTGHRAADIKASADFCLKHKADFVGFDHGGHEVDLKPYKEIFDYVKEGGMHLTVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKENNILLEVCPISNVLLKNAKSFDTHPIRKLYDAGVKVSVSSDDPGMFLTNINDDYEKLYTHLHFTLEDFMKMNEWALEKSFIGCDIKEKIKKLYF

Plasmodium knowlesi

FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable). {ECO:0000269|PubMed:19728741, ECO:0000305|PubMed:19728741}.

3.5.4.31; 3.5.4.4

CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000269|PubMed:19728741};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=22 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 6.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.51 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741). {ECO:0000269|PubMed:19728741};

PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}.

Hydrolase;Metal-binding;Purine salvage;Zinc

adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166]

cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]

2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872]

IPR006650;IPR001365;IPR006330;IPR032466;

3.20.20.140;

A0A1Z5R261

MKPSPHFPEIGKKPKDLIAKDHAFNIAAYISSGADVIAAALRKHVEEEARDLSGEAFLRFMDQLYEQISSLLQSNDVTENLLALRAIDALIDMPFGEGASKVSKFASFLRNVFEVKRDPEILVPASAVLGHLAKAGGAMTADEVERQIKTALGWLTGDRVEYRRFAAVLILKEMAENGSTVFNVHVPEFVDAIWVALRDPKQAVREKAVEALRACLHVIEKRETRWRVQWYYRMCEAAQVGLGRNASVHSIHGSLLAVGELLRNTGEFMMSRYREVADIVLDYLKHRDQLVRRSITSLLPRIAHFLRDRFVTNYLKICMDHILFVLRTPDERASGFVALGEMAGALGVELVPYLPAITSHLQDAIAPRRGRPSLEAISCVGSFAKAMGPAMEPHIRSGLLDAMFFAGLSDKLVDALESISTSIPSLLPTIQERLLDCISQALPKSSIRPGASVGRANRSNSLQQFVDSNSPLLVQLALWTLANFNFKGHELLEFARESVILYLEDEDSSTRKAASLCCCKLVAHSLSASSTSQFGSNRTNRIGGAKRRRLVEEIVEKLLMAAVADADVGVRSSVFKALYRNPAFDDFLAQADILTSIFVALNDEEYDVRELAISVAGRLSEKNPAYVLPALRRYLIQLLTYLDQSMDSKCREESARLLGCLIRSCARLILPYIAPVHKALVTRLCEGTGPNANNALAAGVLATVGELAKVGGFAMRRYLPELMPVVVDALLDGGAVSKREVAVSTLGQIIQSTGYVIAPYNEYPPLLGLLLKLLNGELEWSTRLEVLKVLGIMGALDPHAHKRNQHNLPGQHREVLRPTIETAQHIVSMEELPTDFWPSFSASEDYYSTVAISSLMRILRDPSLSSYHQMVVGSLIFIFKSMGLGCVPYLPKVLPELLRAVRMCEDGGLKEFITWKLGTLISIVRQHIRKYLQDILSLISELWTSSFSLPAPNRTIQGPQGSPVLHLVEQLCLALNDEFRIYLLHILPSCIQVLGDAERCNDYYYVPGILHTLEVFGGNLDEHMHLVAPVLVRLFKVELVDIRRRAIVTLTNLIPKVQVGTHVSALVHHLKLVLDGNNDDLRKDAAEALCCLAHALGEDFTIFVPSIRKILVKHHLRYRKWDEIENRLLRRELLITENLSVQKYTQCPPDVISDPLDDFDGTPSEIADETQRQARSHQVNDVRLRSAGEASQRSTREDWAEWMRHFSIALLKESPSPALRTCARLAQLQPSVGRELFAAGFASCWAQMSESAQEQLVRSLKTAFSSQNIPPEILATLLNLAEFMEHDEKPLPIDTRLLGALAEKCRAFAKALHYKEMEFEAVCTKKMGANPVTVVESLIHINNQLHQHEAAIGILTYSQQNLEVQLKESWYEKLHRWDEALKAYTIKSSQAPGPLQNLDATLGRMRCLAALARWEDLSALCREQWTGAEPSARLEMAPMAANAAWHMGEWDHMAEYVSRLDDGDENKLRMLGNTTASGDGSSNGAFFRAVLSVRSKKYDEARIFVERARRCLATELAALVLESYERAYNNMVRVQQLSELEEVIDYCTLPAESPIADGRRELIRNMWNERIKGTKRNVEVWQALLAVRELVLPPNEDRDTWIKFAKLCWKNGRISQARSTLVKLLQFDPESSPELTLYHAHPQVALAYLKYQYAVGDELKRRDAFSRLQELSMQLATAMGNFPGTSANHGTMSNAGVPLIARVYLTLGTWKKALSPALDDDSIQEILISYNHATLSAKDWGKAWHTWALFNTEVMSRYTFRGRPDIAGKYVVAAVTGYFYSIACQSTTKGVDDSLQDILRLLTLWFNHGATSEVQTALQKGFSLVKIEMWLVVLPQIIARIHSNTRVVRELIQSLLVRIGKGHPQALMYPLLVACKSISILRQRAAQEVVDKIRQHSGGLVDQAQLVSKELIRVAILWHEMWHEALEEASRMYFGEHNIEGMLAVLEPLHAMLERGPETIKENAFIQAYGHELLEAHECCSKYRATGEDAELTKAWDLYYHVFRRIDKQLPSLTTLDLHSVSPELLKCRKLELAVPGTYAADSPLVTIEYFVPQLIVITSKQRPRKLTIHGSDGNDYAFLLKGHEDLRQDERVMQLFGLVNTLLENSRKTSEKDLSIQRYAVIPLSPNSGLIGWVPNCDTLHALIREYRDARKIFLNQEHKLMLAFAPDYDHLPLIAKVEVFQHALQNTEGNDLAKVLWLKSRTSEVWLERRTNYARSLAVMSMVGYLLGLGDRHPSNLMLDRYSGKILHIDFGDCFEASMNREKFPEKVPFRLTRMLVKAMEVSGIEGTFRTTCENVMQVLRTNRDSVMAMMEAFVHDPLINWRLFNFNEVPQVSNYGNAHAHTVVSSEDAVANRELMQPQRGARERELLQAVNQLGDANEVLNERAVAVMARMSDKLTGRDFSSGSALAGAGSSTQHGSEHLASGDARDAQPALSVKVQVQKLILQATSHENLCQNYVGWCPFW

Sorghum bicolor (Sorghum) (Sorghum vulgare)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775, ECO:0000256|RuleBase:RU364109};

ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase

dephosphorylation [GO:0016311]; embryo development ending in seed dormancy [GO:0009793]; gravitropism [GO:0009630]; negative regulation of defense response to virus [GO:0050687]; negative regulation of macroautophagy [GO:0016242]; phosphorylation [GO:0016310]; positive regulation of abscisic acid biosynthetic process [GO:0010116]; positive regulation of auxin mediated signaling pathway [GO:0010929]; positive regulation of brassinosteroid mediated signaling pathway [GO:1900459]; positive regulation of cell growth [GO:0030307]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of embryonic development [GO:0040019]; positive regulation of glucose mediated signaling pathway [GO:1902661]; positive regulation of rRNA processing [GO:2000234]; response to auxin [GO:0009733]; response to rapamycin [GO:1901355]; response to virus [GO:0009615]; rRNA transcription [GO:0009303]; sucrose mediated signaling [GO:0009745]; TOR signaling [GO:0031929]

cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribosome [GO:0005840]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; transcription cis-regulatory region binding [GO:0000976]

IPR011989;IPR016024;IPR003152;IPR009076;IPR036738;IPR011009;IPR024585;IPR000403;IPR036940;IPR018936;IPR003151;IPR014009;IPR026683;IPR011990;

1.20.120.150;1.25.10.10;1.10.1070.11;1.25.40.10;

A0A250YGJ5

MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVRQSSNVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFENARPTQTHMALVQLERVGLLHFVVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKTTGRLCTVAKARGLRACRGELRDTILDWEDALPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGKLVIVNLQPTKHDRHADLRIHGYVDDVMTQLMKHLGLEIPAWDGPRVLEKALPPLPRPPTPKLEPTDKSLAQLNGSVPADSKPEPCTWHNGSQPASPKREQPDSPAPRRPPKRVKAEVTPS

Castor canadensis (American beaver)

FUNCTION: NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (By similarity). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (By similarity). Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B (PubMed:31002797). Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing (By similarity). Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac (By similarity). SIRT6 participation to DSB repair is probably involved in extension of life span (PubMed:31002797). Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53 (By similarity). Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence (By similarity). Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage (By similarity). Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac (By similarity). Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism (By similarity). Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes (By similarity). Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect (By similarity). Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2) (By similarity). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5 (By similarity). Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA (By similarity). Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1 (By similarity). Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2 (By similarity). The defatty-acylase activity is specifically involved in regulation of protein secretion (By similarity). Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion (By similarity). Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170 (By similarity). Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7, ECO:0000269|PubMed:31002797}.

2.3.1.-; 2.3.1.286; 2.4.2.-

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:31002797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637; Evidence={ECO:0000269|PubMed:31002797}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-tetradecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70567, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:141129, ChEBI:CHEBI:189674; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70568; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-hexadecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70563, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14175, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:138936, ChEBI:CHEBI:189673; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70564; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:P59941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221; Evidence={ECO:0000250|UniProtKB:P59941}; CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; Evidence={ECO:0000250|UniProtKB:P59941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19150; Evidence={ECO:0000250|UniProtKB:P59941};

Acetylation;Acyltransferase;Chromatin regulator;Chromosome;Developmental protein;DNA damage;DNA repair;DNA-binding;Endoplasmic reticulum;Glycosyltransferase;Hydrolase;Isopeptide bond;Metal-binding;NAD;Nucleotidyltransferase;Nucleus;Phosphoprotein;Reference proteome;RNA-binding;Telomere;Transferase;Tumor suppressor;Ubl conjugation;Zinc

cardiac muscle cell differentiation [GO:0055007]; circadian regulation of gene expression [GO:0032922]; determination of adult lifespan [GO:0008340]; double-strand break repair [GO:0006302]; ketone biosynthetic process [GO:0042181]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of glycolytic process [GO:0045820]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; pericentric heterochromatin formation [GO:0031508]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein localization to chromatin [GO:0120187]; positive regulation of stem cell differentiation [GO:2000738]; protein delipidation [GO:0051697]; protein destabilization [GO:0031648]; regulation of circadian rhythm [GO:0042752]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of lipid catabolic process [GO:0050994]; regulation of lipid metabolic process [GO:0019216]; retrotransposon silencing [GO:0010526]

chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]

chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA damage sensor activity [GO:0140612]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; NAD-dependent histone H3K18 deacetylase activity [GO:0097372]; NAD-dependent histone H3K56 deacetylase activity [GO:0140765]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent protein deacetylase activity [GO:0034979]; NAD-dependent protein demyristoylase activity [GO:0140773]; NAD-dependent protein depalmitoylase activity [GO:0140774]; nucleosome binding [GO:0031491]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; TORC2 complex binding [GO:1904841]; transcription corepressor activity [GO:0003714]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin regions. Localizes to DNA damage sites: directly recognizes and binds double-strand breaks (DSBs) sites via a tunnel-like structure that has high affinity for DSBs (By similarity). A fraction localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7}.

PTM: Acetylated at Lys-33. Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Phosphorylation at Ser-10 by MAPK8/JNK1 in response to oxidative stress stimulates the mono-ADP-ribosyltransferase activity on PARP1, leading to PARP1 recruitment to double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Monoubiquitinated at Lys-170 by STUB1/CHIP, preventing its degradation by the proteasome. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Sumoylated, leading to specifically decrease ability to deacetylate histone H3 at 'Lys-56' (H3K56ac). {ECO:0000250|UniProtKB:Q8N6T7}.

DOMAIN: The C-terminal disordered region mediates non-specific DNA-binding. {ECO:0000250|UniProtKB:Q8N6T7}.

IPR029035;IPR003000;IPR026590;

2.20.28.200;3.40.50.1220;

A0A286R227

MGVRHSASKDYIAGRPLVPGEAPLDKKNSNFSSWKPVTEIDDRDAKCADNWVPRHPDLIRLTGKHPFNSEPPHADVMKEGWLTPVSMHFVRNHGAVPRLEWGSHRITITGLVERPMEITMDDIAKLPAVTVPCLLTCCGNRRKEVNMVKNSQGFSWGPGAVSVNNWTGARLSDVLKLVGVKSQAQGAKYVHFCGPKGELPKGVDGSYGTALTLGHALDPSMDVLIAYKQNGQFLHPDHGFPCRMLIPGWIGGRSVKWLSHLHVSDKDSQNWYHFHDNKVLPPHVDAESAAKQGWWKDPSFILKELNINSTISSPGHDERILMDQNRRYTMKGYAYSGGGRKIVRVEVSFNGGETWSHPAKIIVTETPNQAGKHWTWVHWELPVDTSQFFTATEVVCRAWDESQNTQPAVLTWTLLGQGNNSMFRLRLHKEVDPQGRLCIRFQQPAPILPGPLGNVGWREQEAGSAVPSAPAAVAAAAPGLDSTKKYVTKAMLEQHVEEASVWFAYKGKVYDGTKFLDDHPGGADSILMAGGEDATEDFDAVHSDSAKKQLEQFYIAELAPEGVPVPANLLYGGVDAAVVVMPGTAAAPLPAIDVDAPFLNPKKQKAAELKEKIKISHDVTLFRFGLEHDEQLLGLPTGKHMLIRKKVTNAEGDEEVVMRAYTPTTANETRGHFDLVVKIYKANVHPKFPEGGKFSQILEALEVGDTVEVKGPIGHFHYDRPGHYKNHKLESEVKRINMIAGGTGLTPMYQVMKAILSNPSDLTEIRLLYANQTEADILLRPELEALAKSHPDRVKIHYTVDRPTPGWKYSSGFIDLDMCERALFRYEPGTISVLCGPPPMLKFACHPNLEKMGFEKGVTSIEF

Ulva prolifera (Green seaweed) (Enteromorpha prolifera)

FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. {ECO:0000305}.

1.7.1.1

CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; Evidence={ECO:0000269|PubMed:29371148};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29371148}; Note=Binds 1 FAD (per monomer/chain). {ECO:0000269|PubMed:29371148}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:P49050}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250|UniProtKB:P49050}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305|PubMed:29371148}; Note=Binds 1 heme group. The heme group is called cytochrome b-557. {ECO:0000305};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for NADH in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:29371148}; Vmax=9055 umol/min/mg enzyme in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:29371148}; Note=kcat is 4900 sec(-1) for NADH in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius). {ECO:0000269|PubMed:29371148};

3D-structure;FAD;Flavoprotein;Heme;Iron;Metal-binding;Molybdenum;Nitrate assimilation;Oxidoreductase

cellular response to nitrite [GO:0071250]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126]; sulfur compound metabolic process [GO:0006790]

mitochondrion [GO:0005739]

FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase activity [GO:0008940]; sulfite oxidase activity [GO:0008482]

IPR008333;IPR001199;IPR036400;IPR018506;IPR017927;IPR001709;IPR039261;IPR014756;IPR005066;IPR008335;IPR001433;IPR000572;IPR036374;IPR022407;IPR017938;

2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10;

A0A286ZLF6

MASHPERGEILLTELQGDSRSLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDVSDCPRTPDTPSSDPRCSTSNNRLMALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSVIIEELSLVASPTLSPRQSVISAQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKAASVALPGWSPSETRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQAPVPAAVPVVDVRLPELAPPATDSAVTKLDFDLEPVPPPAPPRDSSLGEVDEAAELRDLDTPGQDSETLFDTENDRNSILPKSQSEYEPDIPQSGLEYSGIHELEDRRSQQMFQFNLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTTEHVCFVMEYAAGGDLMMHIHTDVFSEPRAAFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLVYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLIDWSALMDKKVKPPFVPTVRGREDVSNFDDEFTSEAPILTPPREPRILSEEEQEMFRDFDYIADWC

Sus scrofa (Pig)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};

ATP-binding;Coiled coil;Cytoplasm;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase

apical junction assembly [GO:0043297]; epithelial cell migration [GO:0010631]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of viral genome replication [GO:0045070]; regulation of cell motility [GO:2000145]

apical junction complex [GO:0043296]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone deacetylase binding [GO:0042826]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase binding [GO:0070063]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR000008;IPR035892;IPR037784;IPR011072;IPR036274;IPR011009;IPR017892;IPR037313;IPR000719;IPR017441;IPR008271;

2.60.40.150;1.10.287.160;1.10.510.10;

A0A286ZLI2

MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVLFYLSDREPLRLGGGEYTAEEVCIKAAQECCISPLCHNLFALYDESTKLWYAPNRTITVDDKTSVRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKVPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMSRFHPNDGGNVLYEVMVTGNLGIQWRQKPNVVPIEKEKNKLKRKKLESKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLIDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVLGGQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFVLKRCCQPKPREISNLLVATKKAQEWQPVYTMSQLSFDRILKNDIMQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKRKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLIQCKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPEEVYQLMRKCWEFQPSNRTTFQNLIEGFEALLK

Sus scrofa (Pig)

2.7.10.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};

Adaptive immunity;ATP-binding;Immunity;Kinase;Membrane;Nucleotide-binding;Proteomics identification;Reference proteome;SH2 domain;Transferase;Tyrosine-protein kinase

adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; cytokine-mediated signaling pathway [GO:0019221]; growth hormone receptor signaling pathway via JAK-STAT [GO:0060397]; interleukin-11-mediated signaling pathway [GO:0038154]; interleukin-15-mediated signaling pathway [GO:0035723]; interleukin-2-mediated signaling pathway [GO:0038110]; interleukin-4-mediated signaling pathway [GO:0035771]; interleukin-6-mediated signaling pathway [GO:0070102]; interleukin-9-mediated signaling pathway [GO:0038113]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of homotypic cell-cell adhesion [GO:0034112]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of sprouting angiogenesis [GO:1903672]; protein localization to cell-cell junction [GO:0150105]; receptor signaling pathway via JAK-STAT [GO:0007259]; response to antibiotic [GO:0046677]; type I interferon-mediated signaling pathway [GO:0060337]; type II interferon-mediated signaling pathway [GO:0060333]

cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]

ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein phosphatase binding [GO:0019903]; ubiquitin protein ligase binding [GO:0031625]

SUBCELLULAR LOCATION: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.

IPR019749;IPR035963;IPR019748;IPR000299;IPR041155;IPR041046;IPR041381;IPR011009;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR008266;IPR020635;IPR016251;IPR020776;

3.30.505.10;1.10.510.10;

A0A286ZML4

MYLFFPPGTDHPQKALKEDKLFFPNKRKPRSMSGHRSARKRCGDSHPESPLGFGHMSTPGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVPSWIAPNLITIIGLSINICTTVLLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIFDVTESQIIIIICQLLTGTLGPWFWNFTIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH

Sus scrofa (Pig)

FUNCTION: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000256|ARBA:ARBA00037663}.

2.7.8.1; 2.7.8.2; 2.7.8.22

CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycerol + CDP-choline = 1,2-di-(9Z-hexadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54336, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:83717, ChEBI:CHEBI:84417; Evidence={ECO:0000256|ARBA:ARBA00035878}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54337; Evidence={ECO:0000256|ARBA:ARBA00035878}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycerol + CDP-ethanolamine = 1,2-di-(9Z-hexadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:54340, ChEBI:CHEBI:15378, ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:84417, ChEBI:CHEBI:138145; Evidence={ECO:0000256|ARBA:ARBA00036341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54341; Evidence={ECO:0000256|ARBA:ARBA00036341}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + CDP-choline = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54240, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74669; Evidence={ECO:0000256|ARBA:ARBA00036096}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54241; Evidence={ECO:0000256|ARBA:ARBA00036096}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + CDP-ethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:54248, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333, ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:74986; Evidence={ECO:0000256|ARBA:ARBA00036523}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54249; Evidence={ECO:0000256|ARBA:ARBA00036523}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoyl-sn-glycerol + CDP-choline = 1,2-didecanoyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54236, ChEBI:CHEBI:15378, ChEBI:CHEBI:18155, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:78226; Evidence={ECO:0000256|ARBA:ARBA00036329}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54237; Evidence={ECO:0000256|ARBA:ARBA00036329}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycerol + CDP-choline = 1,2-dioctanoyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54232, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:76979, ChEBI:CHEBI:78228; Evidence={ECO:0000256|ARBA:ARBA00036651}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233; Evidence={ECO:0000256|ARBA:ARBA00036651}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z-alkenyl)-2-acyl-sn-glycerol + CDP-choline = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:36227, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:77286, ChEBI:CHEBI:77296; EC=2.7.8.22; Evidence={ECO:0000256|ARBA:ARBA00036576}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36228; Evidence={ECO:0000256|ARBA:ARBA00036576}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-2-acyl-sn-glycerol + CDP-choline = 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:36179, ChEBI:CHEBI:15378, ChEBI:CHEBI:36702, ChEBI:CHEBI:52595, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2; Evidence={ECO:0000256|ARBA:ARBA00035779}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36180; Evidence={ECO:0000256|ARBA:ARBA00035779}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + CDP-choline = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54352, ChEBI:CHEBI:15378, ChEBI:CHEBI:55430, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:77184; Evidence={ECO:0000256|ARBA:ARBA00036748}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54353; Evidence={ECO:0000256|ARBA:ARBA00036748}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + CDP-choline = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54348, ChEBI:CHEBI:15378, ChEBI:CHEBI:44811, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:75936; Evidence={ECO:0000256|ARBA:ARBA00036059}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54349; Evidence={ECO:0000256|ARBA:ARBA00036059}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol + CDP-choline = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54332, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74963, ChEBI:CHEBI:82949; Evidence={ECO:0000256|ARBA:ARBA00036100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333; Evidence={ECO:0000256|ARBA:ARBA00036100}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-choline = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54244, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:73001, ChEBI:CHEBI:75466; Evidence={ECO:0000256|ARBA:ARBA00036890}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245; Evidence={ECO:0000256|ARBA:ARBA00036890}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-ethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:54252, ChEBI:CHEBI:15378, ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:73007, ChEBI:CHEBI:75466; Evidence={ECO:0000256|ARBA:ARBA00035972}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54253; Evidence={ECO:0000256|ARBA:ARBA00035972}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2; Evidence={ECO:0000256|ARBA:ARBA00035868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940; Evidence={ECO:0000256|ARBA:ARBA00035868}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:32943, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:64612; EC=2.7.8.1; Evidence={ECO:0000256|ARBA:ARBA00036031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32944; Evidence={ECO:0000256|ARBA:ARBA00036031};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.; PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2. {ECO:0000256|ARBA:ARBA00037890}.; PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3. {ECO:0000256|ARBA:ARBA00037891}.

Endoplasmic reticulum;Glycoprotein;Lipid biosynthesis;Lipid metabolism;Manganese;Membrane;Nucleus;Phospholipid biosynthesis;Phospholipid metabolism;Proteomics identification;Reference proteome;Transferase;Transmembrane;Transmembrane helix

phosphatidylethanolamine biosynthetic process [GO:0006646]

endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; nuclear membrane [GO:0031965]

diacylglycerol cholinephosphotransferase activity [GO:0004142]; ethanolaminephosphotransferase activity [GO:0004307]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.

IPR000462;IPR043130;IPR048254;IPR014472;

1.20.120.1760;

A0A286ZNU0

MSKRKAPQETLNGGITDMLTELANFEKNVNQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKHEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRPKLLHRVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNNEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPVGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE

Sus scrofa (Pig)

FUNCTION: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. {ECO:0000256|RuleBase:RU366014}.

2.7.7.7

CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000256|ARBA:ARBA00024490}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|RuleBase:RU366014}; CATALYTIC ACTIVITY: Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195; Evidence={ECO:0000256|ARBA:ARBA00035582};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

DNA damage;DNA repair;DNA replication;DNA synthesis;DNA-directed DNA polymerase;Lyase;Methylation;Nucleotidyltransferase;Nucleus;Reference proteome;Sodium;Transferase;Ubl conjugation

base-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; DNA replication [GO:0006260]; double-strand break repair via nonhomologous end joining [GO:0006303]; homeostasis of number of cells [GO:0048872]; immunoglobulin heavy chain V-D-J recombination [GO:0071707]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lymph node development [GO:0048535]; neuron apoptotic process [GO:0051402]; salivary gland morphogenesis [GO:0007435]; somatic hypermutation of immunoglobulin genes [GO:0016446]; spleen development [GO:0048536]

cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle microtubule [GO:0005876]

5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU366014}.

IPR002054;IPR010996;IPR028207;IPR018944;IPR027421;IPR037160;IPR022312;IPR002008;IPR003583;IPR043519;IPR029398;

1.10.150.20;3.30.460.10;1.10.150.110;3.30.210.10;

A0A286ZP69

MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPAVAEATVSRAQSPSRSKNTLRPSTTRPPSPESSLLSSCQEKPHPTTPSPCTHTHTHTHTHIHT

Sus scrofa (Pig)

CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000256|ARBA:ARBA00000249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000256|ARBA:ARBA00000249};

Autophagy;Endosome;GTP-binding;Lipid degradation;Lipid metabolism;Nucleotide-binding;Proteomics identification;Reference proteome

autophagosome assembly [GO:0000045]; early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; endosome to plasma membrane protein transport [GO:0099638]; epidermal growth factor catabolic process [GO:0007174]; establishment of vesicle localization [GO:0051650]; lipid catabolic process [GO:0016042]; lipophagy [GO:0061724]; negative regulation of exosomal secretion [GO:1903542]; phagosome acidification [GO:0090383]; phagosome-lysosome fusion [GO:0090385]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of viral process [GO:0048524]; protein targeting to lysosome [GO:0006622]; protein to membrane docking [GO:0022615]; response to bacterium [GO:0009617]; retrograde transport, endosome to Golgi [GO:0042147]; viral release from host cell [GO:0019076]

autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lipid droplet [GO:0005811]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; melanosome membrane [GO:0033162]; mitochondrial membrane [GO:0031966]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; phagophore assembly site membrane [GO:0034045]; retromer complex [GO:0030904]

GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; retromer complex binding [GO:1905394]

SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000256|ARBA:ARBA00037866}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037866}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037866}. Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00037824}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037824}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037824}. Endosome membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004492}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004492}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004492}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004630}. Melanosome membrane {ECO:0000256|ARBA:ARBA00037798}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037798}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037798}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004318}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004318}.

IPR027417;IPR005225;IPR001806;

3.40.50.300;

A0A286ZPB0

MGLWPRTFLLGLLLLGQGTIQAHTSPEEKALEEQLWPETLKSFLFSCTSKKSEPRVPSKSVHSLRPSDIRFVAAIGHMETPPDSGTADPLKQNWTENRPPQACMGVVTVLSDVIRHFSPSVLRPVCTPGKGAVPHDGAEDLWMQAKELVRSMKGNQQLDFQNDWKLINVFFANTSQCHLCPSAQQQRHVTSSLDKLTRVLDHLHQEVPKAFVNLVDLSEALGSLHWQPGTPISPSAEPCRCSGETSQLSRVVTQWSYQETWERLLASSKYNEQESFAVVFQPFFYERALPPPSGKRPLQDPIALALTLWNSMMEPVGQKDEPFSAREKRPVKCPSQEDPYLFTYRNSNYLPRLPTPQAKFEVREGAEISCPDKDPSDTIPTSAGNGAGSRPGNVLDVLTQYRGLSWSAGGDHNLSSVTTLPNILREFNPSLKGFSVGTGRENSPGAFLNQAVAGSRAEDLPAQARRLVDLMKNDTSINFQEDWKIITLFIGGNDLCDVCNDPFRYSPENFTSNIGKALDILHAEVPRAFVNMVKVLQIISLRELYQEKNVSCPRLILRNLCPCVLKFDDNSTELASLIEVNKKYQEGTHQLVESGRYDTREDFTVVVQPFLEKVDMPKTPDGLPDSSFFAPDCFHFSSKAHAHAASALWNNMLEPVGQKTTQHKFESKINIMCPNQDWPYLSTYKNDVQDYGSRLLCSDRAPSASPPTSVHALRPADIQVVAALGDSLTAGNGIGSKADDLSDVTTQYRGLSFSSGGDSYLEKVTTLPNILRKFNGNLTGYAVGTGDANDTNASFNQAVPGAKTKELASQVQTLIQKMKDDHRVNFQGDWKIITVLIGGSDLCDYCTDSNLYSAANFFVHLRNALDILHREVPRALVNLVDFMSPSVMRQTFLGNPDKCPLQQASVFCNCVLTPRESSQELARLEAVTRAYQSSARELVESGRYDTREDFSVVLQPFFSNLRLPVLEDGSLDLSFFAPDCLHPSQKFHSQLSRALWVNMLEPVGRKTDTLDLMADIPLPCPTQNEPFLRTARNSNYTYPSNPAIENWGSDFLCTEWNPSTSVPTSVHELRPADIKVVAALGDSVTTAVGARPSNTSDLPTSWRGLSWSIGGDGDLESHTTLPNILKKFNPNILGFSTGTQEETAGLNVAVEGARARDMPTQARDLVERMKNSAEINLHKDWKLITLFIGSNDLCHYCENPEAHSAQEYVWHIQQALDILYQELPRAFVNVVEVMELAGLYQGQGDTCVMPLAAQSNCACFRGSQENSLEMQELKTVNWNFQSSISGFSFRPQYLQREDFAVVVQPFFRHTLAPLNNRGGADLSIFSEDCLHFSEHGHAELAIALWNNMMEPVGRKTTSNNFTYSRTKLKCPSPDSPYIYTLRNSQLLQDKAAAGPKELPWATPVAAGCGLVVGIGTVMAWRALRRRQRGNPPISLNTGSF

Sus scrofa (Pig)

3.1.1.3; 3.1.1.4; 3.1.1.5

CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000256|ARBA:ARBA00000652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000256|ARBA:ARBA00000652}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669; Evidence={ECO:0000256|ARBA:ARBA00024478}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924; Evidence={ECO:0000256|ARBA:ARBA00024478}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2 H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999; Evidence={ECO:0000256|ARBA:ARBA00023347}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976; Evidence={ECO:0000256|ARBA:ARBA00023347}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000256|ARBA:ARBA00001479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000256|ARBA:ARBA00001479}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence={ECO:0000256|ARBA:ARBA00044468}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940; Evidence={ECO:0000256|ARBA:ARBA00044468}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-octadecenoate + 1,3-dihexadecanoylglycerol + H(+); Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619; Evidence={ECO:0000256|ARBA:ARBA00023336}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984; Evidence={ECO:0000256|ARBA:ARBA00023336}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688; Evidence={ECO:0000256|ARBA:ARBA00043681}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980; Evidence={ECO:0000256|ARBA:ARBA00043681}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000256|ARBA:ARBA00023407}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000256|ARBA:ARBA00023407}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112, ChEBI:CHEBI:64496; Evidence={ECO:0000256|ARBA:ARBA00024155}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916; Evidence={ECO:0000256|ARBA:ARBA00024155}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623, ChEBI:CHEBI:77624; Evidence={ECO:0000256|ARBA:ARBA00023424}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104; Evidence={ECO:0000256|ARBA:ARBA00023424}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466, ChEBI:CHEBI:77623; Evidence={ECO:0000256|ARBA:ARBA00023358}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112; Evidence={ECO:0000256|ARBA:ARBA00023358}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558, ChEBI:CHEBI:77623; Evidence={ECO:0000256|ARBA:ARBA00023339}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108; Evidence={ECO:0000256|ARBA:ARBA00023339}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000256|ARBA:ARBA00023408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000256|ARBA:ARBA00023408}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73002, ChEBI:CHEBI:76084; Evidence={ECO:0000256|ARBA:ARBA00023372}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972; Evidence={ECO:0000256|ARBA:ARBA00023372}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000256|ARBA:ARBA00001855}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000256|ARBA:ARBA00001855}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000256|ARBA:ARBA00001126}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000256|ARBA:ARBA00001126}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; Evidence={ECO:0000256|ARBA:ARBA00023391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; Evidence={ECO:0000256|ARBA:ARBA00023391}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000256|ARBA:ARBA00000597}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000256|ARBA:ARBA00000597}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097; Evidence={ECO:0000256|ARBA:ARBA00023338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928; Evidence={ECO:0000256|ARBA:ARBA00023338}; CATALYTIC ACTIVITY: Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938; Evidence={ECO:0000256|ARBA:ARBA00023386}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605; Evidence={ECO:0000256|ARBA:ARBA00023386}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000256|ARBA:ARBA00023382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000256|ARBA:ARBA00023382}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000256|ARBA:ARBA00023422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000256|ARBA:ARBA00023422}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000256|ARBA:ARBA00000150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000256|ARBA:ARBA00000150}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000256|ARBA:ARBA00023369}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000256|ARBA:ARBA00023369};

Cell membrane;Hydrolase;Lipid metabolism;Membrane;Phospholipid metabolism;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix

phospholipid metabolic process [GO:0006644]; positive regulation of acrosome reaction [GO:2000344]

apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]

lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623]; retinyl-palmitate esterase activity [GO:0050253]; triglyceride lipase activity [GO:0004806]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004247}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004247}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR001087;IPR008265;IPR035547;IPR038885;IPR036514;

3.40.50.1110;

A0A286ZQ79

MGACCSARDLRSVEDSKAREKLKKSKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVKQGEEFERKIGQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDDVFSQVCTHLDTLK

Sus scrofa (Pig)

FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-Rule:MF_03171}.

2.7.4.3; 2.7.4.6

CATALYTIC ACTIVITY: Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate; Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034400}; CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|ARBA:ARBA00034442}; CATALYTIC ACTIVITY: Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098, ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|ARBA:ARBA00034451}; CATALYTIC ACTIVITY: Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690, ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|ARBA:ARBA00034407}; CATALYTIC ACTIVITY: Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682, ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|ARBA:ARBA00034432}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10; Evidence={ECO:0000256|ARBA:ARBA00034410};

ATP-binding;Cytoplasm;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Transferase

ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; outer dense fiber [GO:0001520]

adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03171}.

DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. {ECO:0000256|HAMAP-Rule:MF_03171}.

IPR000850;IPR033690;IPR028582;IPR006267;IPR027417;

3.40.50.300;

A0A286ZS33

MDLSVDHIEEVQNVLNAMQKILECPIFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIIHAFELDTGLQFANNYNFSKKTENNSPEHLKEEVSIIQSMGYRNRAKRLRQSDPEDPTLQETSLSAQLSNLGIVKPLRTQQQIQPQNKSVYIELGSDSSEDTVNKANYCSGGDHGLLETTPQGAKAEAKKDACQFSEKDITNTEHHHSSNKDLTATEKHATEKHPEKYEGISVSNLHVEPCGTDTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPVLAKSQQSRWAESKGTCNDRQTPNTEKKVVLNTDLLYGRNELNKQKPACSDSPRDSQDVPWITLNSSIQKVNEWFSRSDEMLTSDDSQDRRSESNTGVAGAAEVPNEADGHLGSSEKIDLMASDPHGALIRERERGHSKPAESNIEDKIFGKTYRRKASLPNLSHVIEDLILGASAVEPQITQERPLTNKLKRKRRGTSGLDPEDFIKRADSAVVPKTPEKTIEGTDETEQNGQGMNITSKGHENETKSGNVQKEKNVNPTASLGKEPAFRARAEPISSSISNMELELNIHGSKAPKNRLRRKSSTRQIHALELVVNRNPSPPSHTELQIDSCSSSEEMKKRNSDQVPVRHSKKLHLRGDKEPTTGAKKNNRPHEQVNKRPISDAFPELNLTNVPVSITNCSNSNKLQESVSPNLQREENLGTIQVSNSNKDPKDVMLSGGKGFQIERSVENTSISLVPDTDYGTQDSISLLETDTLGKAKTTPNQHVRLCAATENPKELSLGCSKGVRNDTGDFKDPLAHDVNHTQEASIEVEENELDTQYLQSMFKVSKRQTFALFSNPANPEKECTTVHAHSKSLREQSPKVTHEGGQKDENQGKSESKVKHGQSVHTTVDFLVVGQKDKKPSDFAKCGAKGVTGLYQTSQFRGHKTEFINANKPGISQNPYVIPSLSPIRSSVKTICKKNLSEEKFEEPKMSPERTMGNESIIPNTESTVSQNNIQERTFKEGSSGSPNEVGSSTNEVGSSINEVGSSGENVRAEPGRNRGPKLSAMLRLGLMQPEVYKQSLPVSNCNHTEIKRQGENEGIFQAVNADFSPYLISDNPEQPMGSSHASQICSETPDDLLNDDKIKENLNFAESDVKERSAVFSKSAQEGEFKRSPSPLAHRRLAQGHQRWARKLESSEESGSSEDEELPCFQHLLFGKVTNTPSPSTRHNAVAAEGLSKEAGESLVSLKNSLNDCSDQVTSAKASQEHHLSEDVRCSGSLFSSQCSALEDSAANTNSQDPFLMFDPPSKQVEHQSENQEVLSDKELVSEDDERETGLEEDNCQEEQIVDSDLGETAFEYESETSFSEDCSGLSSQSAILTTQQRDTMQDNLLKLQQEMAELEAVLEQHGSQPSHSSPSLIADSCAPEDLLNPEQNTSEKVLTSEKSSDYPITQNPESLSADKFQVSLDRSTSKNKESGMERSSTSKSQLSDSRWYMHSPSRSLQNRSCPSQEELIPVIDLEEQQLTTSEAQDSVKQSYLPRQDLEGTPYLKSGISLFSDDPESDPSENRAPESAHVFSTPLSTSALKLPQFQVKESAKSPAAAHTTNTAGYNVRQESMSRKKPEVISSTKTNSRRISIVASGLTPKEYTLVQKFARKHYITLTNLITEETTHVIMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKEGKMLDEHDFEVRGDVVNGRNHRGPKRARESQDRKIFKGLEICCCGPFTNMPTDQLEWMVLLCGASVVKDPSSFTFRQGTRPVVVVQPDAWPEDSGFHVIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQVPQSCCRPCT

Sus scrofa (Pig)

FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator. {ECO:0000256|PIRNR:PIRNR001734}.

2.3.2.27

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900, ECO:0000256|PIRNR:PIRNR001734};

Cell cycle;Chromosome;DNA damage;DNA recombination;DNA repair;DNA-binding;Nucleus;Reference proteome;Ubl conjugation pathway

cellular response to indole-3-methanol [GO:0071681]; cellular response to ionizing radiation [GO:0071479]; cellular response to tumor necrosis factor [GO:0071356]; centrosome cycle [GO:0007098]; chordate embryonic development [GO:0043009]; chromosome segregation [GO:0007059]; double-strand break repair via homologous recombination [GO:0000724]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; localization [GO:0051179]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of angiogenesis [GO:0045766]; positive regulation of DNA repair [GO:0045739]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular endothelial growth factor production [GO:0010575]; postreplication repair [GO:0006301]; protein autoubiquitination [GO:0051865]; protein K6-linked ubiquitination [GO:0085020]; random inactivation of X chromosome [GO:0060816]; sex-chromosome dosage compensation [GO:0007549]

BRCA1-A complex [GO:0070531]; BRCA1-B complex [GO:0070532]; BRCA1-BARD1 complex [GO:0031436]; BRCA1-C complex [GO:0070533]; cytoplasm [GO:0005737]; DNA repair complex [GO:1990391]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]; XY body [GO:0001741]

damaged DNA binding [GO:0003684]; DNA-binding transcription activator activity [GO:0001216]; identical protein binding [GO:0042802]; p53 binding [GO:0002039]; RNA binding [GO:0003723]; RNA polymerase binding [GO:0070063]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|PIRNR:PIRNR001734}. Chromosome {ECO:0000256|PIRNR:PIRNR001734}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. {ECO:0000256|PIRNR:PIRNR001734}.

IPR011364;IPR031099;IPR025994;IPR001357;IPR036420;IPR013083;

3.40.50.10190;3.30.40.10;

A0A286ZSR3

MNQDLQKERAAASFNPELLTHVLDGSPENTRRRREIENMILSDPDLQHEDLNFLSRSQRYEVAVKKSATTVKKIREFGLADPDEILWFKKLHLVNFVEPVGLNYSMFIPTLLSQGTTAQREKWLPPSKRLEIIGTYAQTELGHGTHLRGLETTATYDPATEEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITQGKCYGLHAFIVPIREQGTHKPLPGITVGDIGPKFGYDEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFIRSFLVGEAARCLSKACTIAIRYSAVRHQSELRPDEPEPQILDYQTQQYKLFPFLATAYAFQFVGAYIKETYHRINENIRQGDLSGLPELHALTAGLKAFTSWTANAAIEACRMACGGHGYSHCSGLPNIYVNFTPTCTFEGENTVMMLQTARFLMKSYNQVHSGKLVCGMVSYLNDLPSQRIQPQQVAAWPTVADINSPDSLIEAYRLRASRLVEIAAKNLQTEMSHRKSKEAAWNLTSIDLVRASEAHCHYVVVKLFAEKLHQIQERSIHAVLRNLCLLYALYGISQNSGDFLQGSIMTESQVTHVNERVKELLMAIRPEAVALVDAFDFQDVTLGSVLGRYDGNVYENMFEWAKKSPLNKTEVKSKNSFSPFLKSFI

Sus scrofa (Pig)

CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + O2 = (2E,5Z,8Z,11Z,14Z,17Z)-icosahexaenoyl-CoA + H2O2; Xref=Rhea:RHEA:69643, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:73862, ChEBI:CHEBI:187901; Evidence={ECO:0000256|ARBA:ARBA00036444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69644; Evidence={ECO:0000256|ARBA:ARBA00036444}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + O2 = (2E,6Z,9Z,12Z,15Z,18Z,21Z)-tetracosaheptaenoyl-CoA + H2O2; Xref=Rhea:RHEA:39119, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:74086, ChEBI:CHEBI:76360; Evidence={ECO:0000256|ARBA:ARBA00036338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39120; Evidence={ECO:0000256|ARBA:ARBA00036338}; CATALYTIC ACTIVITY: Reaction=O2 + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O2; Xref=Rhea:RHEA:38971, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57394, ChEBI:CHEBI:71412; Evidence={ECO:0000256|ARBA:ARBA00036774}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972; Evidence={ECO:0000256|ARBA:ARBA00036774}; CATALYTIC ACTIVITY: Reaction=O2 + octanoyl-CoA = (2E)-octenoyl-CoA + H2O2; Xref=Rhea:RHEA:40175, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57386, ChEBI:CHEBI:62242; Evidence={ECO:0000256|ARBA:ARBA00036210}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176; Evidence={ECO:0000256|ARBA:ARBA00036210}; CATALYTIC ACTIVITY: Reaction=O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2; Xref=Rhea:RHEA:40319, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence={ECO:0000256|ARBA:ARBA00036229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320; Evidence={ECO:0000256|ARBA:ARBA00036229}; CATALYTIC ACTIVITY: Reaction=O2 + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40183, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57385, ChEBI:CHEBI:61405; Evidence={ECO:0000256|ARBA:ARBA00036028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184; Evidence={ECO:0000256|ARBA:ARBA00036028}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000256|ARBA:ARBA00036397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000256|ARBA:ARBA00036397}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + O2 = (2E)-decenoyl-CoA + H2O2; Xref=Rhea:RHEA:40179, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence={ECO:0000256|ARBA:ARBA00036151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180; Evidence={ECO:0000256|ARBA:ARBA00036151}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40171, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375; Evidence={ECO:0000256|ARBA:ARBA00036791}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172; Evidence={ECO:0000256|ARBA:ARBA00036791}; CATALYTIC ACTIVITY: Reaction=glutaryl-CoA + O2 = (2E)-glutaconyl-CoA + H2O2; Xref=Rhea:RHEA:40315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57353, ChEBI:CHEBI:57378; Evidence={ECO:0000256|ARBA:ARBA00036750}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40316; Evidence={ECO:0000256|ARBA:ARBA00036750}; CATALYTIC ACTIVITY: Reaction=hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2; Xref=Rhea:RHEA:40275, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:77075, ChEBI:CHEBI:77085; Evidence={ECO:0000256|ARBA:ARBA00036704}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276; Evidence={ECO:0000256|ARBA:ARBA00036704}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57379, ChEBI:CHEBI:61526; Evidence={ECO:0000256|ARBA:ARBA00036893}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168; Evidence={ECO:0000256|ARBA:ARBA00036893}; CATALYTIC ACTIVITY: Reaction=hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2; Xref=Rhea:RHEA:40311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; Evidence={ECO:0000256|ARBA:ARBA00036399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312; Evidence={ECO:0000256|ARBA:ARBA00036399};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974};

PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000256|ARBA:ARBA00004846}.

Acetylation;FAD;Fatty acid metabolism;Flavoprotein;Lipid metabolism;Oxidoreductase;Peroxisome;Phosphoprotein;Proteomics identification;Reference proteome

ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]; very long-chain fatty acid metabolic process [GO:0000038]

peroxisome [GO:0005777]

FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; palmitoyl-CoA oxidase activity [GO:0016401]

SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.

IPR034171;IPR029320;IPR006091;IPR046373;IPR012258;IPR002655;IPR036250;IPR037069;IPR009100;

1.10.540.10;2.40.110.10;1.20.140.10;

A0A286ZST3

MTVAWRHLLRALHLQTLSPRTPKAGPSLNGAFWTSVTKLGLHTKPIMPPCDFTPERYQSIAYSRVLDIHKQHLSPVQTAYFPEPLLLHQGHMEWLFDYEGNRYLDFFSGIVTVSVGHCHPKLNAAAQTQLGRLWHTSPVFFHPPIHEYAEKLSALLPEPLKVIFLVNSGSEANDLAMLMARAHTNNTDIISFRGAYHGCSPYTIGLTNVGFYKMRIPTGMGCRSTMCPDVFRGPWGGSHCRDSPVQTTRECSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVSGVVQYPKGFLKEAFELVRERGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVVTSPEIAESLAKCLFHFNTFGGNPVACAIGSAVLEVIQDENLQENSREVGTYLLLKLAKLRDEFDIVGDVRGKGLMIGIEMVKDKVGSDLPHSLQLTVALGGCKLTCLVLSERAHGDRKTQRRWISDEQEGRVSTEC

Sus scrofa (Pig)

2.6.1.18; 2.6.1.40; 2.6.1.44

CATALYTIC ACTIVITY: Reaction=(2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine; Xref=Rhea:RHEA:77339, ChEBI:CHEBI:16763, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:74359; Evidence={ECO:0000256|ARBA:ARBA00043679}; CATALYTIC ACTIVITY: Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361, ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40; Evidence={ECO:0000256|ARBA:ARBA00043726}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394; Evidence={ECO:0000256|ARBA:ARBA00043726}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate; Xref=Rhea:RHEA:77355, ChEBI:CHEBI:15361, ChEBI:CHEBI:16763, ChEBI:CHEBI:57972, ChEBI:CHEBI:74359; EC=2.6.1.44; Evidence={ECO:0000256|ARBA:ARBA00043751}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + N(omega),N(omega)-dimethyl-L-arginine = (2S)-2-aminobutanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate; Xref=Rhea:RHEA:77351, ChEBI:CHEBI:16763, ChEBI:CHEBI:58326, ChEBI:CHEBI:74359, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043779}; CATALYTIC ACTIVITY: Reaction=2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminohexanoate; Xref=Rhea:RHEA:77363, ChEBI:CHEBI:35177, ChEBI:CHEBI:58326, ChEBI:CHEBI:58455, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043837}; CATALYTIC ACTIVITY: Reaction=2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate; Xref=Rhea:RHEA:77359, ChEBI:CHEBI:28644, ChEBI:CHEBI:58326, ChEBI:CHEBI:58441, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043826}; CATALYTIC ACTIVITY: Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18; Evidence={ECO:0000256|ARBA:ARBA00043825}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079; Evidence={ECO:0000256|ARBA:ARBA00043825}; CATALYTIC ACTIVITY: Reaction=L-alanine + oxaloacetate = L-aspartate + pyruvate; Xref=Rhea:RHEA:77347, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:57972; Evidence={ECO:0000256|ARBA:ARBA00043764}; CATALYTIC ACTIVITY: Reaction=L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77327, ChEBI:CHEBI:15361, ChEBI:CHEBI:46911, ChEBI:CHEBI:57972, ChEBI:CHEBI:58802; Evidence={ECO:0000256|ARBA:ARBA00043777}; CATALYTIC ACTIVITY: Reaction=N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'-dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77307, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:197308, ChEBI:CHEBI:197310; Evidence={ECO:0000256|ARBA:ARBA00043798}; CATALYTIC ACTIVITY: Reaction=N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-aspartate; Xref=Rhea:RHEA:77343, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043749}; CATALYTIC ACTIVITY: Reaction=N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77303, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043669}; CATALYTIC ACTIVITY: Reaction=N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77319, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; Evidence={ECO:0000256|ARBA:ARBA00043758}; CATALYTIC ACTIVITY: Reaction=glyoxylate + L-alanine = glycine + pyruvate; Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44; Evidence={ECO:0000256|ARBA:ARBA00033660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249; Evidence={ECO:0000256|ARBA:ARBA00033660}; CATALYTIC ACTIVITY: Reaction=glyoxylate + L-ornithine = 5-amino-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77331, ChEBI:CHEBI:36655, ChEBI:CHEBI:46911, ChEBI:CHEBI:57305, ChEBI:CHEBI:58802; Evidence={ECO:0000256|ARBA:ARBA00043808}; CATALYTIC ACTIVITY: Reaction=glyoxylate + N(omega),N('omega)-dimethyl-L-arginine = 5-(3,3'-dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77315, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:197308, ChEBI:CHEBI:197310; Evidence={ECO:0000256|ARBA:ARBA00043659}; CATALYTIC ACTIVITY: Reaction=glyoxylate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77311, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043815}; CATALYTIC ACTIVITY: Reaction=glyoxylate + N(omega)-methyl-L-arginine = 5-(3-methylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77323, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; Evidence={ECO:0000256|ARBA:ARBA00043652};

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000256|ARBA:ARBA00001933};

Proteomics identification;Pyridoxal phosphate;Reference proteome

glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glyoxylate catabolic process [GO:0009436]; L-alanine catabolic process, by transamination [GO:0019481]; positive regulation of nitric oxide biosynthetic process [GO:0045429]

mitochondrion [GO:0005739]

(R)-3-amino-2-methylpropionate-pyruvate transaminase activity [GO:0047305]; alanine-glyoxylate transaminase activity [GO:0008453]; pyridoxal phosphate binding [GO:0030170]

IPR005814;IPR049704;IPR015424;IPR015421;IPR015422;

3.90.1150.10;3.40.640.10;

A0A286ZV67

MFGPAFSVDRAWSQRMSRPGREMGRPAGRGRAGSRVGGGGRGRGQMGAAGQGPWAPRTRQVGAEQGRDLERRAAAPTARRSGDGLPSIGGVSSAPVLCSRSLARVSHAPSPSPSLCPQYDAAPVQSSVVLCSCPSPSMVRTQTESSAAPGVPSGGSRQGPTMDSTAAEARPNTRSLQHAAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEMVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMGGYSPLKAHAFFESVMWENLHHQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSPSSQSLSAVDAGLPQRAGSNIEQYIHDLDTNSFELDLQFSEDEKRLLLEKQASGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCKKIQEVWRHRYQSHPDAAVQ

Sus scrofa (Pig)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

ATP-binding;Nucleotide-binding;Proteomics identification;Reference proteome

calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; epidermal growth factor receptor signaling pathway [GO:0007173]; extrinsic apoptotic signaling pathway [GO:0097191]; hyperosmotic response [GO:0006972]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; intracellular signal transduction [GO:0035556]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of mast cell degranulation [GO:0043304]; type B pancreatic cell development [GO:0003323]

cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]

3-phosphoinositide-dependent protein kinase activity [GO:0004676]; ATP binding [GO:0005524]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR033931;IPR039046;IPR011993;IPR000719;IPR017441;IPR008271;

2.30.29.30;1.10.510.10;

A0A286ZV73

MLARALLLCAAVSLCTAANPCCSNPCQNRGICMSVGFDHYKCDCTRTGFYGENCTTPEFLTRIKLFLKPTPNTVHYILTHFKGVWNIVNNIPFLRNAIMKYVLISRSHLIDSPPTYNMHYGYKSWEAFSNLSYYTRALPPVPDDCPTPMGVKGRKELPDSKEVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDQKRGPAFTKGQGHGVDLSHVYGESLERQHKLRLFKDGKMKYQIIDGEMYPPTAKDTQVEMIYPPHTPEHLRFAVGHEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDERLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDAFQIDGHEYNYQQFLYNNSILLEHGITQFVESFSRQIAGRVAGGRNLPAAVQKVSKASIDQSREMRYQSFNEYRKRFLLKPYRSFEELTGEKEMAAELEALYGDIDAMELYPALLVEKPRPDAIFGETMVEAGAPFSLKGLMGNPICSPEYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFSVQDPQLAKTVTINASSSHSGLDDINPTVLLKERSTEL

Sus scrofa (Pig)

1.14.99.1

CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000256|ARBA:ARBA00036380}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; Evidence={ECO:0000256|ARBA:ARBA00036380}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 13-hydroxy-(4Z,7Z,10Z,14E,16Z,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48820, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90815; Evidence={ECO:0000256|ARBA:ARBA00001305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48821; Evidence={ECO:0000256|ARBA:ARBA00001305}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 17R-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48816, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90814; Evidence={ECO:0000256|ARBA:ARBA00001077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48817; Evidence={ECO:0000256|ARBA:ARBA00001077}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,11R)-dihydroxy-(6E,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48804, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90810; Evidence={ECO:0000256|ARBA:ARBA00000472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48805; Evidence={ECO:0000256|ARBA:ARBA00000472}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15R)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48812, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90812; Evidence={ECO:0000256|ARBA:ARBA00000487}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48813; Evidence={ECO:0000256|ARBA:ARBA00000487}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48808, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90813; Evidence={ECO:0000256|ARBA:ARBA00000608}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48809; Evidence={ECO:0000256|ARBA:ARBA00000608}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000256|ARBA:ARBA00000144}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000256|ARBA:ARBA00001779}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000256|ARBA:ARBA00001779}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78836; Evidence={ECO:0000256|ARBA:ARBA00001704}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50853; Evidence={ECO:0000256|ARBA:ARBA00001704}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78837; Evidence={ECO:0000256|ARBA:ARBA00001382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50857; Evidence={ECO:0000256|ARBA:ARBA00001382}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:42284, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82626; Evidence={ECO:0000256|ARBA:ARBA00001587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42285; Evidence={ECO:0000256|ARBA:ARBA00001587}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 11R-hydroperoxy-(5Z,8Z,12E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:42280, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82628; Evidence={ECO:0000256|ARBA:ARBA00023566}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42281; Evidence={ECO:0000256|ARBA:ARBA00023566}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 O2 = prostaglandin G3; Xref=Rhea:RHEA:50444, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:133133; Evidence={ECO:0000256|ARBA:ARBA00001578}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50445; Evidence={ECO:0000256|ARBA:ARBA00001578}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50848, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90820; Evidence={ECO:0000256|ARBA:ARBA00000949}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50849; Evidence={ECO:0000256|ARBA:ARBA00000949}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48840, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90819; Evidence={ECO:0000256|ARBA:ARBA00001414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48841; Evidence={ECO:0000256|ARBA:ARBA00001414}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50196, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132087; Evidence={ECO:0000256|ARBA:ARBA00001580}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50197; Evidence={ECO:0000256|ARBA:ARBA00001580}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48836, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90818; Evidence={ECO:0000256|ARBA:ARBA00000931}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48837; Evidence={ECO:0000256|ARBA:ARBA00000931}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50200, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132083; Evidence={ECO:0000256|ARBA:ARBA00001068}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50201; Evidence={ECO:0000256|ARBA:ARBA00001068}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + AH2 + O2 = 13R-hydroxy-(7Z,10Z,14E,16Z,19Z)-docosapentaenoate + A + H2O; Xref=Rhea:RHEA:48852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77224, ChEBI:CHEBI:90824; Evidence={ECO:0000256|ARBA:ARBA00000425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48853; Evidence={ECO:0000256|ARBA:ARBA00000425}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + 2 O2 = prostaglandin G1; Xref=Rhea:RHEA:50424, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:133084; Evidence={ECO:0000256|ARBA:ARBA00000224}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50425; Evidence={ECO:0000256|ARBA:ARBA00000224}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000256|ARBA:ARBA00036409}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000256|ARBA:ARBA00036409}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000256|ARBA:ARBA00036358}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000256|ARBA:ARBA00036358}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000256|ARBA:ARBA00036313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000256|ARBA:ARBA00036313}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000256|ARBA:ARBA00035976}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000256|ARBA:ARBA00035976}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 13-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50860, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133819; Evidence={ECO:0000256|ARBA:ARBA00000021}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50861; Evidence={ECO:0000256|ARBA:ARBA00000021}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 9-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50864, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133820; Evidence={ECO:0000256|ARBA:ARBA00001767}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50865; Evidence={ECO:0000256|ARBA:ARBA00001767}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:54212, ChEBI:CHEBI:15379, ChEBI:CHEBI:76079, ChEBI:CHEBI:138100; Evidence={ECO:0000256|ARBA:ARBA00000197}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54213; Evidence={ECO:0000256|ARBA:ARBA00000197}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53676, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137582; Evidence={ECO:0000256|ARBA:ARBA00001736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53677; Evidence={ECO:0000256|ARBA:ARBA00001736}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53680, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137583; Evidence={ECO:0000256|ARBA:ARBA00000678}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53681; Evidence={ECO:0000256|ARBA:ARBA00000678}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53684, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137584; Evidence={ECO:0000256|ARBA:ARBA00000429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53685; Evidence={ECO:0000256|ARBA:ARBA00000429}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:54204, ChEBI:CHEBI:15379, ChEBI:CHEBI:76091, ChEBI:CHEBI:138098; Evidence={ECO:0000256|ARBA:ARBA00000990}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54205; Evidence={ECO:0000256|ARBA:ARBA00000990}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 2 O2 = 2-glyceryl-prostaglandin G2; Xref=Rhea:RHEA:45288, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:85165; Evidence={ECO:0000256|ARBA:ARBA00000559}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289; Evidence={ECO:0000256|ARBA:ARBA00000559}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphocholine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:54216, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138100, ChEBI:CHEBI:138101; Evidence={ECO:0000256|ARBA:ARBA00000763}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54217; Evidence={ECO:0000256|ARBA:ARBA00000763}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphoethanolamine + A + H2O; Xref=Rhea:RHEA:54208, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138098, ChEBI:CHEBI:138099; Evidence={ECO:0000256|ARBA:ARBA00000973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54209; Evidence={ECO:0000256|ARBA:ARBA00000973}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin G2 + AH2 = 2-glyceryl-prostaglandin H2 + A + H2O; Xref=Rhea:RHEA:45292, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:85165, ChEBI:CHEBI:85166; Evidence={ECO:0000256|ARBA:ARBA00001567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293; Evidence={ECO:0000256|ARBA:ARBA00001567}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G1 = A + H2O + prostaglandin H1; Xref=Rhea:RHEA:50432, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:90793, ChEBI:CHEBI:133084; Evidence={ECO:0000256|ARBA:ARBA00001877}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50433; Evidence={ECO:0000256|ARBA:ARBA00001877}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000256|ARBA:ARBA00000489}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G3 = A + H2O + prostaglandin H3; Xref=Rhea:RHEA:50448, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:133133, ChEBI:CHEBI:133134; Evidence={ECO:0000256|ARBA:ARBA00000545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50449; Evidence={ECO:0000256|ARBA:ARBA00000545};

COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970};

PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702}.

Dioxygenase;EGF-like domain;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Microsome;Oxidoreductase;Peroxidase;Prostaglandin biosynthesis;Prostaglandin metabolism;Reference proteome;Signal

cellular response to hypoxia [GO:0071456]; cyclooxygenase pathway [GO:0019371]; response to oxidative stress [GO:0006979]

cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]

enzyme binding [GO:0019899]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}. Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004386}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004386}. Nucleus outer membrane {ECO:0000256|ARBA:ARBA00004509}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004509}.

IPR000742;IPR019791;IPR010255;IPR037120;

1.10.640.10;2.10.25.10;

A0A286ZVY2

MAALSGGGGGGGAEQGQALFNGDMEPEAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASTDTVTSSSSSSLSVLPSSLSVFQNPTDASRSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPPSDSLGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRSDGAPLNQLMRCLRKYQSRTPSPLLHSVPSEIVFDFEPGPVFRGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGEFAAFK

Sus scrofa (Pig)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

ATP-binding;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc

CD4-positive or CD8-positive, alpha-beta T cell lineage commitment [GO:0043369]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; endothelial cell apoptotic process [GO:0072577]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; establishment of protein localization to membrane [GO:0090150]; face development [GO:0060324]; head morphogenesis [GO:0060323]; long-term synaptic potentiation [GO:0060291]; MAPK cascade [GO:0000165]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of synaptic vesicle exocytosis [GO:2000301]; phosphorylation [GO:0016310]; positive regulation of axon regeneration [GO:0048680]; positive regulation of axonogenesis [GO:0050772]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; Ras protein signal transduction [GO:0007265]; regulation of cell population proliferation [GO:0042127]; regulation of T cell differentiation [GO:0045580]; somatic stem cell population maintenance [GO:0035019]; stress fiber assembly [GO:0043149]; substrate adhesion-dependent cell spreading [GO:0034446]; synaptic vesicle exocytosis [GO:0016079]; T cell differentiation in thymus [GO:0033077]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; trehalose metabolism in response to stress [GO:0070413]; visual learning [GO:0008542]

cell body [GO:0044297]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynapse [GO:0098793]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; MAP kinase kinase activity [GO:0004708]; MAP kinase kinase kinase activity [GO:0004709]; scaffold protein binding [GO:0097110]

IPR046349;IPR020454;IPR011009;IPR002219;IPR000719;IPR017441;IPR003116;IPR001245;IPR008271;IPR029071;

3.30.60.20;1.10.510.10;

A0A286ZWK2

MAALTAAFHAGSDPVAWLFPTRAVSERFFLSTATMSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFVVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVCFCTVGLAYCVRCYNSERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD

Sus scrofa (Pig)

3.6.4.10

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000256|ARBA:ARBA00001629};

ATP-binding;mRNA processing;mRNA splicing;Nucleotide-binding;Proteomics identification;Reference proteome;Spliceosome

ATP metabolic process [GO:0046034]; chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated autophagy translocation complex disassembly [GO:1904764]; clathrin coat disassembly [GO:0072318]; late endosomal microautophagy [GO:0061738]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of NLRP3 inflammasome complex assembly [GO:1900226]; negative regulation of supramolecular fiber organization [GO:1902904]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; protein refolding [GO:0042026]; protein targeting to lysosome involved in chaperone-mediated autophagy [GO:0061740]; regulation of cell cycle [GO:0051726]; regulation of postsynapse organization [GO:0099175]; regulation of protein stability [GO:0031647]; RNA splicing [GO:0008380]; slow axonal transport [GO:1990832]

autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; glycinergic synapse [GO:0098690]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; postsynaptic cytosol [GO:0099524]; postsynaptic specialization membrane [GO:0099634]; presynaptic cytosol [GO:0099523]; protein folding chaperone complex [GO:0101031]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; terminal bouton [GO:0043195]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; ATP-dependent protein folding chaperone [GO:0140662]; C3HC4-type RING finger domain binding [GO:0055131]; clathrin-uncoating ATPase activity [GO:1990833]; G protein-coupled receptor binding [GO:0001664]; heat shock protein binding [GO:0031072]; phosphatidylserine binding [GO:0001786]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]

IPR043129;IPR018181;IPR029048;IPR029047;IPR013126;

1.20.1270.10;3.30.30.30;3.30.420.40;

A0A286ZZ96

MQRSPLEKASIFSKLFFSWTRPILRKGYRQRLELSDIYHISSSDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIILYLGEVTKAVQPLLLGRIIASYDPDNKAERSIAIYLGVGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWELLQASAFCGLAFLVVLALFQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGLFVVFLSVLPYALLKGIMLRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGKLFEKAKQNNNSRKISNGDNSLFFSNFSLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSQRPDFSSKLMGYDTFDQFTAERRNSIITETLRRFSLEGDASVSWNETKKQSFKQTGEFGEKRKNSILNSINSIRKFSIVQKTPLQMNGFEEDSGEPLERRLSLVPDSEHGEAILPRSNVINAGPTFQGRRRQSVLNLMTRSSVNQGQSIHRKTATSTRKMSLVPQANLTEIDIYSRRLSQDTGLEISEEINEEDLRECFFDDVESIPTVTTWNTYLRYVTVHKSLIFVLIWCLVVFLAEVAACLVVLCLLKKTSPQDKGNSTKGANNSYAVIITSTSAYYVFYIYVGVADGLLALGLFRGLPLVHTLITVSKILHRKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVAVVSVLKPYIFLATVPVIVAFILLRAYFLHTSQQLKQLESEGRSPIFTHLITSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGTVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPAEGDQPNRSFKPSKDGQLSKVMIIENQHVKKDDIWPSGGQMTVKDLTAKYVDGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTEGEIQVDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYGQWNDQEIWKVAEEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLGKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRLLSEKSLFRQAISPLDRLKLLPHRNSSKQRSRSKIAALKEETEEEVQETRL

Sus scrofa (Pig)

FUNCTION: Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. Mediates the transport of chloride ions across the cell membrane. Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. {ECO:0000256|RuleBase:RU362037}.

5.6.1.6

CATALYTIC ACTIVITY: Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000256|ARBA:ARBA00034073, ECO:0000256|RuleBase:RU362037};

ATP-binding;Chloride;Chloride channel;Endoplasmic reticulum;Endosome;Glycoprotein;Ion channel;Ion transport;Isomerase;Isopeptide bond;Lipoprotein;Membrane;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Transport;Ubl conjugation

amelogenesis [GO:0097186]; bicarbonate transport [GO:0015701]; cellular response to cAMP [GO:0071320]; cellular response to forskolin [GO:1904322]; chloride transmembrane transport [GO:1902476]; cholesterol biosynthetic process [GO:0006695]; cholesterol transport [GO:0030301]; establishment of localization in cell [GO:0051649]; intracellular pH elevation [GO:0051454]; membrane hyperpolarization [GO:0060081]; multicellular organismal-level water homeostasis [GO:0050891]; positive regulation of enamel mineralization [GO:0070175]; positive regulation of exocytosis [GO:0045921]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; response to endoplasmic reticulum stress [GO:0034976]; sperm capacitation [GO:0048240]; transepithelial water transport [GO:0035377]; vesicle docking involved in exocytosis [GO:0006904]

apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; chloride channel complex [GO:0034707]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]

ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; bicarbonate transmembrane transporter activity [GO:0015106]; chloride channel inhibitor activity [GO:0019869]; enzyme binding [GO:0019899]; intracellularly ATP-gated chloride channel activity [GO:0005260]; isomerase activity [GO:0016853]; PDZ domain binding [GO:0030165]; protein-folding chaperone binding [GO:0051087]; Sec61 translocon complex binding [GO:0106138]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362037}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362037}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.

IPR003593;IPR011527;IPR036640;IPR003439;IPR017871;IPR009147;IPR047082;IPR025837;IPR027417;

1.20.1560.10;3.40.50.300;

A0A287A2E8

MGRALLLLLRWLLLPALWRGAIAEAREDTKHTLPFPGPLPGSPQADHMPFSFPHTRGHQATSMLPPTQPGRPHTRNTALPRVTSRSKFLPRLAFNHTVGHIILSEHKDVKFNCSINIPNIYQDSAAISWWKDGKELLGAHHSITQFYPDDEVTAVIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYVEVQGLPHFTRQPESMNVTKNTAFNLTCQAVGPPEPVNIFWVQNSSRVNELPEKSPSVLTVPGLTETAIFSCEAHNDKGLTVSKGIQINIKAIPSPPSEVRVHNSTAHSILISWLPGFDGYSPLSDCNIQVKEVDPLSNGSVMTFNTSASPHLYRVEQLQALANYSIAMSCMNEVGWSALSRWILASTTEGAPSVAPLNVTLFLNESSNKVTVRWIEPPIKRQHGELVGYQISHEWQSAETSKELSEEAGQNSSLAQLSVQAYNATCTVRIAAVTTGGVGPFSDPVKIFIPAHGRVDFAPSSTPAPGNADPVLIILGCFCGFVLIGLVLYISLAIRKRFQETKFGSAFTEEDSELVVSYIAKKSFCRRAIELTLQSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLNQQDGTSQKVAVKTMKLDNFSHREIEEFLSEAACMKDFNHPNVIRLLGVCIEMSPQGIPKPMVILPFMKYGDLHTYLLYSRLDTGPKHIPLQTLLKFMVDIAQGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMHSCWRAEPLDRPTFSVLRLQLEKLLESLPEVRDKADVIYINTQFPESCEGLAEGSALVQLDLNIDPNSVIASCASGAAVSVVTAEVHENRAEEGRYILNGGSEGWEDQASASLAPGPAGKNGTFPEDRRGRNGASWSQSSTLPLGSPSPDGLLFADDSSEDSEVLK

Sus scrofa (Pig)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Proteomics identification;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

cell migration [GO:0016477]; establishment of localization in cell [GO:0051649]; natural killer cell differentiation [GO:0001779]; negative regulation of cytokine production [GO:0001818]; negative regulation of leukocyte apoptotic process [GO:2000107]; negative regulation of lymphocyte activation [GO:0051250]; nervous system development [GO:0007399]; neutrophil clearance [GO:0097350]; phagocytosis [GO:0006909]; platelet activation [GO:0030168]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; retina development in camera-type eye [GO:0060041]; secretion by cell [GO:0032940]; spermatogenesis [GO:0007283]; substrate adhesion-dependent cell spreading [GO:0034446]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vagina development [GO:0060068]

cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR003599;IPR013151;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;

2.60.40.10;1.10.510.10;

A0A287A5G5

MVRAKSWTLKKHFVGYPTPSNFELKTVELPPLKNGEVLLEALFLTVDPYMRIAARKLKEGDMMMGEQVARVIESKNAAFPTGTIVVALLGWTTHSISDGKNLERLLAEWPDTLPLSLALGTVGMPGLTAYFGLLDICGLKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVACLKKYGFDVAFNYKTIESLEETLKKASPEGYDCYFDNVGGEFSNAVTSQMKKFGRIAICGAISTYNRTGPPPPGPPPEVVIYNELCFQGFIVTRWQGEVRQKALRDLLKWVSEGKIQYHEHITEGFENMPAAFMGMLKGENLGKAIVKA

Sus scrofa (Pig)

1.3.1.48; 1.3.1.74

CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213; Evidence={ECO:0000256|ARBA:ARBA00023498}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374, ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590; Evidence={ECO:0000256|ARBA:ARBA00023548}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133408; Evidence={ECO:0000256|ARBA:ARBA00023544}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586; Evidence={ECO:0000256|ARBA:ARBA00023544}; CATALYTIC ACTIVITY: Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:79072, ChEBI:CHEBI:133411; Evidence={ECO:0000256|ARBA:ARBA00023543}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594; Evidence={ECO:0000256|ARBA:ARBA00023543}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208, ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133346; Evidence={ECO:0000256|ARBA:ARBA00023517}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209; Evidence={ECO:0000256|ARBA:ARBA00023517}; CATALYTIC ACTIVITY: Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112; Evidence={ECO:0000256|ARBA:ARBA00023553}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738; Evidence={ECO:0000256|ARBA:ARBA00023553}; CATALYTIC ACTIVITY: Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974; Evidence={ECO:0000256|ARBA:ARBA00023496}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205; Evidence={ECO:0000256|ARBA:ARBA00023496}; CATALYTIC ACTIVITY: Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; Evidence={ECO:0000256|ARBA:ARBA00023696}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618; Evidence={ECO:0000256|ARBA:ARBA00023696}; CATALYTIC ACTIVITY: Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH; Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748; Evidence={ECO:0000256|ARBA:ARBA00023504}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782; Evidence={ECO:0000256|ARBA:ARBA00023504}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276; Evidence={ECO:0000256|ARBA:ARBA00024160}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790; Evidence={ECO:0000256|ARBA:ARBA00024160}; CATALYTIC ACTIVITY: Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74; Evidence={ECO:0000256|ARBA:ARBA00023507}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739; Evidence={ECO:0000256|ARBA:ARBA00023507}; CATALYTIC ACTIVITY: Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH; Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455; Evidence={ECO:0000256|ARBA:ARBA00023691}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614; Evidence={ECO:0000256|ARBA:ARBA00023691}; CATALYTIC ACTIVITY: Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH; Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741; Evidence={ECO:0000256|ARBA:ARBA00023530}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786; Evidence={ECO:0000256|ARBA:ARBA00023530}; CATALYTIC ACTIVITY: Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00034052}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778; Evidence={ECO:0000256|ARBA:ARBA00034052}; CATALYTIC ACTIVITY: Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309; Evidence={ECO:0000256|ARBA:ARBA00023545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609; Evidence={ECO:0000256|ARBA:ARBA00023545};

Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome

prostaglandin metabolic process [GO:0006693]

cytoplasm [GO:0005737]

13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase (NADP+) activity [GO:0035798]

IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;

3.90.180.10;3.40.50.720;

A0A287A7V3

MASRDSASWERRDRRSMAASTLWFSLLLAAASAGRATALWPWPQYIKTSDWSYTIVPHTFQFQYHKSSAAQVGCSVLDEAFQRYRDLLFGSVTLHFRHRVEKWHISEKNSLVVLVVTPGCDQLPSLESVENYTLTINDEQCFLLSETVWGALRGLETFSQLIWKSPEGTFYINRTEIEDFPRFPHRGLLLDTSRHYLPLASILDTLDVMAYNKFNVFHWHLVDDSSFPYESFTFPDLTKKGSYNPSTHIYTARDVKEVIEYARLRGIRVLAEFDTPGHTQSWGPGVPGLLTPCYSGSQPSGTFGPVNPTLNYTYEFMSTFFSEISSVFPDFYLHLGGDEVDFTCWKSNPDIQNFMKQKGFGKDFKKLESFYIQTLLGIVSGYGKGYVVWQEVFDNKVKVRPDTIIQVWREEIPVKYMKEMELVTLAGFRALLSAPWYLNHITYGPDWKEVYMVEPLAFEGTPEQKALVIGGEACMWGEYVDSTNLVPRLWPRAGAVAERLWSNKAVTNLDFAFKRLTHFRCELLRRGVQAQPLSVGYCDVEFEQT

Sus scrofa (Pig)

3.2.1.52

CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377, ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEBI:153064; Evidence={ECO:0000256|ARBA:ARBA00023541}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64385; Evidence={ECO:0000256|ARBA:ARBA00023541}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = a beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, ChEBI:CHEBI:90164; Evidence={ECO:0000256|ARBA:ARBA00023953}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48277; Evidence={ECO:0000256|ARBA:ARBA00023953}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000256|ARBA:ARBA00001231, ECO:0000256|PIRNR:PIRNR001093}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3 (d18:1(4E)) + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47940, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:60065, ChEBI:CHEBI:71502; Evidence={ECO:0000256|ARBA:ARBA00043767}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941; Evidence={ECO:0000256|ARBA:ARBA00043767}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47968, ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:79210, ChEBI:CHEBI:79218; Evidence={ECO:0000256|ARBA:ARBA00043827}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969; Evidence={ECO:0000256|ARBA:ARBA00043827}; CATALYTIC ACTIVITY: Reaction=beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + N-acetyl-D-galactosamine; Xref=Rhea:RHEA:64372, ChEBI:CHEBI:15377, ChEBI:CHEBI:28037, ChEBI:CHEBI:152565, ChEBI:CHEBI:152566; Evidence={ECO:0000256|ARBA:ARBA00023505}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64373; Evidence={ECO:0000256|ARBA:ARBA00023505};

Disulfide bond;Glycosidase;Hydrolase;Lysosome;Proteomics identification;Reference proteome;Zymogen

adult walking behavior [GO:0007628]; carbohydrate metabolic process [GO:0005975]; cell morphogenesis involved in neuron differentiation [GO:0048667]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; lipid storage [GO:0019915]; lysosome organization [GO:0007040]; maintenance of location in cell [GO:0051651]; myelination [GO:0042552]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; sensory perception of sound [GO:0007605]; sexual reproduction [GO:0019953]; skeletal system development [GO:0001501]

azurophil granule [GO:0042582]; beta-N-acetylhexosaminidase complex [GO:1905379]; cytosol [GO:0005829]; lysosome [GO:0005764]; membrane [GO:0016020]

acetylglucosaminyltransferase activity [GO:0008375]; beta-N-acetylhexosaminidase activity [GO:0004563]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]; protein heterodimerization activity [GO:0046982]

SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.

IPR025705;IPR015883;IPR017853;IPR029018;IPR029019;

3.30.379.10;3.20.20.80;

A0A287ABK7

ESGHDGDDADGDDANDEWNVTWNTSNPDFTKCFQNTVLVWVPCSYLWVCFPFYFLYLSRHDRGYIQMTHLNKAKTALGFLLWIVCWADLFYSFWERSLGKLLAPVFLVSPTLLGVTMLLATFLIQIERRRGVQSSGIMLTFWLVALLCAIAILRSKIMTALKEDAVVVDIFRNVTFYIYFALVLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLMVQGYRQPLEITDLWSLNKEDMSEQVVPVLVKNWKKECAKSRKQPVRIVYSSKDPAKPKGGSKVDVNEEAEALIVKSPQKERDPSLFKVLYKTFGPYFLMSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYFFTALLFISACLQTLVLHQYFHICFVSGMRIKSAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMIFMVPLNAMMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKEKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALCTFAVYVTIDKNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIQRLPIKDVGTTNSITVKNATFSWARSDPPTLHGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNVSLRENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLFDDPLSAVDAHVGKHIFENVVGPKGMLKNKTRLLVTHGLSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASAEQEQGEPEDGLGGISSPGKEAKQMENGVLVTEAAGKHLQRQFSSSSSYSGDVGRHHTSTAELQKPGAQAEDTWKLMEADKAQTGQVKLSVYWDYMKAIGLFISFLSIFLFLCNHVAALVSNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGVTVFAYSMAVSIGGIFASRRLHLDLLHNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVVGACIIILLATPVAAVIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLEFVGNCIVLFAALFAVISRHNLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSDTEKEAPWRIPEVAPPSTWPQVGRVEFRDYGLRYRDDLDLVLKHINVTIDGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIVIDDVNIAQIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSEEEVWTSLELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFHDCTVLTIAHRLNTIMDYTRVIVLDKGEIREHGSPSELLQQRGLFYGMAKDAGLV

Sus scrofa (Pig)

7.6.2.2; 7.6.2.3

CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00000793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence={ECO:0000256|ARBA:ARBA00000793}; CATALYTIC ACTIVITY: Reaction=2',3'-cGAMP(in) + ATP + H2O = 2',3'-cGAMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:74887, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143093, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036427}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000256|ARBA:ARBA00024162}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001064}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952; Evidence={ECO:0000256|ARBA:ARBA00001064}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + vincristine(in) = ADP + H(+) + phosphate + vincristine(out); Xref=Rhea:RHEA:60160, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143658, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036384}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60161; Evidence={ECO:0000256|ARBA:ARBA00036384}; CATALYTIC ACTIVITY: Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+) + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64677, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148; Evidence={ECO:0000256|ARBA:ARBA00036199};

ATP-binding;Membrane;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix;Transport

cyclic nucleotide transport [GO:0070729]; export across plasma membrane [GO:0140115]; glutathione transmembrane transport [GO:0034775]; phospholipid translocation [GO:0045332]; sphingolipid translocation [GO:0099039]; transepithelial transport [GO:0070633]; xenobiotic transport [GO:0042908]; xenobiotic transport across blood-brain barrier [GO:1990962]

apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]

ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled lipid transmembrane transporter activity [GO:0034040]; carboxylic acid transmembrane transporter activity [GO:0046943]; efflux transmembrane transporter activity [GO:0015562]; glutathione transmembrane transporter activity [GO:0034634]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR003593;IPR011527;IPR036640;IPR003439;IPR017871;IPR005292;IPR027417;

1.20.1560.10;3.40.50.300;

A0A287AEZ4

MSGGGADQQSSPPGSLFLSPPAPAPKNGSSSDSSVGEKLGAAAADAGAGRTEEYRRRRHTMDKDSRGAAATTTTEHRFFRRSVICDSNATALELPGLPLPLPQPGAAAVAQQRSPPEPHREETLTPAVAHVAQQPPAAATPGEPAAAVPAAASAPGSASRDRQVAQPSQAGSKEEPPSARSGSGGGSAKEPQEERSQQQDDIEELETKAVGMSNDGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLTKSERQRFKEEGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYSIKDLLNHAFFQEETGVRVELAEEDDGEKIAIKLWLRIEDIKKLKGKYKDNEAIEFSFDLERDVPEDVAQEMVESGYVCEGDHKTMAKAIKDRVSLIKRKREQRQLVREEQEKRKQEESSLKQQGEQQSSASQAGILQPSSASTGLPAAATTSASVSTQVEPEEPEADQHQQLQYQQPSISVLSDGTVDSGQGSSVFTESRVSSQQTVSYGSQHEQAHSTCTLPGHTASVVQAQAQPHGGYPPSSMAQGQSQGQPSSSSLTGIPSSQPVQHSQQQQGVQQTAPSQQTVQYSLPQTSAPSEPTTAQPASQPQPPQVLPPVSAGKQLPVSQPVPTIQGEPQISVATQPSVVPVHSGAHFLPVGQPLPPSLLPQYPVSQVPSAPHVSAAQPGFSPLPVTAAAGVNQPLLTLASSAAAAAVPGGSTVVPSQLPTLLQPVTQLPSQAHPQLLQTAVQSMGIPANLGQTAEAPLPSGDVLYQGFPPRLPPQYPGDSNIAPSSSVASVCIPSTVLSPPRPTEALAAPGYFPTVVQSYAESNLLVPVGSIGGQIQVSQPAVSLAQAPTTSSQQAALESTQGVSQVAPPEPVPAAPPQPTQPTTLVSSIDSAHSDVASGMSDGNENVPSSSGRHEGRTIKRHYRKSVRSRSRHEKTSRPKLRILNVSNKGDRVVECQLETHNRKMVTFKFDLDGDNPEEIATIMVNNDFILAIEREAFVDQVREIIEKADEMLSEDVSVEPEGDQGLENLQGKDDYGFSGSQKLEGEFKQPIPASSMPQQIAGLPTSSLTQVVHSAGRRFIVSPVPESRLRESKVFTSEISDTVAASTSPGTGMNLSHSASSLSLQQAFSELRRAQMTEGPSTAPPHFSHTGPTFPVVPPSMSSIAGAAATPSVSVPATSCPFSDISTSVTPSEVTASTEKGIAGVATCTGVISSSGLTVPPASDSPILSSVVSSITVPVAVSVSTTSLSVQAPTPGSIVSNTGTFPSISVAMTSASAVSSTAAPGAKPPPVSSQQVSGSTAGITTLASVPTTAPAPSVASQPSLSLSSSTSAPTLAETIVVSAHSLDKASHSSTAGLALSLPASSSSASPAAGVSSSVSQPGVAHPLVIPSAVASIPVLSQAGPTCAPLLPQVPGIPPLVQPAASVPAVQQTLVHSQPQPALLPNQPHTHCPEMDADAQPRAPGIDDIKTLEEKLRSLFSEHSSSGTQHASVSLETSLVVETTVTPGIPTTAVAPGKLMTSTTSTCLPPTSLPLGTTGLSILPVVTPGQVSTPVSTIPAVKPGTAPSKPPSTKPPVLPLGTELPAGTPPSEQLPPFPGPSLMQAQQPLEDLDAQLRRTLSPETVVLTSTVGPVSVVAPTAAVEAGAQLQKDVSQVTEGPIPAPTSGTGVFQMGRFQVSVAMDDTQKEGKNKSEDVKSVHFESSTSESSVLSSSSPESTLVKPEPNGTAIHGISSDMPDSAHKTSASEAKSEAGQPTKVGRFQVTTTADKVGRFSVSRTEDAIAEAKKEGPVASPPFMDLEHSILPAVIPKKEKPELSEPSHLNGPSSDLEAAFLSRDGDDGSGSPHSPPQLCSKSLPIQSLSQSLSNSFNSSYMSSDNESDIEDEDLKLELRRLREKHLKEIQDLQSRQKHEIESLYTRLGKAPPAVIIPAAAPLAGRRRRPTKSKGSKSSRSSSLGNKSPGPGNLSGQSTATVLHPQQTLPAPGNIPETGQNQLLQPLKPSPSSDNLYSAFTSDGAISVPSLSAPGQGTSSTNTVGGTVSSQAAQAQPPTMTSSRKGTFTDDLHKLVDNWARDAMNLSGRRGSKGHMSYEGPGMARKFSAPGQLCISMTSNLGGSAPISAASATSLGHFTKSMCPPQQYGFPAPPFGTQWSGTGGPAPQPLSQFQPVGTASLQNFNISNLQKSISNPPGSNLRTT

Sus scrofa (Pig)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Transferase

cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; chemokine (C-C motif) ligand 21 signaling pathway [GO:0038116]; heart development [GO:0007507]; intracellular chloride ion homeostasis [GO:0030644]; intracellular signal transduction [GO:0035556]; lymphocyte migration into lymph node [GO:0097022]; monoatomic ion homeostasis [GO:0050801]; negative regulation of autophagy [GO:0010507]; negative regulation of cell-cell adhesion mediated by integrin [GO:0033633]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of leukocyte cell-cell adhesion [GO:1903038]; negative regulation of pancreatic juice secretion [GO:0090188]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of sodium ion transport [GO:0010766]; non-membrane-bounded organelle assembly [GO:0140694]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of mitotic cytokinesis [GO:1903490]; positive regulation of potassium ion import across plasma membrane [GO:1903288]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of T cell chemotaxis [GO:0010820]; positive regulation of termination of RNA polymerase II transcription [GO:1904595]; potassium ion homeostasis [GO:0055075]; protein insertion into ER membrane by stop-transfer membrane-anchor sequence [GO:0045050]; regulation of mRNA export from nucleus [GO:0010793]; regulation of sodium ion transmembrane transport [GO:1902305]; sodium ion transmembrane transport [GO:0035725]; T cell receptor signaling pathway [GO:0050852]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; molecular condensate scaffold activity [GO:0140693]; phosphatase binding [GO:0019902]; potassium channel inhibitor activity [GO:0019870]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR024678;IPR000719;IPR008271;

1.10.510.10;

A0A287AIV4

MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPATRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFTAAVQAMDCETHSPQVRQQFPAPIAWSGTDAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS

Sus scrofa (Pig)

2.7.11.23; 2.7.12.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00000972}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00001076}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00001687}; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000256|ARBA:ARBA00036222}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217; Evidence={ECO:0000256|ARBA:ARBA00036222};

ATP-binding;Nucleotide-binding;Nucleus;Reference proteome;Transcription;Transcription regulation

amyloid-beta formation [GO:0034205]; circadian rhythm [GO:0007623]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of DNA methylation-dependent heterochromatin formation [GO:0090310]; negative regulation of microtubule polymerization [GO:0031115]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of protein deacetylation [GO:0090312]; positive regulation of RNA splicing [GO:0033120]

axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]

ATP binding [GO:0005524]; histone H3T45 kinase activity [GO:0140857]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]; tau protein binding [GO:0048156]; transcription coactivator activity [GO:0003713]

SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.

IPR011009;IPR044131;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A287AM88

MERRAGSCLCSCLAVLALLPALSLAQYESWPHYPEYFQQPAPEYHRPQAPSDVVKIQLRLAGQKRKHSEGRLEVYYNGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNVYCTGQEATLAACSSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINNIENMNIQVEDIRIRAILSAYRKRTPVTEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMMFAARKKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPVKNVTCENGLPAVVSCVPGQVFSADGPSRFRKAYKPEQPLVRLRGGANVGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAITGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDAGVRCNIPAMGFQKKLRLNGGRNPYEGRVEVLVERNGSLVWGTVCGENWGIVEAMVVCRQLGLGFASNAFQETWYWHGNAHNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAGVACSETAPDLVLNAEIVQQSTYLEDRPMFMLQCAMEENCLAASAAQTNPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKSYECANFGEQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNYEVAESDYTNNIMKCRTRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLINNQLTSR

Sus scrofa (Pig)

FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). {ECO:0000256|RuleBase:RU367046}.

1.4.3.13

CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000256|ARBA:ARBA00036237, ECO:0000256|RuleBase:RU367046};

COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000256|ARBA:ARBA00001935, ECO:0000256|RuleBase:RU367046};

Basement membrane;Calcium;Chromatin regulator;Chromosome;Copper;Disulfide bond;Endoplasmic reticulum;Extracellular matrix;LTQ;Metal-binding;Nucleus;Oxidoreductase;Reference proteome;Repeat;Repressor;Secreted;Signal;TPQ;Transcription;Transcription regulation

collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein modification process [GO:0036211]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040]

basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]

calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720]

SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.

PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000256|RuleBase:RU367046}.

IPR001695;IPR019828;IPR001190;IPR017448;IPR036772;

3.10.250.10;

A0A287AMJ0

MTAEQRRNLHAFGDYVRKTLDPTFILSYMAPWFRDDEVQHIQAEKNNKGPTEAASLFLQFLLELQEEGWFRGFLDALNQAGYCGLCEAIESWDFQKIEKLEEYRSLLRRLQPEFKTTINPKDILPEIAECLISQECEEILQICSSKGLMAGAEKMVECLLRSDKENWPKTLKLALEKEESRFSELWMVDKGAEDVKMKDLEDDEMKTCDVQIFYKEEPENQNLSQNSCSSSAPHTYSPLKPRKYQLELALPAQNGKNTIICAPTGCGKTFVSLLICEHHLKKFPRGRKGKVVFFAIQLPVYEQQKSVFSKHFERLGYKVAGISGATSDTVCVEQIVENNDIIILTPQILVNCLTNGTIPSLSVFTLMIFDECHNTSKQHPYNVIMFNYLDRKLGGSSDSLPQVIGLTASVGVGDAKNKAEATEYICKLCASLDTSVIATVRDNLEELEEVVYKPQKFFRKVELRTTDRFKCIISQLMMEIESLAKSIFEELGTITLGGLFQIQNSNFGTQKYEQWIVKVQKECAVFQMPDKDKESRICKALFSYMSHLRIYNDALIINEHARMKDALDYLKDFFRNIRAAGFDEIEQDLTQRFEEKLQELESISIDPSNENPKLRDLCFILQEEYHLNPETRTILFVKTRALVDALKKWIKENPKLSFLKPSILTGRGKTNQNIGMTLPAQKCVLDTFRTDKDNKILITTSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTANADLIDKEKMNMYKEEMMNGAILILQTWDEAVFKEKIHQIQIREKIIRDNQGKPEPVPDKKTKKLLCKKCKAFACYTADIRMVENCHFTVVGDAFRERFVSKLHPKPKSFGNIEKRAKIYCARPDCSHDWGIYVRYKAFEMPFIKIESFVVEDIATGVQTVHAKWKDFNFEKLSFDAAEMAGGAQDLGLQGMGNLE

Sus scrofa (Pig)

3.6.4.13

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000256|ARBA:ARBA00029316}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000256|ARBA:ARBA00029316};

ATP-binding;Cytoplasm;Helicase;Hydrolase;Immunity;Innate immunity;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Repeat;RNA-binding;Zinc

antiviral innate immune response [GO:0140374]; cellular response to exogenous dsRNA [GO:0071360]; detection of virus [GO:0009597]; gene expression [GO:0010467]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of myeloid dendritic cell cytokine production [GO:0002735]; positive regulation of response to cytokine stimulus [GO:0060760]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell migration [GO:0030334]; RIG-I signaling pathway [GO:0039529]

actin cytoskeleton [GO:0015629]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; ribonucleoprotein complex [GO:1990904]; ruffle membrane [GO:0032587]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; pattern recognition receptor activity [GO:0038187]; RNA helicase activity [GO:0003724]; single-stranded RNA binding [GO:0003727]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.

IPR031964;IPR042145;IPR011545;IPR011029;IPR014001;IPR001650;IPR027417;IPR041204;IPR038557;IPR021673;

1.20.1320.30;1.10.533.10;3.40.50.300;2.170.150.30;

A0A287ANF9

MSLRSLSLWFPLLLLLLPPPPALPEDPRAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPELWTWLRTSLRPSPSFFHFLLTHGRWFWEFVNATFIRDMLMRLVLTVRSNLIPSPPTYNTAHDYISWESFSNVSYYTRILPSVPQDCPTPMGTKGKKQLPDAELLSRRFLLRRKFIPDPQGANLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYHLRLFKDGKLKYQVLNGEMYPPSVEEAPVLMHYPRGVPPRSQMAMGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWDDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAVEFNQLYHWHPLMPNSFRVGPQDYSYEQFLFNTSMLMDYGVEALVDAFSRQIAGRIGGGRNMDHHVLHVAVGLIKDSRELRLQPFNEYRKRFGLKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCLPNSIFGESMIEIGAPFSLKGLLGNPICSPQYWKASTFGGEMGFNLVKTATLRKLVCLNTKTCPYVAFRVPDLRQEDGPGVERPSTEL

Sus scrofa (Pig)

1.14.99.1

CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000256|ARBA:ARBA00000144}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000256|ARBA:ARBA00001779}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000256|ARBA:ARBA00001779}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000256|ARBA:ARBA00036409}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000256|ARBA:ARBA00036409}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000256|ARBA:ARBA00036358}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000256|ARBA:ARBA00036358}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000256|ARBA:ARBA00036313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000256|ARBA:ARBA00036313}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000256|ARBA:ARBA00035976}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000256|ARBA:ARBA00035976}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000256|ARBA:ARBA00000489};

COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970};

PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702}.

Dioxygenase;EGF-like domain;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Microsome;Oxidoreductase;Peroxidase;Prostaglandin biosynthesis;Prostaglandin metabolism;Proteomics identification;Reference proteome;Signal

cyclooxygenase pathway [GO:0019371]; regulation of blood pressure [GO:0008217]; regulation of cell population proliferation [GO:0042127]; response to oxidative stress [GO:0006979]

cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; neuron projection [GO:0043005]; photoreceptor outer segment [GO:0001750]

heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]

IPR000742;IPR019791;IPR010255;IPR037120;

1.10.640.10;2.10.25.10;

A0A287APC7

MTNPTEHSLPANSIVETQEGEFGCTVMDLRKLMELRSTDAINQINVHYGGVVNLCSRLKTNPVEGLSGNPADLEKRKQVFGQNFIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPPGEENEQCGLPVSSPEDEGEAEAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGLQNRIEKEQKFSVIRNGHIIQLPVAEIVVGDIAQIKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLERDPMLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGASEGEEGEKKKKGKKQGAPENRNKAKTQDGVALEIQPLNSQEGIDNEEKEKKAAKLPKKEKSVLQGKLTRLAVQIGKAGLIMSAITVLILILYFVIDTFVIHNRPWLAECTPIYVQYFVKFFIIGITVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYIGDTRYHQIPSPDVLVPKVLDLIVNGISINSAYTSKILPPEKEGGLPRQVGNKTECALLGFVTDLKQDYHAVRSEVPEEKLYKVYTFNSVRKSMSTVIEKPGGGYRMYSKGASEIILRKCNRILDKKGEAVPFKSKDRDEMVRTVIEPMACEGLRTICLAYRDFNDVEPLWDNESEILTELTCIAVVGIEDPVRPEVPEAIAKCKRAGITVRMVTGDNINTARAIATKCGIVTPGDDFLCLEGKEFNRLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTVGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTDSLLKRRPYGRNKPLISRTMMKNILGHAVYQLTVIFFLVFAGEKFFDIDSGRKAPLHSPPSQHYTIIFNTFVLMQLFNEINSRKIHGERNVFSGIFRNLIFCSVVLGTFISQILIVEFGGKPFSCTNLTLSQWFWCLFIGIGELLWGQVISTIPTQSLKFLKEAGHGTTKEEITKDAEGLDEIDHAEMELRRGQILWFRGLNRIQTQIDVINTFQTGASFKGVLKRQTMGQHLDVKHVPSSSYVTVAPVKSPPTTSVAAAVSSPTLGNQSGQSVP

Sus scrofa (Pig)

FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of calcium. {ECO:0000256|RuleBase:RU361146}.

7.2.2.10

CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000256|RuleBase:RU361146};

ATP-binding;Calcium;Calcium transport;Cell membrane;Ion transport;Membrane;Nucleotide-binding;Proteomics identification;Reference proteome;Translocase;Transmembrane;Transmembrane helix;Transport

calcium ion export [GO:1901660]; cellular response to acetylcholine [GO:1905145]; cellular response to epinephrine stimulus [GO:0071872]; flagellated sperm motility [GO:0030317]; negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071878]; negative regulation of angiogenesis [GO:0016525]; negative regulation of arginine catabolic process [GO:1900082]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of cellular response to vascular endothelial growth factor stimulus [GO:1902548]; negative regulation of citrulline biosynthetic process [GO:1903249]; negative regulation of gene expression [GO:0010629]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of the force of heart contraction [GO:0098736]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; positive regulation of protein localization to plasma membrane [GO:1903078]; regulation of cell cycle G1/S phase transition [GO:1902806]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of transcription by RNA polymerase II [GO:0006357]; response to hydrostatic pressure [GO:0051599]; urinary bladder smooth muscle contraction [GO:0014832]

intracellular membrane-bounded organelle [GO:0043231]; membrane raft [GO:0045121]; sperm flagellum [GO:0036126]; T-tubule [GO:0030315]; Z disc [GO:0030018]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase inhibitor activity [GO:0036487]; P-type calcium transporter activity [GO:0005388]; PDZ domain binding [GO:0030165]; protein phosphatase 2B binding [GO:0030346]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.

IPR022141;IPR006068;IPR004014;IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR006408;IPR001757;IPR044492;

3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;

A0A287AQV4

MGKEFCWMEEPSPHGQDSASRGHFFKDPGMPSETPQAEERAAGCPRLSAAHLRKGSLEKRPPGDKDTKEHLWISPDTPSRCLWQLGRPVTDSPHHHTTLAKSPQILPDILKKIGDTPMVRINKIGRRFGLKCELLAKCEFFNAGGSVKDRISLRMVEDAERAGTLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLRNEIPNSHILDQYRNASNPLAHYDITAEEILLQCNGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSVLAEPEELNQTEQTAYEVEGIGYDFIPTVLDRSVVDKWFKSNDEEAFAFARMLIAQEGLLCGGSAGSAMSVAVKAAQELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGFMKEEDLSVKKPWWWHLRVQELSLSAPLTVLPTVTCEHTIEILREKGFDQAPVVDESGVVLGMVTLGNMLSSLLAGKIQPSDQVRKVIYKQFKQIRLTDPLGKLSHILEMDHFALVVHEQIQSWDLALSGVGGGPADHSHGESSKRQMVFGVVTAIDLLNFVAARERIQKR

Sus scrofa (Pig)

4.2.1.22

CATALYTIC ACTIVITY: Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine; Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22; Evidence={ECO:0000256|ARBA:ARBA00001175, ECO:0000256|RuleBase:RU361204};

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|RuleBase:RU361204};

PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2. {ECO:0000256|ARBA:ARBA00005003}.

Amino-acid biosynthesis;CBS domain;Cysteine biosynthesis;Heme;Iron;Isopeptide bond;Lyase;Metal-binding;Pyridoxal phosphate;Reference proteome

blood vessel diameter maintenance [GO:0097746]; blood vessel remodeling [GO:0001974]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cerebellum morphogenesis [GO:0021587]; cysteine biosynthetic process from serine [GO:0006535]; cysteine biosynthetic process via cystathionine [GO:0019343]; DNA protection [GO:0042262]; endochondral ossification [GO:0001958]; homocysteine catabolic process [GO:0043418]; hydrogen sulfide biosynthetic process [GO:0070814]; L-cysteine catabolic process [GO:0019448]; L-serine catabolic process [GO:0006565]; maternal process involved in female pregnancy [GO:0060135]; regulation of nitric oxide mediated signal transduction [GO:0010749]; response to folic acid [GO:0051593]; superoxide metabolic process [GO:0006801]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

carbon monoxide binding [GO:0070025]; cystathionine beta-synthase activity [GO:0004122]; cysteine synthase activity [GO:0004124]; heme binding [GO:0020037]; L-cysteine desulfhydrase activity [GO:0080146]; modified amino acid binding [GO:0072341]; nitric oxide binding [GO:0070026]; nitrite reductase (NO-forming) activity [GO:0050421]; oxygen binding [GO:0019825]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; S-adenosyl-L-methionine binding [GO:1904047]; ubiquitin protein ligase binding [GO:0031625]

IPR046353;IPR000644;IPR046342;IPR005857;IPR001216;IPR001926;IPR036052;

3.40.50.1100;3.10.580.10;

A0A287ASP9

MASGSASKISSSNWKRSRDKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREAGSVPEGLHKEVQEAFLALHKHGCLFRDLVRIQGKDLLTPVSRLLIGNPGCTYKYLNTRLFTVPWPVKGSDAKYNEAEIGAACQTFLKLNDYLQIETIQALEELAAKEKANIDTVPVCIGPDFPRVGMGSSFDGHDEVDRKSRAAYNLTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYNYSCEGPEEESEDDPQLEGRDPDVWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGLPPRFSSTHRVAECSTGTLDYILQRCQLALQNVRDEADSGEVSLKSLEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYKKCTDWWCQPMTQLEELWKKMEGATHAVLREVRREGAPVEQSSDILTAILAVLTTRQNLRREWHARCQSRIARTLPVDQKPECRPYWEKDDPSMPLPFDLTDTVAELRGLLLEAKP

Sus scrofa (Pig)

1.14.11.53

CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6)-methyladenosine in U6 snRNA + O2 = adenosine in U6 snRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:57900, Rhea:RHEA-COMP:13573, Rhea:RHEA-COMP:13574, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; Evidence={ECO:0000256|ARBA:ARBA00000560}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in U6 snRNA + O2 = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in U6 snRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:57904, Rhea:RHEA-COMP:15030, Rhea:RHEA-COMP:15031, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:85958, ChEBI:CHEBI:85959; Evidence={ECO:0000256|ARBA:ARBA00000383}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + O2 = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:57896, Rhea:RHEA-COMP:11518, Rhea:RHEA-COMP:11519, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:85958, ChEBI:CHEBI:85959; Evidence={ECO:0000256|ARBA:ARBA00000305}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(1)-methyladenosine in tRNA + O2 = an adenosine in tRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:54576, Rhea:RHEA-COMP:10242, Rhea:RHEA-COMP:12312, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; Evidence={ECO:0000256|ARBA:ARBA00001575}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=1.14.11.53; Evidence={ECO:0000256|ARBA:ARBA00033605};

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|ARBA:ARBA00001954};

Cytoplasm;Dioxygenase;Iron;Metal-binding;Nucleus;Oxidoreductase;Reference proteome

adipose tissue development [GO:0060612]; DNA dealkylation involved in DNA repair [GO:0006307]; mRNA destabilization [GO:0061157]; oxidative single-stranded DNA demethylation [GO:0035552]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of brown fat cell differentiation [GO:0090335]; regulation of lipid storage [GO:0010883]; regulation of multicellular organism growth [GO:0040014]; regulation of respiratory system process [GO:0044065]; regulation of white fat cell proliferation [GO:0070350]; RNA repair [GO:0042245]; temperature homeostasis [GO:0001659]

cytosol [GO:0005829]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]

broad specificity oxidative DNA demethylase activity [GO:0035516]; ferrous iron binding [GO:0008198]; mRNA N6-methyladenosine dioxygenase activity [GO:1990931]; tRNA demethylase activity [GO:1990984]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.

IPR037151;IPR032868;IPR024366;IPR038413;IPR024367;

2.60.120.590;1.20.58.1470;

A0A287ATK9

MARPYICLLALAAMLLLGIATISRSRGLRDKAHQSAPRIPSQFSQEERVAMKEALKGAIQIPTVSFSPKELNTTALAEFGEYIRKVFPTVFKTSFIRHEVVGEYSHLFTVHGSDPSLQPYMLLAHIDVVPAPDEGWDVPPFSGLERNGFIYGRGTIDNKNSLMGILQALELLLIRNYIPRRSFFIALGHDEEVMGVNGAQKISALLQARGVQLAFIVDEGSFIFDGFIPGLKNPFAMVAVSQKGLINLMLQVNTTPGHSSAPPKETSIGILAAAVNRLEQTPMPNMFGDGPMKMALQELANEFSFPTNLFLSNMWLFRPLVSRLMERNYITNALVRTTTALTMFNSGIKVNVIPAVAQAIVDFRIHPAQTVQEVLKLAKDIVADDRVQFHVLNAFDPPPISPYDDQALGYQLLRQTIQSVFPEVNIVVPGTCVGNTDSRHYSNLTTGIYLFNPLYLQPQSFRLDGDHQMIERNLVESEAMGAVPTPSSL

Sus scrofa (Pig)

CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51312, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:58095, ChEBI:CHEBI:134022; Evidence={ECO:0000256|ARBA:ARBA00034626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51313; Evidence={ECO:0000256|ARBA:ARBA00034626}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51314; Evidence={ECO:0000256|ARBA:ARBA00034626}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z-octadecenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51300, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58095, ChEBI:CHEBI:134020; Evidence={ECO:0000256|ARBA:ARBA00034630}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301; Evidence={ECO:0000256|ARBA:ARBA00034630}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302; Evidence={ECO:0000256|ARBA:ARBA00034630}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992; Evidence={ECO:0000256|ARBA:ARBA00034640}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318; Evidence={ECO:0000256|ARBA:ARBA00034640}; CATALYTIC ACTIVITY: Reaction=H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L-phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L-phenylalanine; Xref=Rhea:RHEA:64132, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:77016, ChEBI:CHEBI:149701; Evidence={ECO:0000256|ARBA:ARBA00034635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64133; Evidence={ECO:0000256|ARBA:ARBA00034635}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305, ChEBI:CHEBI:59002; Evidence={ECO:0000256|ARBA:ARBA00034637}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109; Evidence={ECO:0000256|ARBA:ARBA00034637}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64110; Evidence={ECO:0000256|ARBA:ARBA00034637}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384, ChEBI:CHEBI:149697; Evidence={ECO:0000256|ARBA:ARBA00034616}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117; Evidence={ECO:0000256|ARBA:ARBA00034616}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64118; Evidence={ECO:0000256|ARBA:ARBA00034616}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + L-asparagine; Xref=Rhea:RHEA:64136, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58048, ChEBI:CHEBI:149730; Evidence={ECO:0000256|ARBA:ARBA00034627}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64137; Evidence={ECO:0000256|ARBA:ARBA00034627}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + L-glutamine; Xref=Rhea:RHEA:51356, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58359, ChEBI:CHEBI:134033; Evidence={ECO:0000256|ARBA:ARBA00034643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51357; Evidence={ECO:0000256|ARBA:ARBA00034643}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L-leucine; Xref=Rhea:RHEA:51360, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57427, ChEBI:CHEBI:134035; Evidence={ECO:0000256|ARBA:ARBA00034652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361; Evidence={ECO:0000256|ARBA:ARBA00034652}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362; Evidence={ECO:0000256|ARBA:ARBA00034652}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L-lysine; Xref=Rhea:RHEA:64192, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:32551, ChEBI:CHEBI:149731; Evidence={ECO:0000256|ARBA:ARBA00034633}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64193; Evidence={ECO:0000256|ARBA:ARBA00034633}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + L-methionine; Xref=Rhea:RHEA:64144, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57844, ChEBI:CHEBI:149732; Evidence={ECO:0000256|ARBA:ARBA00034645}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64145; Evidence={ECO:0000256|ARBA:ARBA00034645}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L-serine; Xref=Rhea:RHEA:51352, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:33384, ChEBI:CHEBI:134031; Evidence={ECO:0000256|ARBA:ARBA00034646}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51353; Evidence={ECO:0000256|ARBA:ARBA00034646}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + L-tryptophan; Xref=Rhea:RHEA:64176, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57912, ChEBI:CHEBI:149733; Evidence={ECO:0000256|ARBA:ARBA00034619}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64177; Evidence={ECO:0000256|ARBA:ARBA00034619}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L-tyrosine; Xref=Rhea:RHEA:64184, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58315, ChEBI:CHEBI:149734; Evidence={ECO:0000256|ARBA:ARBA00034625}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64185; Evidence={ECO:0000256|ARBA:ARBA00034625}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L-phenylalanine; Xref=Rhea:RHEA:64124, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:149699; Evidence={ECO:0000256|ARBA:ARBA00034620}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64125; Evidence={ECO:0000256|ARBA:ARBA00034620}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + octadecanoate; Xref=Rhea:RHEA:64128, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:58095, ChEBI:CHEBI:149700; Evidence={ECO:0000256|ARBA:ARBA00034641}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64129; Evidence={ECO:0000256|ARBA:ARBA00034641}; CATALYTIC ACTIVITY: Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14; Evidence={ECO:0000256|ARBA:ARBA00034644}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566; Evidence={ECO:0000256|ARBA:ARBA00034644}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567; Evidence={ECO:0000256|ARBA:ARBA00034644}; CATALYTIC ACTIVITY: Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824, ChEBI:CHEBI:138093; EC=3.5.1.114; Evidence={ECO:0000256|ARBA:ARBA00034622}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185; Evidence={ECO:0000256|ARBA:ARBA00034622}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186; Evidence={ECO:0000256|ARBA:ARBA00034622};

PATHWAY: Amino-acid metabolism. {ECO:0000256|ARBA:ARBA00034698}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000256|ARBA:ARBA00004872}.

Hydrolase;Metal-binding;Protease;Proteomics identification;Reference proteome;Signal;Zinc

amide biosynthetic process [GO:0043604]; amide catabolic process [GO:0043605]; amino acid metabolic process [GO:0006520]; cellular lipid metabolic process [GO:0044255]; proteolysis involved in protein catabolic process [GO:0051603]

carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; metal ion binding [GO:0046872]

IPR036264;IPR047177;IPR002933;IPR011650;

3.30.70.360;3.40.630.10;

A0A287AUI9

MEQPPAPKRIDLGPVNGNNQLAFPSWREEYDNIWSSSCKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTVSIFKFRVSVLFLFRSRDYKQRLTEEEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSVEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKSPEQRATATQLLQHPFIKNAKPVSILRDLITDAMEIKAKRHEEQQRELEEEEENSDEDELDSHTMVKTSSESVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMEYFDKQDFKNKSHENCSQNMHEPFPVSKNVFPDNWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQNF

Sus scrofa (Pig)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

Apoptosis;ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Transferase

canonical Wnt signaling pathway [GO:0060070]; cell differentiation involved in embryonic placenta development [GO:0060706]; central nervous system development [GO:0007417]; endocardium development [GO:0003157]; epithelial cell proliferation [GO:0050673]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; hepatocyte apoptotic process [GO:0097284]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of organ growth [GO:0046621]; neural tube formation [GO:0001841]; organ growth [GO:0035265]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; primitive hemopoiesis [GO:0060215]; protein import into nucleus [GO:0006606]; protein localization to centrosome [GO:0071539]; protein stabilization [GO:0050821]; protein tetramerization [GO:0051262]; regulation of cell differentiation involved in embryonic placenta development [GO:0060800]; regulation of MAPK cascade [GO:0043408]

centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR024205;IPR049568;IPR036674;IPR000719;IPR017441;IPR011524;

1.10.287.4270;4.10.170.10;1.10.510.10;

A0A287AV88

MGGRGGASWRSLGAPGHWSARLPHTCHPPMGPLPLCPPIGLSLLLLLGPGLGLSAASQRSHVHRRGLIELAGTVNCVGTRTPVAYMNYGCYCGLGGHGQPLDAIDWCCHYHDCCYKRAEDAGCSPKMDRYSWKCVDQHILCGPAQDKCQELMCKCDQAVAYCLAQTEYNIKYLFYPRFLCEKDSPKCD

Sus scrofa (Pig)

3.1.1.4

CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000256|ARBA:ARBA00001479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000256|ARBA:ARBA00001479}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000256|ARBA:ARBA00001804}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000256|ARBA:ARBA00001804}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000256|ARBA:ARBA00001855}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000256|ARBA:ARBA00001855}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000256|ARBA:ARBA00001126}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000256|ARBA:ARBA00001126}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000256|ARBA:ARBA00001129}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000256|ARBA:ARBA00001129}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000256|RuleBase:RU361236};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR601211-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR601211-2};

Calcium;Disulfide bond;Hydrolase;Lipid metabolism;Metal-binding;Reference proteome;Secreted

arachidonic acid secretion [GO:0050482]; axon guidance [GO:0007411]; defense response to virus [GO:0051607]; low-density lipoprotein particle remodeling [GO:0034374]; lysophospholipid transport [GO:0051977]; phosphatidic acid metabolic process [GO:0046473]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine metabolic process [GO:0046337]; phosphatidylglycerol metabolic process [GO:0046471]; phosphatidylserine metabolic process [GO:0006658]; phospholipid metabolic process [GO:0006644]; platelet activating factor catabolic process [GO:0062234]; positive regulation of lipid storage [GO:0010884]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of protein metabolic process [GO:0051247]; regulation of macrophage activation [GO:0043030]

extracellular space [GO:0005615]

1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]

SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361236}.

IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;

1.20.90.10;

A0A287AVR4

MPTPSAAPPQAKGFRRAVSELDAKQAEAIMSPRFVGRRQSLIQDARKEREKAEAAAAASEPGEALEVGALAERDGKALLNLLFTLRATKPPSLSRALKTFETFEAQIHHLETRPAQKPRAEAPHLEYFVRCEVPSAALPGLLSSVRRVAEDVRGTGENKVLWFPRKVSELDKCHHLVTKFDPELDLDHPGFSDQVYRQRRKLIAQIAFQYRQGDPIPRVEYTAEEIATWKEVYTTLRGLYATHACREHLEAFELLERFCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAVDVLDSPHAIRRSLEGVQDELHTLAHALSAIG

Sus scrofa (Pig)

1.14.16.2

CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; Evidence={ECO:0000256|ARBA:ARBA00033689}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18202; Evidence={ECO:0000256|ARBA:ARBA00033689};

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|ARBA:ARBA00001954, ECO:0000256|PIRSR:PIRSR601273-2};

PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000256|ARBA:ARBA00004700}.

Catecholamine biosynthesis;Cell projection;Cytoplasm;Iron;Metal-binding;Monooxygenase;Neurotransmitter biosynthesis;Oxidoreductase;Phosphoprotein;Reference proteome

dopamine biosynthetic process from tyrosine [GO:0006585]; eating behavior [GO:0042755]; embryonic camera-type eye morphogenesis [GO:0048596]; epinephrine biosynthetic process [GO:0042418]; eye photoreceptor cell development [GO:0042462]; heart development [GO:0007507]; hyaloid vascular plexus regression [GO:1990384]; learning [GO:0007612]; locomotory behavior [GO:0007626]; mating behavior [GO:0007617]; memory [GO:0007613]; norepinephrine biosynthetic process [GO:0042421]; regulation of heart contraction [GO:0008016]; response to ethanol [GO:0045471]; response to hypoxia [GO:0001666]; synaptic transmission, dopaminergic [GO:0001963]; visual perception [GO:0007601]

axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; melanosome membrane [GO:0033162]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; smooth endoplasmic reticulum [GO:0005790]; synaptic vesicle [GO:0008021]

enzyme binding [GO:0019899]; iron ion binding [GO:0005506]; tyrosine 3-monooxygenase activity [GO:0004511]

SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000256|ARBA:ARBA00004234}.

IPR045865;IPR001273;IPR018301;IPR036951;IPR036329;IPR019774;IPR041903;IPR049321;IPR005962;IPR019773;IPR021164;

3.30.70.260;1.10.800.10;

A0A287AWF4

MELSDVRCLSGSEELYTIHPTPPAGDGGSGSRPQRLLWQTAVRHITEQRFIHGHRGSGGSGSGGSGKASDPAGGGPNHHASQLSGGDSALPLYSLGPRERAHSTGGTKVFPERSGSGSGSGGGGDLGFLHLDCAPSNSDFFLSGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHTYLQYSGLVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVVLQVLIPRLAVISINQVAAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAHCCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLNGDYSVEEGHGKERNEFLRKHNIETYLIKQPEESLLSLPEDIVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLLFITAIQSLLPSSRVMPMVIQFSILIMLHSALVLITTAEDYKCLPLVLRKTCCWINETYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETIYAGLFLRYDNLNHSGEDFLGTKEASLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMQELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWEHLCALADFSLALTESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLILKDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLVQSLNRQRQKQLLNENSNPGIIKGHYNRRTLLTPSGPEPGAQAEGPDKSELP

Sus scrofa (Pig)

FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000256|PIRNR:PIRNR039050}.

4.6.1.1

CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00001593, ECO:0000256|PIRNR:PIRNR039050};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR039050}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

ATP-binding;cAMP biosynthesis;Lyase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix

adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; cellular response to glucagon stimulus [GO:0071377]; cellular response to morphine [GO:0071315]; glucose mediated signaling pathway [GO:0010255]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; neuroinflammatory response [GO:0150076]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of long-term synaptic depression [GO:1900454]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of synaptic plasticity [GO:0031915]; regulation of cellular response to stress [GO:0080135]; regulation of cytosolic calcium ion concentration [GO:0051480]

apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body membrane [GO:0032809]; postsynaptic density [GO:0014069]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR001054;IPR018297;IPR032628;IPR030672;IPR009398;IPR029787;

3.30.70.1230;

A0A287AXH1

MVLYTTPFPNSCLSALHAVSWALIFPCYWLADRLLASFIPTTYEKRQRADDPCYLQLLCTLLFTPVYLALLVASLPFAFLGFLLWSPLQSARRPYIYSRLEDKGSAGGVALLNEWKGTGPGKSFCFATANLCLLPDSLARLNNVFNTQARAKEIGQRIRNGASRPQIKIYIDSPTNTSISAASFSSLVSPQGSDGVARGVPGSIKRTASVEYKGDSGRHASDEAANGLASGDPADGGCLEDACIVRISGDEGGRPPEAIDPPAGGQARNGASGGPRGQTPNHSQQDGDSGSLGSPSASRESLVKARAGADGGSGEPGANNKLPYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCSFKCLNSGLFFASRYPIMDVAYHCYPNGRLSDSLASKGALYLKVQVGSTPQDQRIVGYISCTHLHALPEDSDIRCEQLNMLQDWLADFRKSTSSSSTANPEELVAFDIICGDFNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDKDGLYDEEVCTPDNLQKVLESEEGRREYLAFPTSKSPGGGQKGRKDLLKGNGRRIDYMLHGEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEDEA

Sus scrofa (Pig)

3.1.4.12

CATALYTIC ACTIVITY: Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-octadecyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:39923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74001, ChEBI:CHEBI:75216, ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00035963}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39924; Evidence={ECO:0000256|ARBA:ARBA00035963}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00000008}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence={ECO:0000256|ARBA:ARBA00000008}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexadecanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-hexadecanoylsphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72959, ChEBI:CHEBI:78646, ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00023739}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45645; Evidence={ECO:0000256|ARBA:ARBA00023739}; CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000256|ARBA:ARBA00023999}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000256|ARBA:ARBA00023999}; CATALYTIC ACTIVITY: Reaction=a sphingosylphosphocholine + H2O = a sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84410, ChEBI:CHEBI:85171, ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00036120}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45297; Evidence={ECO:0000256|ARBA:ARBA00036120}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine + H2O = an N-acyl-sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64583, ChEBI:CHEBI:83273, ChEBI:CHEBI:295975; Evidence={ECO:0000256|ARBA:ARBA00036372}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45301; Evidence={ECO:0000256|ARBA:ARBA00036372};

PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004760}.; PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.

Lipid metabolism;Membrane;Reference proteome;Sphingolipid metabolism;Transmembrane;Transmembrane helix

BMP signaling pathway [GO:0030509]; bone growth [GO:0098868]; bone mineralization [GO:0030282]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to magnesium ion [GO:0071286]; cellular response to oxidised low-density lipoprotein particle stimulus [GO:0140052]; cellular response to peptide [GO:1901653]; cellular response to redox state [GO:0071461]; cellular response to tumor necrosis factor [GO:0071356]; ceramide metabolic process [GO:0006672]; chondrocyte development involved in endochondral bone morphogenesis [GO:0003433]; collagen metabolic process [GO:0032963]; dentinogenesis [GO:0097187]; DNA biosynthetic process [GO:0071897]; endochondral ossification [GO:0001958]; extracellular matrix assembly [GO:0085029]; G1 to G0 transition [GO:0070314]; hematopoietic progenitor cell differentiation [GO:0002244]; lung alveolus development [GO:0048286]; mitotic nuclear division [GO:0140014]; multicellular organism growth [GO:0035264]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; peptide hormone secretion [GO:0030072]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; polysaccharide transport [GO:0015774]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of smooth muscle cell proliferation [GO:0048661]; regulation of cartilage development [GO:0061035]; regulation of leukocyte migration [GO:0002685]; regulation of protein phosphorylation [GO:0001932]; sphingolipid mediated signaling pathway [GO:0090520]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684]

cytoplasm [GO:0005737]; extracellular region [GO:0005576]; Golgi cis cisterna [GO:0000137]; plasma membrane [GO:0005886]

identical protein binding [GO:0042802]; neutral sphingomyelin phosphodiesterase activity [GO:0061751]; phosphatidic acid binding [GO:0070300]; phosphatidylserine binding [GO:0001786]; sphingomyelin phosphodiesterase activity [GO:0004767]

IPR036691;IPR005135;IPR038772;IPR017766;

3.60.10.10;

A0A287AXV6

MNMSVLTLQEYEFEKQFNENEAIQWMQENWKKSFLVSALYAAFIFGGRHVMNKRAKFELRKPLVLWSLSLAVFSIFGALRTGAYMLYILMTKGLKYSVCDQGFYNGPVSKFWAYAFVLSKAPELGDTIFIILRKQKLIFLHWYHHITVLLYSWYSYKDMVAGGGWFMTMNYGVHSVMYSYYALRAAGFRVSRKFAMFITLSQITQMLVGCVVNYLVFHWMQQDQCYSHFPNIFWSSLMYLSYLVLFCHFFFEAYIGKMRKTTKAD

Sus scrofa (Pig)

FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03206}.

2.3.1.199

CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555; Evidence={ECO:0000256|ARBA:ARBA00001297}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676; Evidence={ECO:0000256|ARBA:ARBA00001297}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; Evidence={ECO:0000256|ARBA:ARBA00001347}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512; Evidence={ECO:0000256|ARBA:ARBA00001347}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012; Evidence={ECO:0000256|ARBA:ARBA00000592}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504; Evidence={ECO:0000256|ARBA:ARBA00000592}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034, ChEBI:CHEBI:74054; Evidence={ECO:0000256|ARBA:ARBA00001158}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524; Evidence={ECO:0000256|ARBA:ARBA00001158}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57384, ChEBI:CHEBI:71407; Evidence={ECO:0000256|ARBA:ARBA00001211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316; Evidence={ECO:0000256|ARBA:ARBA00001211}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57349, ChEBI:CHEBI:57384, ChEBI:CHEBI:57385; Evidence={ECO:0000256|ARBA:ARBA00001634}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168; Evidence={ECO:0000256|ARBA:ARBA00001634}; CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000256|HAMAP-Rule:MF_03206, ECO:0000256|RuleBase:RU361115}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetradecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:60140, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:57384, ChEBI:CHEBI:62543; Evidence={ECO:0000256|ARBA:ARBA00001237}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60141; Evidence={ECO:0000256|ARBA:ARBA00001237};

PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03206}.

Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Glycoprotein;Lipid biosynthesis;Lipid metabolism;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix

fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty acid biosynthetic process [GO:0042759]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of cold-induced thermogenesis [GO:0120162]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]

fatty acid elongase complex [GO:0009923]

fatty acid elongase activity [GO:0009922]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03206}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03206}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

PTM: N-Glycosylated. {ECO:0000256|HAMAP-Rule:MF_03206}.

IPR030457;IPR002076;IPR033675;

A0A287AYB4

MGTSHRMLLVLGCLFTGPSLILCQLSLPSILPNENEKVVQLNASFSLRCFGESEVSWQYPMSEEENPSVEIRSEENNSGLFVTVLEVVSASAAHTGLYTCYYNHTQREESEIEGRAIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLLSDGVVHASYDSRQGFNGTFTVGPYICEATVRGKKFQTIPFNVYALKATSELDLEMEALKTVYKAGESIVVTCAVFNNEVVDLQWTYPGQVKGKGITMLEETKVPSIKLVYTLMVPEATVKDSGDYECAARQATREVKEMKKVTISVHERGFIEIKPNFSPLEAVNLHEVRHFVVDVQAYPPPRIAWLKDNLTLTENLTEITTDIERIQEIRYRSKLKLIRAKEEDSGHYTIVVQNEDDVKSYTFELLTQVPSSILDLVDDHHGSNGEQTVRCTAEGTPLPDIEWMICKDIKKCNNETSWTILANNVSNIITEIHPRDRSTVEGQVTFAKVEETVAVRCLAKNLLGVESRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSRHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDNSDGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL

Sus scrofa (Pig)

FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development. {ECO:0000256|PIRNR:PIRNR500950}.

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Cell membrane;Chemotaxis;Developmental protein;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

adrenal gland development [GO:0030325]; cardiac myofibril assembly [GO:0055003]; cell chemotaxis [GO:0060326]; cellular response to amino acid stimulus [GO:0071230]; cellular response to reactive oxygen species [GO:0034614]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic digestive tract morphogenesis [GO:0048557]; estrogen metabolic process [GO:0008210]; extracellular matrix organization [GO:0030198]; face morphogenesis [GO:0060325]; hematopoietic progenitor cell differentiation [GO:0002244]; in utero embryonic development [GO:0001701]; Leydig cell differentiation [GO:0033327]; lung development [GO:0030324]; luteinization [GO:0001553]; male genitalia development [GO:0030539]; metanephric glomerular capillary formation [GO:0072277]; negative regulation of platelet activation [GO:0010544]; odontogenesis of dentin-containing tooth [GO:0042475]; phosphorylation [GO:0016310]; platelet aggregation [GO:0070527]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway [GO:0038091]; positive regulation of chemotaxis [GO:0050921]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of mesenchymal stem cell differentiation [GO:2000739]; retina vasculature development in camera-type eye [GO:0061298]; roof of mouth development [GO:0060021]; signal transduction involved in regulation of gene expression [GO:0023019]; white fat cell differentiation [GO:0050872]

cell junction [GO:0030054]; cilium [GO:0005929]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; microvillus [GO:0005902]; nucleoplasm [GO:0005654]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; metal ion binding [GO:0046872]; platelet-derived growth factor alpha-receptor activity [GO:0005018]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor binding [GO:0005161]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; vascular endothelial growth factor binding [GO:0038085]; vascular endothelial growth factor receptor activity [GO:0005021]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|PIRNR:PIRNR500950}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|PIRNR:PIRNR500950}. Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}.

IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR011009;IPR027290;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR001824;

2.60.40.10;1.10.510.10;

A0A287AYN9

MKGDRTIPIGEGTGKEEGPSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELVLRGSSRRLDLLHQQLQELHAHVVLPDPAATAHDAPQSPGAGGPTCSATNLSLVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQACQLESQAAPDEAQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAPKTPDRKALSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAATSAAFSARLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPSPSVGGPGTPESRTPFLSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNTWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNPSAIGTFSPGASPGPEARSTGDISVEKLNLGTDLDGSPQKSPLGPPSSPSSLSSPIQETSTTPQLPSETQETPGPTLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAISIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWDALLARRLPPPFVPTLSGRTDVSNFDEEFTGESPTLSPPRDARPLTATEQAAFRDFDFVAGSC

Sus scrofa (Pig)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};

ATP-binding;Coiled coil;Cytoplasm;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Proteomics identification;Reference proteome;Repeat;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase

B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; epithelial cell migration [GO:0010631]; hyperosmotic response [GO:0006972]; intracellular signal transduction [GO:0035556]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of protein phosphorylation [GO:0001933]; phosphorylation [GO:0016310]; post-translational protein modification [GO:0043687]; regulation of cell motility [GO:2000145]; regulation of germinal center formation [GO:0002634]; regulation of immunoglobulin production [GO:0002637]; regulation of transcription by RNA polymerase II [GO:0006357]; renal system process [GO:0003014]; spleen development [GO:0048536]

cleavage furrow [GO:0032154]; endosome [GO:0005768]; midbody [GO:0030496]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; histone H3T11 kinase activity [GO:0035402]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR000008;IPR035892;IPR037784;IPR011072;IPR036274;IPR011009;IPR017892;IPR037317;IPR037313;IPR000719;IPR017441;IPR008271;

1.10.287.160;1.10.510.10;

A0A287AZD5

MSPWQPLVLVLLVLGCSAAPKPRQPTFVVFPGDLRTNLSDRQLAEEYLYRYGYTQVAEMTDRKQSLEPALKLLQQRLSLPQTGELDTTTLNAMRAPRCGVPDLGKFQTFEGDLKWHHHDITYWIQNYSEDLPRDVIDDAFARAFALWSEVTPLNFTRVYGPNADIVIQFGVKEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDEELWSLGKGVVVPTYFGNAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDTDRQFGFCPSERLFTRDGNADGKPCVFPFTFEGRSYSSCTTDGRSDGYRWCGTTANYDQDKLYGFCPTRADSTVTGGNSAGDLCVFPFTFLGKEYSACTREGRSDGHLWCATTSNFDKDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSTVPEALMYPMYSFTEEHPLHEDDVRGIQYLYGSRPKPEPRPPTTTTAEPQSTVPPTVCVTGPPTTRPSERSTAGPTGPPSAGPTGPPTAGPSAAPTVSLGPGEDICNVDIFDAIAEIRNRLHFFKDGKYWRLSEGKEHRVQGPFLIKDRWPALPHKLDSAFEEPLSKKIFFFSGRQVWVYTGASVLGPRRLDKLGLGPEVARVTGALPREAGKVLLFSQQNFWRFDVKTQKVDSRSATRVDQMFPGVPLNTHDIFQYQEKAYFCQARFFWRVSSRNEVNQVDYVGYVTFDLLKCPED

Sus scrofa (Pig)

3.4.24.35

CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence={ECO:0000256|ARBA:ARBA00001425};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-2};

Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen

apoptotic process [GO:0006915]; cell migration [GO:0016477]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; embryo implantation [GO:0007566]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; negative regulation of epithelial cell differentiation involved in kidney development [GO:2000697]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; positive regulation of apoptotic process [GO:0043065]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of keratinocyte migration [GO:0051549]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; proteolysis [GO:0006508]; response to amyloid-beta [GO:1904645]; skeletal system development [GO:0001501]

extracellular matrix [GO:0031012]; extracellular space [GO:0005615]

identical protein binding [GO:0042802]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.

IPR000562;IPR036943;IPR000585;IPR036375;IPR018487;IPR018486;IPR013806;IPR033739;IPR024079;IPR001818;IPR021190;IPR021158;IPR006026;IPR002477;IPR036365;

3.40.390.10;2.10.10.10;2.110.10.10;

A0A287B440

MAQDDSRQRDAGRIKNAFLSFEETGSANSSPKDMDENESNQSLMTSSQYSKESVRKRQDSRNSGGSDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNLSIPSVLRWLIMEKDHSSVPCSKEELDKELPVLRPYFIRDPEDAGVREAALRVTWLGHATVMVEMDELIFLTDPVFSARASPSQHMGPKRFRRPPCSIGELPRIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCSAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQTKRSVAIHWGTFALANEHYLEPPVKLSEALERYGLKTEDFFVLKHGESRYLNTDDENFE

Sus scrofa (Pig)

3.1.4.54

CATALYTIC ACTIVITY: Reaction=1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:56464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:138663, ChEBI:CHEBI:140452; Evidence={ECO:0000256|ARBA:ARBA00044474}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56465; Evidence={ECO:0000256|ARBA:ARBA00044474}; CATALYTIC ACTIVITY: Reaction=H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(9Z-octadecenoyl) ethanolamine; Xref=Rhea:RHEA:45532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71466, ChEBI:CHEBI:74546, ChEBI:CHEBI:85291; Evidence={ECO:0000256|ARBA:ARBA00023539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45533; Evidence={ECO:0000256|ARBA:ARBA00023539}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-3-phosphate + an N-acylethanolamine + H(+); Xref=Rhea:RHEA:53164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:52640, ChEBI:CHEBI:57970, ChEBI:CHEBI:85216; Evidence={ECO:0000256|ARBA:ARBA00023521}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53165; Evidence={ECO:0000256|ARBA:ARBA00023521}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:45596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:72860, ChEBI:CHEBI:85334; Evidence={ECO:0000256|ARBA:ARBA00023516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45597; Evidence={ECO:0000256|ARBA:ARBA00023516}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-sn-glycero-3-phosphate + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:45592, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:71464, ChEBI:CHEBI:85335; Evidence={ECO:0000256|ARBA:ARBA00023492}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45593; Evidence={ECO:0000256|ARBA:ARBA00023492}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine; Xref=Rhea:RHEA:45528, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546, ChEBI:CHEBI:85277; Evidence={ECO:0000256|ARBA:ARBA00023540}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45529; Evidence={ECO:0000256|ARBA:ARBA00023540}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine; Xref=Rhea:RHEA:56548, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:140532; Evidence={ECO:0000256|ARBA:ARBA00023542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56549; Evidence={ECO:0000256|ARBA:ARBA00023542}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine; Xref=Rhea:RHEA:45544, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74544, ChEBI:CHEBI:85223; Evidence={ECO:0000256|ARBA:ARBA00023561}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545; Evidence={ECO:0000256|ARBA:ARBA00023561}; CATALYTIC ACTIVITY: Reaction=H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-butanoyl ethanolamine; Xref=Rhea:RHEA:45620, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85298, ChEBI:CHEBI:85304; Evidence={ECO:0000256|ARBA:ARBA00023528}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45621; Evidence={ECO:0000256|ARBA:ARBA00023528}; CATALYTIC ACTIVITY: Reaction=H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-decanoyl ethanolamine; Xref=Rhea:RHEA:45608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85295, ChEBI:CHEBI:85301; Evidence={ECO:0000256|ARBA:ARBA00023560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45609; Evidence={ECO:0000256|ARBA:ARBA00023560}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-dodecanoylethanolamine; Xref=Rhea:RHEA:45556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546, ChEBI:CHEBI:85263, ChEBI:CHEBI:85294; Evidence={ECO:0000256|ARBA:ARBA00023499}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45557; Evidence={ECO:0000256|ARBA:ARBA00023499}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:45540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:74546, ChEBI:CHEBI:78097; Evidence={ECO:0000256|ARBA:ARBA00023534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45541; Evidence={ECO:0000256|ARBA:ARBA00023534}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-hexanoyl ethanolamine; Xref=Rhea:RHEA:45616, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85297, ChEBI:CHEBI:85303; Evidence={ECO:0000256|ARBA:ARBA00023523}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45617; Evidence={ECO:0000256|ARBA:ARBA00023523}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-octadecanoyl ethanolamine; Xref=Rhea:RHEA:45536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546, ChEBI:CHEBI:85292, ChEBI:CHEBI:85299; Evidence={ECO:0000256|ARBA:ARBA00023524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45537; Evidence={ECO:0000256|ARBA:ARBA00023524}; CATALYTIC ACTIVITY: Reaction=H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-octanoyl ethanolamine; Xref=Rhea:RHEA:45612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85296, ChEBI:CHEBI:85302; Evidence={ECO:0000256|ARBA:ARBA00023500}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45613; Evidence={ECO:0000256|ARBA:ARBA00023500}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-tetradecanoylethanolamine; Xref=Rhea:RHEA:45552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546, ChEBI:CHEBI:85262, ChEBI:CHEBI:85293; Evidence={ECO:0000256|ARBA:ARBA00023547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45553; Evidence={ECO:0000256|ARBA:ARBA00023547};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR038896-51}; Note=Binds 2 zinc divalent cations per subunit. {ECO:0000256|PIRSR:PIRSR038896-51};

Lipid degradation;Lipid metabolism;Metal-binding;Phospholipid degradation;Phospholipid metabolism;Reference proteome;Zinc

host-mediated regulation of intestinal microbiota composition [GO:0048874]; N-acylethanolamine metabolic process [GO:0070291]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; phospholipid catabolic process [GO:0009395]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of inflammatory response [GO:0050729]; temperature homeostasis [GO:0001659]

cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; Golgi membrane [GO:0000139]; membrane-bounded organelle [GO:0043227]

bile acid binding [GO:0032052]; identical protein binding [GO:0042802]; N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity [GO:0102200]; N-acylphosphatidylethanolamine-specific phospholipase D activity [GO:0070290]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.

IPR001279;IPR024884;IPR036866;

3.60.15.10;

A0A287B4X9

MALPSLLLLVAALAGGVRPPGPRNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRALPVDLRFVSSELDGACSEYLAPLRAVDLKLYHDPDLLLGPGCVYPAASVARFASHWRLPLLTAGAVASGFSAKNEHYRTLVRTGPSAPKLGEFVVMLHGHFNWTARAALLYLDARTDDRPHYFTIEGVFEALQGSNLSVQHQVYAREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQAQRENLTNGDYVFFYLDVFGESLRAGPTRSTGRPWQDNHTREQAQALREAFQTVLVITYREPPNPEYQEFQNRLLIRAREDFGVELAPSLMNLIAGCFYDGILLYAEVLNETIQEGGTREDGLRIVEKMQGRRYHGVTGLVVMDKNNDRETDFVLWAMGDLDSGDFQPAAHYSGAEKQIWWTGRPIPWVKGAPPLDNPPCAFDLDDPSCDKTPLSTLAIVALGTGITFIMFGVSSFLIFRKLMLEKELASMLWRIRWEELQFGNSERYHKGAGSRLTLSLRGSSYGSLMTAHGKYQIFANTGHFKGNVVAIKHVNKKRIELTRQVLFELKHMRDVQFNHLTRFIGACIDPPNICIVTEYCPRGSLQDILENDSINLDWMFRYSLINDLVKGMAFLHNSIIASHGSLKSSNCVVDSRFVLKITDYGLASFRSTAEPDDSHALYAKKLWTAPELLSGNPLPTTGMQKADVYSFGIILQEIGLRSGPFYLEGLDLSPKEIVQKVRNGQRPYFRPSIDRTQLNEELVMLMERCWAQDPAERPDFGQIKGFIRRFNKEGGTSILDNLLLRMEQYANNLEKLVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNFDVYKVETIGDAYMVVSGLPGRNGQRHAPEIARMALALLDAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGQALKIHVSSTTKDALDELGCFQLELRGDVEMKGKGKMRTYWLLGERKGPAGLL

Sus scrofa (Pig)

FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. {ECO:0000256|ARBA:ARBA00043880}.

4.6.1.2

CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000256|RuleBase:RU003431};

cGMP biosynthesis;Coiled coil;Lyase;Membrane;Osteogenesis;Reference proteome;Signal;Transmembrane;Transmembrane helix

activation of meiosis involved in egg activation [GO:0060466]; axonogenesis involved in innervation [GO:0060385]; blood circulation [GO:0008015]; blood vessel remodeling [GO:0001974]; c-di-GMP signaling [GO:0061939]; cellular response to cGMP [GO:0071321]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to peptide [GO:1901653]; cGMP biosynthetic process [GO:0006182]; chemical synaptic transmission [GO:0007268]; chondrocyte differentiation [GO:0002062]; chondrocyte proliferation [GO:0035988]; chromosome organization [GO:0051276]; collateral sprouting [GO:0048668]; cumulus cell differentiation [GO:0001549]; digestive tract morphogenesis [GO:0048546]; endochondral ossification [GO:0001958]; epidermal growth factor receptor signaling pathway [GO:0007173]; execution phase of apoptosis [GO:0097194]; female genitalia development [GO:0030540]; gastric emptying [GO:0035483]; genitalia morphogenesis [GO:0035112]; growth plate cartilage development [GO:0003417]; limb morphogenesis [GO:0035108]; lymph vessel development [GO:0001945]; MAPK cascade [GO:0000165]; meiotic cell cycle process involved in oocyte maturation [GO:1903537]; multicellular organism growth [GO:0035264]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of oocyte maturation [GO:1900194]; neuron apoptotic process [GO:0051402]; neuronal action potential [GO:0019228]; post-anal tail morphogenesis [GO:0036342]; receptor guanylyl cyclase signaling pathway [GO:0007168]; response to fibroblast growth factor [GO:0071774]; response to luteinizing hormone [GO:0034699]; response to salt [GO:1902074]; sensory perception of sound [GO:0007605]; smooth muscle tissue development [GO:0048745]; spermatogenesis [GO:0007283]; startle response [GO:0001964]; vacuole organization [GO:0007033]; vascular wound healing [GO:0061042]; vasculogenesis [GO:0001570]; vestibulocochlear nerve maturation [GO:0021647]; white fat cell differentiation [GO:0050872]

cilium [GO:0005929]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; guanylate cyclase activity [GO:0004383]; identical protein binding [GO:0042802]; natriuretic peptide receptor activity [GO:0016941]; peptide hormone binding [GO:0017046]; protein kinase activity [GO:0004672]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR001054;IPR018297;IPR001828;IPR001170;IPR011009;IPR029787;IPR028082;IPR000719;IPR001245;

3.40.50.2300;3.30.70.1230;1.10.510.10;

A0A287B575

MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGPEGRRKRRPGITVENLLCLDNAVWKEFSEEWTSELRPGRPKGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEFKTDWACRVPRNFFFPLSWVGGKGVTPLPLVWLLSGQLPTPGEALETTSGS

Sus scrofa (Pig)

FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. {ECO:0000256|PIRNR:PIRNR037913}.

3.5.1.98

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000256|ARBA:ARBA00029357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173; Evidence={ECO:0000256|ARBA:ARBA00029357}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000256|ARBA:ARBA00029372}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000256|ARBA:ARBA00029372}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; Evidence={ECO:0000256|ARBA:ARBA00029349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109; Evidence={ECO:0000256|ARBA:ARBA00029349};

Chromatin regulator;Hydrolase;Metal-binding;Nucleus;Reference proteome;Repressor;Transcription;Transcription regulation

cellular response to fluid shear stress [GO:0071498]; circadian regulation of gene expression [GO:0032922]; cornified envelope assembly [GO:1903575]; DNA repair-dependent chromatin remodeling [GO:0140861]; establishment of mitotic spindle orientation [GO:0000132]; establishment of skin barrier [GO:0061436]; in utero embryonic development [GO:0001701]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of JNK cascade [GO:0046329]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of TOR signaling [GO:0032008]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian rhythm [GO:0042752]; regulation of mitotic cell cycle [GO:0007346]; regulation of multicellular organism growth [GO:0040014]; regulation of protein stability [GO:0031647]; spindle assembly [GO:0051225]; transcription by RNA polymerase II [GO:0006366]

cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Rpd3L-Expanded complex [GO:0070210]; transcription repressor complex [GO:0017053]

chromatin DNA binding [GO:0031490]; cyclin binding [GO:0030332]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone decrotonylase activity [GO:0160009]; metal ion binding [GO:0046872]; NF-kappaB binding [GO:0051059]; protein de-2-hydroxyisobutyrylase activity [GO:0160010]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037913}.

IPR000286;IPR003084;IPR023801;IPR037138;IPR023696;

3.40.800.20;

A0A287B896

MKQLPPQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPIFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSLTKKTLQNRFLTALGNEKQNDMPNSPAVPLQVDSTPKIKTDIGDTLSTTEESSPPKSRVELGKIHFKKHLLHVTSRPLLTTTTAVTSPPPPILPLPAVVAESTTVDSPPSSPPPPPPPPQAPAPSSPAPITEPVALPHTPVTVLMTAPVNVAARALKEPPVIIVPESSEVDTKPYTVSNSSEEHITHNLSEQADIPSQKEDSHIGKEEEMPDSSKSSLGSKKTGSRKKSSQSEGTFLGSESDEDSIRTSSSQKSHDLKYSANIEKERDSKKNLAPLKSEDLGKSSRSKTERDDKYFSYSKLERDTRYISSRCRSERERRRSRSRSRSERGSRSSLSYSRSERSHYYDSDRRYHRSSPYRERARYSRLYTDNRARESSDSEDEYKKTYSRRTSSHSSSYRDLRTSSSYSKSDRDCKTESSYLEMEKRGKYSSKLERESKRTSENESVKRCCSPPNELGFRRGSSYSKHDTSASRYKSAPSRPIPKTDKFKNSFCCTELNEEIRQSHSFGLQTPCSKGSELRMISKVPEKEKTESPSPSNRLNDSPTFKKLDESPIFKSEFIGRDSHDSIKELDSLCKVKNDQLKSYCSTELNVNGSPGVESDLATFCTSKTDTVLMSSDDSVTGLEVSPLVKACMISSNGFQNINRCKEKDNTCIQHTRSGSPFRETESLLLPHQDKLMCLPVDYSNTVVKEPVDMRVSCCKTKDSDIYCTSNDSRPSLCHSEAENTEPLVTKISSNSFMDMHLKSKTVICDNRNLTDQHSKFACGEYKQSVGSTSSASINHFDNLYQSAGSSCIASSLQTLPPGIKVDSLPLLQCGDNTSPVLDAVLKSKSTEFLKHAEKETSIEVDGGLPDSGRGFASWENRHNNGLSGKCVQERQEEGNSILPDRKGRPEVSLDEEGGRGHAHTSDDSEVVFSSCDLNLTMEDSDGVTYTLKCDSSGHASEIVSTVHEDYSGSSESSSDESDSEDTDSDDSSIPRNRLQSVVVVPKNSTLPMEETSPCSSRSSQSYRHYSDHWEDERLETRRHSYEEKFESITSKSCAQTEKFFLHKGTEKNPEISFTHPSRKQVDNHLPEITHPQSDGVDSTSHTDVKSDSLGRPNSEEMVKAKIASRQQEELPVYSSDDFEDVPNKSRQQATFPKRPDSRLGKTELNFSSCEISRVDGFRSSEELRNLGWDFSHQEKPTTTYQQPDSSYGSCGGHKYQQNTEQYGGTRNYWQGNGYWDPRSAGRPPGTGVVYDQIQGQVPDSLTDDREEEENWDQHGGSHFSNQSNKFFLSLQKDKGTVQAPEISSNSIKDSLAVNEKKDLSKNLERNDMKDRGPLKKRRQELDSESESDSELQDRKKVRVEVEQGETAVPLGSALVGPSCVMEDFRDPQRWKEYAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSRLMVRIETLEQKLTCLKLIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEIIKTLEHLPIPTKNMLEESKVLPVIQRWSQTKTAVPQLSEGDGYSSENTSRAHTPLNTPDPSTKLSTEADIDTPKKVALRKLKIISENSMDSAISDATSELEGKDGKEDLDQLENVHVEEEEELQSQQLLTQQLPESKVDSEIAVEGSKLPTSEPEPDTEIEPKESNGTKLDEPIAEETPSQDEEEGVSDVESERSQEQPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKESTITERGRDAVGFRDQTVAPKTPNRSRERDPDKQTQNKEKRKRRGSLSPPSSAYERGTKRPDDRYDTPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPYDSLGYNAPHHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHSQPLVGHSTEALAAPPPVPVVPHVAAPVEVSSSQYVAQSDGVVHQDSSVNVLPVPAPGPVQGQNYGVWDSNQQSVSVQQQYSPAQSQAIYYQGQTCPAVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAHPQGVVVQPTAAVTTIVAPGQPQPLQPPEMVVTNNLLDLPPPSPPKPKTIILPPNWKTARDPEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKTSKKPKTAEADTSSELAKKSKEIFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKELKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE

Sus scrofa (Pig)

2.1.1.359

CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359; Evidence={ECO:0000256|ARBA:ARBA00000317};

Chromatin regulator;Chromosome;Methyltransferase;Nucleus;Reference proteome;S-adenosyl-L-methionine;Transcription;Transcription regulation;Transferase

angiogenesis [GO:0001525]; cell migration involved in vasculogenesis [GO:0035441]; coronary vasculature morphogenesis [GO:0060977]; defense response to virus [GO:0051607]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic placenta morphogenesis [GO:0060669]; endodermal cell differentiation [GO:0035987]; forebrain development [GO:0030900]; mesoderm morphogenesis [GO:0048332]; methylation [GO:0032259]; microtubule cytoskeleton organization involved in mitosis [GO:1902850]; mismatch repair [GO:0006298]; morphogenesis of a branching structure [GO:0001763]; neural tube closure [GO:0001843]; nucleosome organization [GO:0034728]; pericardium development [GO:0060039]; positive regulation of autophagy [GO:0010508]; positive regulation of interferon-alpha production [GO:0032727]; regulation of cytokinesis [GO:0032465]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of gene expression [GO:0010468]; regulation of mRNA export from nucleus [GO:0010793]; regulation of protein localization to chromatin [GO:1905634]; response to type I interferon [GO:0034340]; stem cell development [GO:0048864]; transcription elongation by RNA polymerase II [GO:0006368]

chromosome [GO:0005694]; nucleus [GO:0005634]

alpha-tubulin binding [GO:0043014]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]

SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR006560;IPR003616;IPR001214;IPR046341;IPR044437;IPR042294;IPR013257;IPR038190;IPR035441;IPR001202;IPR036020;

2.20.70.10;1.20.930.10;2.170.270.10;1.10.1740.100;

A0A287BAJ5

MVFQTRHPSWIILCYIWLLRFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIIENLAIFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGSSRCDCEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSVTTGQAAPSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRERTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNYSPRLDVATLEEATGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKERAERPKFEQIVGILDKMIRNPNSLKTPLGTCSRPISPLLDQNTPDFTTFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV

Sus scrofa (Pig)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Disulfide bond;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

axon guidance [GO:0007411]; brain development [GO:0007420]; branching morphogenesis of a nerve [GO:0048755]; ephrin receptor signaling pathway [GO:0048013]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of synapse assembly [GO:0051964]; nephric duct morphogenesis [GO:0072178]; neuron apoptotic process [GO:0051402]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell-cell adhesion [GO:0022407]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of postsynapse organization [GO:0099175]; regulation of protein autophosphorylation [GO:0031952]; retinal ganglion cell axon guidance [GO:0031290]

dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; chemorepellent activity [GO:0045499]; GPI-linked ephrin receptor activity [GO:0005004]; growth factor binding [GO:0019838]; transmembrane-ephrin receptor activity [GO:0005005]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR027936;IPR034283;IPR001090;IPR003961;IPR036116;IPR008979;IPR009030;IPR013783;IPR011009;IPR000719;IPR017441;IPR001660;IPR013761;IPR001245;IPR011641;IPR008266;IPR020635;IPR016257;IPR001426;

2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;

A0A287BB27

MGQQPGKVLGDQRRPSLPALHFIKGAGKKDSSRHGGPHCNVFVEHEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTRNGQGWVPSNYVTPVSSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKKGMRGAASPLLQAPELPTKTRTARRAAEHKDAPDVPETPHSKGPGETDPPDHEPAVSPLLPRKERGPQDGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAVEDEGREASNGALALAPSDAAEPAKSPKPSGGAGVPNGAFRESGGAGFRSPHLWKKSSTLTSSRLAASEEESGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRASENRSDQVTRGTVTPPPRLAKKTEEEADEVFRDTAESSPGSSPPTLTPKLLRRQVPSSSSLPHKEDAGKCSALGAPAEPGPPTSRAGPGASGGPSKAPGEESRVRRHKPASESPGRDKGKLSKLKPAPPPPPPASVGKVGKSSQSPSQEAAGEVGPSGKAKPAALAVDAVNSDAAKPSQLGDGVKKPVLPSVPKPQSSTKPAGTPTSPASAPCTLPTASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGMVLDGTEALCLAVSRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENSLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR

Sus scrofa (Pig)

2.7.10.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO:0000256|RuleBase:RU362096};

Adaptive immunity;ATP-binding;Cytoplasm;Immunity;Kinase;Nucleotide-binding;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase

actin cytoskeleton organization [GO:0030036]; activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; B cell proliferation involved in immune response [GO:0002322]; B cell receptor signaling pathway [GO:0050853]; B-1 B cell homeostasis [GO:0001922]; Bergmann glial cell differentiation [GO:0060020]; BMP signaling pathway [GO:0030509]; canonical NF-kappaB signal transduction [GO:0007249]; cell-cell adhesion [GO:0098609]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cellular senescence [GO:0090398]; cerebellum morphogenesis [GO:0021587]; circulatory system development [GO:0072359]; DN4 thymocyte differentiation [GO:1904157]; DNA conformation change [GO:0071103]; endothelial cell migration [GO:0043542]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; establishment of localization in cell [GO:0051649]; integrin-mediated signaling pathway [GO:0007229]; microspike assembly [GO:0030035]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cellular senescence [GO:2000773]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of mitotic cell cycle [GO:0045930]; neural tube closure [GO:0001843]; neuroepithelial cell differentiation [GO:0060563]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuropilin signaling pathway [GO:0038189]; phagocytosis [GO:0006909]; phosphorylation [GO:0016310]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; positive regulation of blood vessel branching [GO:1905555]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of T cell migration [GO:2000406]; positive regulation of type II interferon production [GO:0032729]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; post-embryonic development [GO:0009791]; protein localization to cytoplasmic microtubule plus-end [GO:1904518]; regulation of axon extension [GO:0030516]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of extracellular matrix organization [GO:1903053]; regulation of microtubule polymerization [GO:0031113]; regulation of modification of synaptic structure [GO:1905244]; regulation of T cell differentiation [GO:0045580]; signal transduction in response to DNA damage [GO:0042770]; spleen development [GO:0048536]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]; transitional one stage B cell differentiation [GO:0002333]

actin cytoskeleton [GO:0015629]; cell leading edge [GO:0031252]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]

actin filament binding [GO:0051015]; ATP binding [GO:0005524]; bubble DNA binding [GO:0000405]; ephrin receptor binding [GO:0046875]; four-way junction DNA binding [GO:0000400]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase binding [GO:0051019]; neuropilin binding [GO:0038191]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; proline-rich region binding [GO:0070064]; protein kinase C binding [GO:0005080]; protein self-association [GO:0043621]; protein tyrosine kinase activity [GO:0004713]; sequence-specific double-stranded DNA binding [GO:1990837]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]; syntaxin binding [GO:0019905]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004370}.

IPR035837;IPR015015;IPR011009;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;

1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10;

A0A287BBC4

MTTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGSQVAAQKRPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEEEE

Sus scrofa (Pig)

2.7.1.77; 3.1.3.5; 3.1.3.99

CATALYTIC ACTIVITY: Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036349}; CATALYTIC ACTIVITY: Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592, ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00036204}; CATALYTIC ACTIVITY: Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714, ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036695}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715; Evidence={ECO:0000256|ARBA:ARBA00036695}; CATALYTIC ACTIVITY: Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584, ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036089}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000256|ARBA:ARBA00036953}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719; Evidence={ECO:0000256|ARBA:ARBA00036953}; CATALYTIC ACTIVITY: Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530, ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57464; Evidence={ECO:0000256|ARBA:ARBA00036213}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531; Evidence={ECO:0000256|ARBA:ARBA00036213}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside; Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274, ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77; Evidence={ECO:0000256|ARBA:ARBA00036260}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000256|ARBA:ARBA00035871}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485; Evidence={ECO:0000256|ARBA:ARBA00035871}; CATALYTIC ACTIVITY: Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate; Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57673; Evidence={ECO:0000256|ARBA:ARBA00036911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380; Evidence={ECO:0000256|ARBA:ARBA00036911}; CATALYTIC ACTIVITY: Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP; Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596, ChEBI:CHEBI:57673, ChEBI:CHEBI:58053; Evidence={ECO:0000256|ARBA:ARBA00036593}; CATALYTIC ACTIVITY: Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate; Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194; Evidence={ECO:0000256|ARBA:ARBA00036191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384; Evidence={ECO:0000256|ARBA:ARBA00036191}; CATALYTIC ACTIVITY: Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572, ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053, ChEBI:CHEBI:61194; Evidence={ECO:0000256|ARBA:ARBA00036258}; CATALYTIC ACTIVITY: Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588, ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865, ChEBI:CHEBI:58053; Evidence={ECO:0000256|ARBA:ARBA00036826};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR017434-2}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};

Allosteric enzyme;ATP-binding;Cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Proteomics identification;Reference proteome;Transferase

adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; dGMP metabolic process [GO:0046054]; GMP metabolic process [GO:0046037]; IMP catabolic process [GO:0006204]; IMP metabolic process [GO:0046040]; negative regulation of defense response to virus by host [GO:0050689]; protein K48-linked ubiquitination [GO:0070936]

cytosol [GO:0005829]

5'-nucleotidase activity [GO:0008253]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; IMP 5'-nucleotidase activity [GO:0050483]; metal ion binding [GO:0046872]; nucleoside phosphotransferase activity [GO:0050146]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.

IPR036412;IPR008380;IPR023214;IPR016695;

3.40.50.1000;

A0A287BBJ7

MPLAPGATLPRSPHPNPTRRPRRPSPGGGAARGVRPAAVTWAAPANRRTPRCRTRPAGRGSSSWWRRSERARDRGPAMEREVQRLRAAFQTGRSRPLAFRLQQLQALRRMVQEREEDLLAAIAADLSKSKLNAYSQEVLTILGEIDLALEKLPEWAAARPAEKNLLTMLDEAYVQPEPLGVMLIIGAWNYPLVLSIQPLIGAIAAGNAVIIKPSEISENTAKILAKLLPQYLDQDLYAVINGGVEETTKLLEQRFDHILYTGSTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDPDCDLDVACRRIAWGKYMNCGQTCIAPDYVLCEPSLQDQVVQKMKEAVKEFYGDNIKDSPDYERIVNLRHFKRIQSLLEGQKIAFGGETDEATRYIAPTILTDVDPEAKVMREEIFGPILPIVPVKNADEAVKFINEREKPLAFYVFSRNNKLIKRMIEATSSGGVTGNDVIMHFMLSSLPFGGVGSSGMGAYHGKHSFETFSHLRPCLLKSLKGEGANKLRYPPNSQSKVDWAKFFFLKRVSKGRLGLLFLALLGVVLAVLLKVGAGAPSIPGAPTLETNSVL

Sus scrofa (Pig)

1.2.1.3; 1.2.1.94

CATALYTIC ACTIVITY: Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:72745; Evidence={ECO:0000256|ARBA:ARBA00035777}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+) + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83276; EC=1.2.1.94; Evidence={ECO:0000256|ARBA:ARBA00036228}; CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+); Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00035953}; CATALYTIC ACTIVITY: Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14-tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268; Evidence={ECO:0000256|ARBA:ARBA00035974}; CATALYTIC ACTIVITY: Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) + NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298, ChEBI:CHEBI:76299; Evidence={ECO:0000256|ARBA:ARBA00036932}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate; Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00035984}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate; Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00000589}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate; Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:84067; Evidence={ECO:0000256|ARBA:ARBA00035786}; CATALYTIC ACTIVITY: Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH; Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036881}; CATALYTIC ACTIVITY: Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) + NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036717}; CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000256|ARBA:ARBA00024149}; CATALYTIC ACTIVITY: Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036332}; CATALYTIC ACTIVITY: Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+); Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036265};

Endoplasmic reticulum;Fatty acid metabolism;Lipid metabolism;Membrane;Microsome;Oxidoreductase;Proteomics identification;Reference proteome;Transmembrane;Transmembrane helix

cellular aldehyde metabolic process [GO:0006081]; central nervous system development [GO:0007417]; epidermis development [GO:0008544]; fatty acid metabolic process [GO:0006631]; hexadecanal metabolic process [GO:0046458]; peripheral nervous system development [GO:0007422]; phytol metabolic process [GO:0033306]

cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]

3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; long-chain-alcohol oxidase activity [GO:0046577]; long-chain-aldehyde dehydrogenase activity [GO:0050061]; medium-chain-aldehyde dehydrogenase activity [GO:0052814]; protein homodimerization activity [GO:0042803]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004131}.

IPR016161;IPR016163;IPR016160;IPR029510;IPR016162;IPR015590;IPR012394;

A0A287BBY6

MVRALMAGGGKEHRSWRSGPDTVRRARRCLVARPSRGSWWSPAAGLNMAPFLRISFNSYELGSLKTADEASQPFCAVRMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDIDCKQSMRGEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCRDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVYNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCQMKVANLCGINQKLLAEALNQVTQRPVRKSESEVAETVGIYQNFEKKPGVSGDDVSAGTGTYGKIWESSTKCSIDNFIFIKVLGKGSFGKVLLAELKGKKEFFAIKALKKDVVLIDDDVECTMVEKRVLALAGENPFLTHLFCTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIICGLQFLHQKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENMLGDKQASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDSPYYPRWITRESKDILEKLLERDTGKRLGVTGNIRTHPFFKTINWTLLEKRAVEPPFKPKVRSPGDYSNFDQEFLNEKPRLSFSDKNLIDSMDQTAFAGFSFLNPKFERLLEN

Sus scrofa (Pig)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569, ECO:0000256|PIRNR:PIRNR000551};

ATP-binding;Cytoplasm;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger

apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; cell chemotaxis [GO:0060326]; cellular response to angiotensin [GO:1904385]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hydroperoxide [GO:0071447]; cellular response to UV [GO:0034644]; cellular senescence [GO:0090398]; defense response to bacterium [GO:0042742]; DNA damage response [GO:0006974]; immunoglobulin mediated immune response [GO:0016064]; intracellular signal transduction [GO:0035556]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of filopodium assembly [GO:0051490]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of platelet aggregation [GO:0090331]; neutrophil activation [GO:0042119]; phosphorylation [GO:0016310]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of glucosylceramide catabolic process [GO:2000753]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of sphingomyelin catabolic process [GO:2000755]; positive regulation of superoxide anion generation [GO:0032930]; post-translational protein modification [GO:0043687]; termination of signal transduction [GO:0023021]

cell-cell junction [GO:0005911]; cytosol [GO:0005829]; endolysosome [GO:0036019]; endoplasmic reticulum [GO:0005783]; nuclear matrix [GO:0016363]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; enzyme activator activity [GO:0008047]; insulin receptor substrate binding [GO:0043560]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.

IPR000961;IPR046349;IPR000008;IPR035892;IPR020454;IPR011009;IPR002219;IPR027436;IPR017892;IPR014376;IPR000719;IPR017441;IPR008271;

3.30.60.20;2.60.40.150;1.10.510.10;

A0A287BDE3

MKPRRSTSPFREITVEPDSKLVSRPNWEPEPQETPNTQPESGQEKTPIAQPASKLQQGHNTQQEPTAQQRPLTQQEPFAQNEAESQQELRAQDKSALQQEFLVPLEPAPQQSPPIQRVPFTNHEVISWYGPGPGKEQETQLREGSRAQQGHRPQNGPPALTEPMFQERPQQSDSTAQYTAPAQGVRSQKGSLVQWQFPSKPNEPPQQQPVSEQKTFLEWVTDSGTESDLKSTLETNSPPKRDGKMAQGMKLAFEGKPNYEVMSGFGGTPTPRKKTSGQNPRHYRNTASRLTHSMDLRTMTQSLVTLAEDNMAFFSGQGPGETARRLSGVFAGIREQALGLEPALGRLLSVAHLFDLDAETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALAYYAQRLLAINRPGKLFFEGDEGVTADFLREYVTLHKGCFYGRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVTASSLFTSGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIEVLSSLANMASATVRVSRLLSLPPKAFEMPLTADPKLTVTISPPLAHTGPGPVLVRLISYDLREGQDSEELSSLVRSEGPRGLELRPRPQQAPRSRSLVVHIHGGGFVAQTSKSHEPYLKSWAQELGVPILSIDYSLAPEAPFPRALEECFYAYCWAVKHCGLLGSTGERICLAGDSAGGNLCFTVSLRAAAYGVRVPDGIMAAYPATMLQSAASPSRLLSLMDPLLPLSVLSKCVSAYAGGEMEDHSDSDQKALGMMGLVRRDTALLFRDLRLGASSWLNSFLELSGHKSRPNLVPTEEPMRRSVSEAALAQPEGPLGTDSLKYLTLHDLSLSSETQDTPELSLSAETLGPTTPSAVNFLFRPEDAPEEAEARDEISTKEEKVYSVRAAFPEGFHPRRSSQGAIQMPLYSAPIVKNPFMSPLLAPDSMLQTLPPVHIVACALDPMLDDSVMFARRLRSLGQPVTLHVVEDLPHGFLSLAALCRETRQAAALCVDRIRFILNPPGPATPAGPTTPPV

Sus scrofa (Pig)

3.1.1.23; 3.1.1.79

CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:53753; Evidence={ECO:0000256|ARBA:ARBA00023334}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381; Evidence={ECO:0000256|ARBA:ARBA00023334}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000256|ARBA:ARBA00000652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000256|ARBA:ARBA00000652}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:75937; Evidence={ECO:0000256|ARBA:ARBA00023366}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456; Evidence={ECO:0000256|ARBA:ARBA00023366}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38659, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:73990; Evidence={ECO:0000256|ARBA:ARBA00023353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38660; Evidence={ECO:0000256|ARBA:ARBA00023353}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75937; Evidence={ECO:0000256|ARBA:ARBA00023356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39936; Evidence={ECO:0000256|ARBA:ARBA00023356}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence={ECO:0000256|ARBA:ARBA00044468}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940; Evidence={ECO:0000256|ARBA:ARBA00044468}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000256|ARBA:ARBA00023407}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000256|ARBA:ARBA00023407}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-glycerol + acetate + H(+); Xref=Rhea:RHEA:38563, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:34115, ChEBI:CHEBI:75936; Evidence={ECO:0000256|ARBA:ARBA00023406}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564; Evidence={ECO:0000256|ARBA:ARBA00023406}; CATALYTIC ACTIVITY: Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38383, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990, ChEBI:CHEBI:75824; Evidence={ECO:0000256|ARBA:ARBA00023360}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38384; Evidence={ECO:0000256|ARBA:ARBA00023360}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000256|ARBA:ARBA00000361}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000256|ARBA:ARBA00000361}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000256|ARBA:ARBA00023382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000256|ARBA:ARBA00023382}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000256|ARBA:ARBA00001613}; CATALYTIC ACTIVITY: Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol + H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79; Evidence={ECO:0000256|ARBA:ARBA00000354}; CATALYTIC ACTIVITY: Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+); Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868; EC=3.1.1.79; Evidence={ECO:0000256|ARBA:ARBA00001413}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79; Evidence={ECO:0000256|ARBA:ARBA00000803}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000256|ARBA:ARBA00023384}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000256|ARBA:ARBA00023384}; CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, ChEBI:CHEBI:46898; Evidence={ECO:0000256|ARBA:ARBA00023350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; Evidence={ECO:0000256|ARBA:ARBA00023350};

PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000256|ARBA:ARBA00004879}.; PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.

Cell membrane;Cholesterol metabolism;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Proteomics identification;Reference proteome;Steroid metabolism;Sterol metabolism

cholesterol metabolic process [GO:0008203]; triglyceride catabolic process [GO:0019433]

caveola [GO:0005901]; cytosol [GO:0005829]; lipid droplet [GO:0005811]

acylglycerol lipase activity [GO:0047372]; hormone-sensitive lipase activity [GO:0033878]; retinyl-palmitate esterase activity [GO:0050253]; sterol esterase activity [GO:0004771]; triglyceride lipase activity [GO:0004806]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lipid droplet {ECO:0000256|ARBA:ARBA00004502}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004345}.

IPR029058;IPR013094;IPR010468;IPR002168;IPR033140;

3.40.50.1820;

A0A287BG16

MRFREPLLGGSAATMPGASLQRACRLLVAVCALHLGVTLIYYLTGRDLSRLPQLVGVPTPLQGGSNSAAAIGQPSGELRPRGAAPQPPLRASSKPSSGGDSSPDADSRPGPGPASNLTSAPVPSTAARLPPACPEESPLLVGPMLIEFNMAVDLKLVEKQNPEVNMGGHYTPKDCTSPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGVYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKEQFLTINGFPNNYWGWGGEDDDIFNRLAFKGMSVSRPNAMIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNTLTYLVLDIERYPLFTKITVDIGTPS

Sus scrofa (Pig)

FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000256|RuleBase:RU368121}.

2.4.1.-

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936, ECO:0000256|RuleBase:RU368121};

PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.

Glycoprotein;Glycosyltransferase;Golgi apparatus;Manganese;Membrane;Metal-binding;Proteomics identification;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix

acute inflammatory response [GO:0002526]; angiogenesis involved in wound healing [GO:0060055]; binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; development of secondary sexual characteristics [GO:0045136]; epithelial cell development [GO:0002064]; epithelial cell proliferation [GO:0050673]; extracellular matrix organization [GO:0030198]; galactose metabolic process [GO:0006012]; lactose biosynthetic process [GO:0005989]; lipid metabolic process [GO:0006629]; macrophage migration [GO:1905517]; negative regulation of epithelial cell proliferation [GO:0050680]; penetration of zona pellucida [GO:0007341]; positive regulation of apoptotic process [GO:0043065]; positive regulation of circulating fibrinogen levels [GO:0061755]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; protein N-linked glycosylation [GO:0006487]; regulation of acrosome reaction [GO:0060046]

basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; desmosome [GO:0030057]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; protein-containing complex [GO:0032991]

beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; cytoskeletal protein binding [GO:0008092]; lactose synthase activity [GO:0004461]; manganese ion binding [GO:0030145]; N-acetyllactosamine synthase activity [GO:0003945]

SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein {ECO:0000256|RuleBase:RU368121}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.

IPR003859;IPR027791;IPR027995;IPR029044;

A0A287BGG6

MKGKEEKESGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDSQSVKAHFFLGQCQLEMESYDEAIANLQRAYNLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQENELHSYLTRLIVAERERELEECQRNHEGEEDDGHIRAQQACIEAKHDKYLADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY

Sus scrofa (Pig)

2.3.2.27

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};

Coiled coil;Proteomics identification;Reference proteome;Repeat;TPR repeat

cellular response to misfolded protein [GO:0071218]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of chaperone-mediated protein complex assembly [GO:0090035]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of proteolysis [GO:0045862]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein stabilization [GO:0050821]; regulation of glucocorticoid metabolic process [GO:0031943]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nuclear inclusion body [GO:0042405]; nucleoplasm [GO:0005654]; protein folding chaperone complex [GO:0101031]; ubiquitin ligase complex [GO:0000151]; Z disc [GO:0030018]

G protein-coupled receptor binding [GO:0001664]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; kinase binding [GO:0019900]; misfolded protein binding [GO:0051787]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; R-SMAD binding [GO:0070412]; TPR domain binding [GO:0030911]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-ubiquitin ligase activity [GO:0034450]

IPR045202;IPR041312;IPR011990;IPR019734;IPR003613;IPR013083;

6.10.140.2020;1.25.40.10;3.30.40.10;

A0A287BIE4

MAQSLRLHFAARRSNTYPLSETSGDDLDSSIHMCFTRPTRISTSNVVQMKLTPRQTALAPLIKENVKSQERSSVPSPENVNKKSSCLQISLQPTRYSGCLQSSHVLAGSDDASFTCVLKDGSAVVDNDLSAVDDGTFLSSSVICSGSLSNFSASENGSYSSNSSDYGSCTSITSGGSYTNSITSDSSGCGFPPTDDTFFGGNLSSDSTSNRSVPNRNTAPCEILSRSTSTVPFVQDDLDHGLEIMKLPMIRNSKIPLKRCSSLVIFPRSPSNTPPTSPTSTGTFLSKGSYQTSHQFVISPSEVAHNEDGTNAKGFLSTAVNGLRLSKTTSTPGEVRDIRPLHRKGSLQKKTVIANNSPNQTACEKSSEGYSCVSVHFTQQKATTLNCETANGDCKPGMSEIKLNSDSEYIKRMHRTSAYLPSSQNIDCQINISRQLERPNLQINKNHAILRRSISLGGTYPNISCLSSLKHNCSKGGPSQLLIKFASGNEGKVDNLTRDSNRDFTNDPSNSLKHSCKTRDDFLGQVDVPLYPLPTENPRMERPYTFKDFVLHPRSHKSRVKGYLRLKMTYLPKTSGSEEDNTEQAEELEPGWVVLDQPDAACNLQQQQEPSPLPPGWEERQDILGRTYYVNHESRRTQWKRPSLQDTLTDAENGNIQLQAQRAFTTRRQISEETESVDSRESSENWEIIREDEATMYSNQAFPSSPPSNNLDVQTHLAEELNARLTVCGNSATGQPVSSSNHSSRRSSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNCRTTTWLKPTLQASVTTETSQLPSSQSSSTGPQAQAPTSDAAQQVTQPSEMEQGSLPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPAHLRGKTSLDPSSDLGPLPPGWEERTHTDGRIFYINHNIKKTQWEDPRLQNVAITGPAVPYSRDYKRKYEFFRRKLKKQNDIPNKFEMKLRRATVLEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKTITLHDMESVDGEYYNSLRWILENDPTELDLRFVIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSVNHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQSFTVEQWGTPEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFDGVD

Sus scrofa (Pig)

2.3.2.26

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906}.

Reference proteome;Ubl conjugation pathway

cellular response to UV [GO:0034644]; DNA damage response [GO:0006974]; formation of structure involved in a symbiotic process [GO:0044111]; glucocorticoid receptor signaling pathway [GO:0042921]; innate immune response [GO:0045087]; negative regulation of sodium ion transport [GO:0010766]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuromuscular junction development [GO:0007528]; neuron projection development [GO:0031175]; positive regulation of nucleocytoplasmic transport [GO:0046824]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein catabolic process [GO:0045732]; progesterone receptor signaling pathway [GO:0050847]; protein polyubiquitination [GO:0000209]; protein targeting to lysosome [GO:0006622]; protein ubiquitination [GO:0016567]; receptor catabolic process [GO:0032801]; receptor internalization [GO:0031623]; regulation of dendrite morphogenesis [GO:0048814]; regulation of membrane potential [GO:0042391]; regulation of monoatomic ion transmembrane transport [GO:0034765]; regulation of synapse organization [GO:0050807]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; viral budding [GO:0046755]

cell cortex [GO:0005938]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

beta-2 adrenergic receptor binding [GO:0031698]; proline-rich region binding [GO:0070064]; protein domain specific binding [GO:0019904]; RNA polymerase binding [GO:0070063]; sodium channel inhibitor activity [GO:0019871]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]

IPR035892;IPR000569;IPR035983;IPR001202;IPR036020;

2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;

A0A287BKF3

MENHMFSVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGQPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTRPLAPPTAAVDLSHQSAAGKEQTVVVDGATGPGNGPQHIPDHGQEAGSLSHTNGLAPRPPSQDPAKKSAAVTLQGSGENNKLLKEIEPVLNLLSSGSKGINRGEPAKAETKDVEIQVDRDMDGKSHKTLPLGVENDRVFNDLWGKGNMPVVLNNPYSEKEQPPASGKQSPTKNGSPSKCPRFLKVKNWETDVVLSDTLHLKSTLGTGCTEHICMGSVMLPSQHIRRPEDVHTKEQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIETTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHIKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSILGDPANVAFTEICIQQGWKPPRSRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDSSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVHEERKYPEPLRFFPRKGPSLARGYTELRGLAAARDSQHRSYKVRFNSVSSYSDSRKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLSYVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGNQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPLNQLVKVELLEERNTALGVISNWTDEHRIPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPSTLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAVVSYRTRDGEGPIHHGVCSSWLNRIQADEVVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMSPCPMVLVFGCRQSKIDHIYKEETLQAKSKGVFRELYTAYSREPDKPKKYVQDILQEQLAEAVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSVEDAGVFISRLRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS

Sus scrofa (Pig)

1.14.13.39

CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={ECO:0000256|ARBA:ARBA00035595}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; Evidence={ECO:0000256|ARBA:ARBA00035595};

COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|ARBA:ARBA00001917}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970};

Calmodulin-binding;FAD;Flavoprotein;FMN;Heme;Iron;Metal-binding;NADP;Oxidoreductase;Reference proteome;Ubl conjugation

arginine catabolic process [GO:0006527]; multicellular organismal response to stress [GO:0033555]; muscle contraction [GO:0006936]; negative regulation of blood pressure [GO:0045776]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide mediated signal transduction [GO:0007263]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; response to heat [GO:0009408]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; retrograde trans-synaptic signaling by nitric oxide [GO:0098924]; vasodilation [GO:0042311]

cytosol [GO:0005829]; dendritic spine [GO:0043197]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]

calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]

SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.

IPR003097;IPR017927;IPR001094;IPR008254;IPR001709;IPR029039;IPR039261;IPR023173;IPR044943;IPR044940;IPR044944;IPR012144;IPR004030;IPR036119;IPR001433;IPR001478;IPR036034;IPR017938;

2.30.42.10;3.40.50.360;3.90.440.10;3.40.50.80;2.40.30.10;

A0A287BLH5

MAASRKCGAERNARQRGKFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGLKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ

Sus scrofa (Pig)

3.6.4.13

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000256|ARBA:ARBA00001556};

ATP-binding;Biological rhythms;Helicase;Hydrolase;Isopeptide bond;Nucleotide-binding;Nucleus;Proteomics identification;Reference proteome;RNA-binding

alternative mRNA splicing, via spliceosome [GO:0000380]; androgen receptor signaling pathway [GO:0030521]; BMP signaling pathway [GO:0030509]; epithelial to mesenchymal transition [GO:0001837]; intracellular estrogen receptor signaling pathway [GO:0030520]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; mRNA transcription [GO:0009299]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nuclear-transcribed mRNA catabolic process [GO:0000956]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; primary miRNA processing [GO:0031053]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of androgen receptor signaling pathway [GO:0060765]; rhythmic process [GO:0048511]

catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]

ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; MH2 domain binding [GO:0035500]; mRNA 3'-UTR binding [GO:0003730]; nuclear androgen receptor binding [GO:0050681]; pre-mRNA binding [GO:0036002]; primary miRNA binding [GO:0070878]; R-SMAD binding [GO:0070412]; ribonucleoprotein complex binding [GO:0043021]; RNA helicase activity [GO:0003724]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR011545;IPR014001;IPR001650;IPR027417;IPR012587;IPR000629;IPR014014;

3.40.50.300;

A0A287BLU1

MTPGVQGQRTGRLQHFSALRGKAGNCSEAAPKCSSSAVKFPGLAVGTEGTMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSGVDGGISVQAEASLPRNLLFKYATNSKEVIGVVSKEYIPKGTRFGPLIGEIYTNDTVPKNANRKYFWRIYSRGELHHFIDGFNEEKSNWLRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTMMNDTQIQSHPKQQSTEKHELCPRNVPKREYSVKEILKLDSHPPKGKDLYRSNISPLTSEKGPDDFRKNGSPDMPFYPRVVYPIRAPLPEDFVKASLAYGMERPTYITHSPIPSSTPPSPSARSSPDRSLQSCSPHSSPGNAVSPLAPGAQEHRDSYAYLNAPYGAAEGLGSYPGYAPAPHLPPAFIPSYNAHYPKFLLPPYGMNCNSLGAVGNINGLNNFGLFPRLYPVYGGLLGGGGLPPPMLAPASLPSSLPSEGTRRLLQPEHPREVLVPAPSHSAFSLPGAAASLKDKACSPTSGSPTAGTAATAEHVVQPKATSAAAAAPGGGNDEAVNLIKNKRNMTGYKTLPYPLKKQNGKIKYECNVCAKTFGQLSNLKVHLRVHSGERPFKCQTCNKGFTQLAHLQKHYLVHTGEKPHECQVCHKRFSSTSNLKTHLRLHSGEKPYQCKVCPAKFTQFVHLKLHKRLHTRERPHKCAHCHKSYIHLCSLKVHLKGHCPAAPATGLPLEDLTRINEEIEKFDISDNADRLEDMEDNIDVTSVVEKEILAVVRKEKEETGLKVSLQRNVGNGLLSGCSLYESTDPSLLKLPHSNPLPLGPVKVKQETVEPMDP

Sus scrofa (Pig)

FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection. Binds specifically to the PRDI element in the promoter of the beta-interferon gene. Drives the maturation of B-lymphocytes into Ig secreting cells. Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions. {ECO:0000256|PIRNR:PIRNR013212}.

2.1.1.-

Metal-binding;Methyltransferase;Reference proteome;Transferase;Zinc;Zinc-finger

aorta development [GO:0035904]; artery morphogenesis [GO:0048844]; cell fate commitment [GO:0045165]; coronary vasculature development [GO:0060976]; eye photoreceptor cell development [GO:0042462]; gene expression [GO:0010467]; germ cell development [GO:0007281]; heart valve development [GO:0003170]; intestinal epithelial cell development [GO:0060576]; kidney development [GO:0001822]; maternal placenta development [GO:0001893]; methylation [GO:0032259]; morphogenesis of a branching structure [GO:0001763]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; post-embryonic development [GO:0009791]; regulation of cell population proliferation [GO:0042127]; regulation of extrathymic T cell differentiation [GO:0033082]; regulation of natural killer cell differentiation [GO:0032823]; regulation of NK T cell differentiation [GO:0051136]; regulation of transcription by RNA polymerase II [GO:0006357]; retinal bipolar neuron differentiation [GO:0060040]; sebum secreting cell proliferation [GO:1990654]; trophoblast giant cell differentiation [GO:0060707]; ventricular septum development [GO:0003281]

cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR013212}. Cytoplasm {ECO:0000256|PIRNR:PIRNR013212}.

IPR016608;IPR044413;IPR001214;IPR046341;IPR036236;IPR013087;

3.30.160.60;2.170.270.10;

A0A287BMD1

MPVQAAQWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQTAINTDIDVLPVNFALLQLVGAQVPDHQSIKLSNLGENKNYEVAKKCVEDLALYLKPLSGGKGVASLNQSALSRPMQRKLVTLVNCQLVEEEGRVRAMRAARSLGERTVTELILQHQNPQQLSANLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRSYEALRREHDAQIVHIAMEAGLRISPEQWSSLLYGDLAHKSHMQSIIDKLQSPESFAKSVQELTIVLQRTGDPANLNRLRPHLELLANIDPNPDAVSPTWEQLENAMVAVKTVVHGLVDFIQNYSRKGHETPQPQPNSKYKTSMCRDLRQQGGCPRGTNCTFAHSQEELEKYRLRNKKINATVRTFPLLNKVGVNNTVTTTAGNVISVIGSTETTGKIVPSTNGVSNAENSVSQLIPRSTDSTLRALETVKKVGKVGTNGQNAAGPSAESVTENKIGSPPKTPVSNVTATSAGPSNVGTELNSVPPKSSPFITRVPVYPQHSENIQYFQDPRTQIPFEVPQYPQAGYYPPPPTVPAGVAPCVPRFVRSNNVPESSLPPASMPYADHYSTFSPRDRMNSTPYQPPPPQPYGPVPPVPSGMYAPVYDSRRIWRPPMYQRDDIIRSNSLPPMDVMHSSVYQTSLRERYNSLDGYYSVACQPPSEPRTTVPLPREPCGHLKTSCEEQIRRKPEQWAQQYHTQKAPLVSSTLPVATQSPTPPSPLFSVDFRTDFSESVSGTKFEEDHLSHYSPWSCGTIGSCINSIDSEPRDVIANSNAVLMDLDSGDVKRRVHLFETQRRTKEEDPIIPFSDGPIISKWGAISRSSRTGYHTTDPVQATASQGSATKPISVSDYVPYVNAVDSRWSSYGNEATSSAHYIERDRFIVTDLSGHRKHSSTGDLLSIELQQAKSNSLLLQREANALAMQQKWNSLDEGRHLTLNLLSKEIELRNGELQSDYTEDATDTKPDRDIELELSALDTDEPDGQGEQIEEILDIQLGISSQNDQLLNGTAVENGHPVQQHQKEPLEQKRQSLGEDHVILEEQKAILPVTSCFSQPLPVSISSASCLPITTSVSVGNLILKTHVMSEDKNDFLKPVANGKMVNS

Sus scrofa (Pig)

2.3.2.27

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};

Metal-binding;Reference proteome;Transferase;Zinc;Zinc-finger

B cell homeostasis [GO:0001782]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lymph node development [GO:0048535]; multicellular organism growth [GO:0035264]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; post-embryonic development [GO:0009791]; protein polyubiquitination [GO:0000209]; regulation of miRNA metabolic process [GO:2000628]; spleen development [GO:0048536]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]; T follicular helper cell differentiation [GO:0061470]; ubiquitin-dependent protein catabolic process [GO:0006511]

cell surface [GO:0009986]; cytoplasmic stress granule [GO:0010494]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; P-body [GO:0000932]

DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA stem-loop binding [GO:0035613]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.

IPR041523;IPR048575;IPR000571;IPR036855;IPR001841;IPR013083;IPR017907;

1.20.120.1790;4.10.1000.10;3.30.40.10;

A0A287BMP7

MLNPGLSSSSGRGGASASPPDLSEVPASRRKLGFPAAHPSREPRPVESLAGHTTDLRNQEKLLSARAEVKAAIKYALTVGYRHIDCAAIYGNELEIGEALQETVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTIRYDATHYKDTWKALEALVAKGLVRALGLSNFSSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPNEPVLLEEPVVQALAEKYNRSPAQILLRWQVQRKVICIPKSVTPSRILQNIQVFDFTFSPEEMKQLDALNKNLRFIVPMLTVDGKRVPRDAGHPLYPFNDPY

Sus scrofa (Pig)

1.1.1.19; 1.1.1.2; 1.1.1.20; 1.1.1.372; 1.1.1.54

CATALYTIC ACTIVITY: Reaction=3-deoxyfructose + NADP(+) = 3-deoxyglucosone + H(+) + NADPH; Xref=Rhea:RHEA:58668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60777, ChEBI:CHEBI:142685; Evidence={ECO:0000256|ARBA:ARBA00023987}; CATALYTIC ACTIVITY: Reaction=L-gulonate + NADP(+) = aldehydo-D-glucuronate + H(+) + NADPH; Xref=Rhea:RHEA:14909, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142686; EC=1.1.1.19; Evidence={ECO:0000256|ARBA:ARBA00023919}; CATALYTIC ACTIVITY: Reaction=L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + H(+) + NADPH; Xref=Rhea:RHEA:18925, ChEBI:CHEBI:15378, ChEBI:CHEBI:17587, ChEBI:CHEBI:18268, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.20; Evidence={ECO:0000256|ARBA:ARBA00023969}; CATALYTIC ACTIVITY: Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; Evidence={ECO:0000256|ARBA:ARBA00023978}; CATALYTIC ACTIVITY: Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH; Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54; Evidence={ECO:0000256|ARBA:ARBA00023997}; CATALYTIC ACTIVITY: Reaction=glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH; Xref=Rhea:RHEA:23592, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.372; Evidence={ECO:0000256|ARBA:ARBA00023947}; CATALYTIC ACTIVITY: Reaction=glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH; Xref=Rhea:RHEA:38111, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27975, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.372; Evidence={ECO:0000256|ARBA:ARBA00023958}; CATALYTIC ACTIVITY: Reaction=hydroxyacetone + NADP(+) = H(+) + methylglyoxal + NADPH; Xref=Rhea:RHEA:27986, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158, ChEBI:CHEBI:27957, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00024000};

Cell membrane;Cytoplasm;Membrane;NADP;Reference proteome

aldehyde catabolic process [GO:0046185]; cellular detoxification of aldehyde [GO:0110095]; D-glucuronate catabolic process [GO:0042840]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; glucuronate catabolic process to xylulose 5-phosphate [GO:0019640]; L-ascorbic acid biosynthetic process [GO:0019853]

apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; synapse [GO:0045202]

alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; glucuronolactone reductase activity [GO:0047941]; L-glucuronate reductase activity [GO:0047939]; S-nitrosoglutathione reductase activity [GO:0080007]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004370}.

IPR020471;IPR044481;IPR018170;IPR023210;IPR036812;

3.20.20.100;

A0A287BNZ9

MRGSGSALPGSCGARTSPPAQAPSRQLPPAAMSAAIEREFEELDAQNRWQQLYLEIRSESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNVENDYINASLVDIAEARRSYILTQGPLPNTGCHFWLMVWQQKTKAVVMLNRVVEKESVKCAQYWPTKDSREMLFKETGFSVKFLSEDVKSYYTVHLLQLGNTNSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLDPEHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQLLLNMRQYRMGLIQTPDQLRFSYMTIIEGAKFIKGDSNIQKRWKELSKEDVCPVFDHSPTKIMTEKYNGNRIGLEEEKLTGDRCTGLSSKMQDAVEDNSESALRKRIREDRRAGTAQKVQQMKQRLNETERKRKRWLYWQPILTKMGFVSVILVGAFVGWTLFFQQNVL

Sus scrofa (Pig)

3.1.3.48

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000256|PIRNR:PIRNR000926};

Endoplasmic reticulum;Hydrolase;Membrane;Protein phosphatase;Receptor;Reference proteome;Transmembrane;Transmembrane helix

B cell differentiation [GO:0030183]; dephosphorylation [GO:0016311]; erythrocyte differentiation [GO:0030218]; glucose homeostasis [GO:0042593]; insulin receptor recycling [GO:0038020]; insulin receptor signaling pathway [GO:0008286]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemotaxis [GO:0050922]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of interleukin-2-mediated signaling pathway [GO:1902206]; negative regulation of interleukin-4-mediated signaling pathway [GO:1902215]; negative regulation of interleukin-6-mediated signaling pathway [GO:0070104]; negative regulation of lipid storage [GO:0010888]; negative regulation of macrophage colony-stimulating factor signaling pathway [GO:1902227]; negative regulation of macrophage differentiation [GO:0045650]; negative regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000587]; negative regulation of positive thymic T cell selection [GO:1902233]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; negative regulation of type II interferon-mediated signaling pathway [GO:0060336]; negative regulation of tyrosine phosphorylation of STAT protein [GO:0042532]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of PERK-mediated unfolded protein response [GO:1903899]; regulation of hepatocyte growth factor receptor signaling pathway [GO:1902202]; T cell differentiation [GO:0030217]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome lumen [GO:0031904]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]

integrin binding [GO:0005178]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein kinase binding [GO:0019901]; receptor tyrosine kinase binding [GO:0030971]; STAT family protein binding [GO:0097677]; syntaxin binding [GO:0019905]

IPR029021;IPR000242;IPR012265;IPR016130;IPR003595;IPR000387;

3.90.190.10;

A0A287BSC3

MWSIGTLAGSKEKRGNGPCLGEVALGEGAFLPEAIPPRSSPASSDPSKGGRGTGWRSGLEKEKEDKKESQRHRGTERREGHMDRDRERQRYRDKLSDAEADTQRRADKTEGARNTAPKRHRRKLAEDKDTHNETRTGTESEPELAEREADGRTGKPGGKRAREAREPRVRREPSPGAGRERVPRLPAGGALAPRAGLGGGCAGRAPASRGRGRGGRERGRGRAAPAAFGPRGRLYKPAGEVASAASRSRHSAPPDPCTYSTSLLPGQSFTHELFAGLEHQLTPDHWAAHPLPPPPSYLWAPERKQVLECTMISLFLVLAIGSCLTNSLVPEKEKDPKYWRDQAQQTLKNALRLQTLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHKPGEETRLEMDKFPYVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQRTQCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALIQGCKDIAYQLMHNIRDIEVIMGGGRKYMFPKNRTDVEYEMDEKARGTRLDGLNLIDVWKSFKPRHKHSHYIWNRTELLALDPHTVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVEMAIRILIKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIEQAGSMTSVEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHDNYQAQSAVPLRHETHGGEDVAIFARGPMAHLLHGVHEQNYIPHVMAYAACIGANRDHCASASSSGSPSPGPLLLLLALLPLGILF

Sus scrofa (Pig)

3.1.3.1

CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000256|ARBA:ARBA00036139}; CATALYTIC ACTIVITY: Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29376; Evidence={ECO:0000256|ARBA:ARBA00036923}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000256|ARBA:ARBA00034440}; CATALYTIC ACTIVITY: Reaction=H2O + N-phosphocreatine = creatine + phosphate; Xref=Rhea:RHEA:12977, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092; EC=3.9.1.1; Evidence={ECO:0000256|ARBA:ARBA00036122}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12978; Evidence={ECO:0000256|ARBA:ARBA00036122}; CATALYTIC ACTIVITY: Reaction=H2O + phosphoethanolamine = ethanolamine + phosphate; Xref=Rhea:RHEA:16089, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57603, ChEBI:CHEBI:58190; Evidence={ECO:0000256|ARBA:ARBA00036048}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16090; Evidence={ECO:0000256|ARBA:ARBA00036048}; CATALYTIC ACTIVITY: Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal; Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310, ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; Evidence={ECO:0000256|ARBA:ARBA00035851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534; Evidence={ECO:0000256|ARBA:ARBA00035851}; CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000256|ARBA:ARBA00036105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018; Evidence={ECO:0000256|ARBA:ARBA00036105}; CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; Evidence={ECO:0000256|ARBA:ARBA00035865}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577; Evidence={ECO:0000256|ARBA:ARBA00035865};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};

Cell membrane;Disulfide bond;Glycoprotein;GPI-anchor;Hydrolase;Lipoprotein;Magnesium;Membrane;Metal-binding;Phosphoprotein;Proteomics identification;Reference proteome;Zinc

dephosphorylation [GO:0016311]

mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]

ADP phosphatase activity [GO:0043262]; alkaline phosphatase activity [GO:0004035]; ATP hydrolysis activity [GO:0016887]; inorganic diphosphate phosphatase activity [GO:0004427]; metal ion binding [GO:0046872]; phosphoamidase activity [GO:0050187]; phosphoethanolamine phosphatase activity [GO:0052732]; pyridoxal phosphatase activity [GO:0033883]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Extracellular vesicle membrane {ECO:0000256|ARBA:ARBA00037828}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00037828}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00037800}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00037800}.

IPR001952;IPR018299;IPR017850;

3.40.720.10;

A0A2C9F3F0

MATKAVCVLKGDGPVQGTIYFELKARAEDSVVTGTIKGLAEGDHGFHVHHLEIIHKVGCTSAGPHFNPESKKHGGPKDQERHVGDLGNVTAGKDGVATVYIEDSVIALSGDHSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGITQ

Sus scrofa (Pig)

FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000256|ARBA:ARBA00003917, ECO:0000256|RuleBase:RU000393}.

1.15.1.1

CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000256|RuleBase:RU000393};

COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000256|RuleBase:RU000393}; Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|RuleBase:RU000393}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};

Copper;Lipoprotein;Metal-binding;Oxidoreductase;Palmitate;Reference proteome;Zinc

action potential initiation [GO:0099610]; anterograde axonal transport [GO:0008089]; apoptotic process [GO:0006915]; auditory receptor cell stereocilium organization [GO:0060088]; determination of adult lifespan [GO:0008340]; ectopic germ cell programmed cell death [GO:0035234]; embryo implantation [GO:0007566]; gene expression [GO:0010467]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide biosynthetic process [GO:0050665]; intracellular iron ion homeostasis [GO:0006879]; locomotory behavior [GO:0007626]; muscle cell cellular homeostasis [GO:0046716]; myeloid cell homeostasis [GO:0002262]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of developmental process [GO:0051093]; negative regulation of inflammatory response [GO:0050728]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of reproductive process [GO:2000242]; neurofilament cytoskeleton organization [GO:0060052]; neuronal action potential [GO:0019228]; ovarian follicle development [GO:0001541]; peripheral nervous system myelin maintenance [GO:0032287]; positive regulation of cytokine production [GO:0001819]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of phagocytosis [GO:0050766]; positive regulation of superoxide anion generation [GO:0032930]; regulation of blood pressure [GO:0008217]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of multicellular organism growth [GO:0040014]; relaxation of vascular associated smooth muscle [GO:0060087]; removal of superoxide radicals [GO:0019430]; response to axon injury [GO:0048678]; response to ethanol [GO:0045471]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to xenobiotic stimulus [GO:0009410]; retina homeostasis [GO:0001895]; retrograde axonal transport [GO:0008090]; sensory perception of sound [GO:0007605]; spermatogenesis [GO:0007283]; superoxide anion generation [GO:0042554]

axon cytoplasm [GO:1904115]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]

copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; protein phosphatase 2B binding [GO:0030346]; protein-folding chaperone binding [GO:0051087]; small GTPase binding [GO:0031267]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR036423;IPR024134;IPR018152;IPR001424;

2.60.40.200;

A0A2G3A286

MDENSKPKSVLDSLGEEIVRIITPVSIYMLLVVILVTVLNNDTDSSNPSFTSIATVAYNESSSDSNWDKLKGALLNALVFVVVVTVVTFLLVLLFYFRCTKFLKYYMGFSSFLVLGFMGGEIAIFLIGKFRVPIDCVSFGLILFNFTVVGVLAVFMSKMAIVVTQGYLVVIGVLVAYWFTMLPEWTTWVLLVAMALYDLAAVLLPGGPLRLLVELAMSRDEDIPALVYEARPVIDRESVPRGGFVQRRVWRERRETEFGSDENLDSRSNLNSNVNSISESRSVLEGHPLYGSDENERNAVDMEDGQVSREDSELAAPLIQHRINVRMNLQEGSNDDFALEGIGLGSSGAIKLGLGDFIFYSVLVARAAMYDFMTVYACYLAIIADLGITLMLLAFYQKALPALPVSVLLGVLFYLLTWLLLEIFVVQCSMNLLMF

Capsicum annuum (Capsicum pepper)

FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. {ECO:0000256|RuleBase:RU361148}.

3.4.23.-

Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Protease;Reference proteome;Transmembrane;Transmembrane helix

amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta metabolic process [GO:0050435]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485]

apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]

aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000256|RuleBase:RU361148}.

IPR001108;IPR006639;IPR042524;

1.10.472.100;

A0A2G3A294

MTRHNMEEKKKKKVLDLISSFFKRSNKKQEMDENSKPKSVLDSLGEEIVRIITPVSIYMLLVVILVTVLNNDTDSSNPSFTSIATVAYNESSSDSNWDKLKGALLNALVFVVVVTVVTFLLVLLFYFRCTKFLKYYMGFSSFLVLGFMGGEIAIFLIGKFRVPIDCVSFGLILFNFTVVGVLAVFMSKMAIVVTQGYLVVIGVLVAYWFTMLPEWTTWVLLVAMALYDLAAVLLPGGPLRLLVELAMSRDEDIPALVYEARPVIDRESVPRGGFVQRRVWRERRETEFGSDENLDSRSNLNSNVNSISESRSVLEGHPLYGSDENERNAVDMEDGQVSREDSELAAPLIQHRINVRMNLQEGSNDDFALEGIGLGSSGAIKLGLGDFIFYSVLVARAAMYDFMTVYACYLAIIAGLGITLMLLAFYQKALPALPVSVLLGVLFYLLTRLLLEIFVVQCSMNLLMF

Capsicum annuum (Capsicum pepper)

FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. {ECO:0000256|RuleBase:RU361148}.

3.4.23.-

Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Protease;Reference proteome;Transmembrane;Transmembrane helix

amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta metabolic process [GO:0050435]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485]

apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]

aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000256|RuleBase:RU361148}.

IPR001108;IPR006639;IPR042524;

1.10.472.100;

A0A2H4DGV8

MEPFTTFSLVASSLILLICWALVKANKPAKNLPPGPPKLPIIGNMHQLESQSPHRVLRKLSRKYGPIMHLQLGQVPTVVISTPRLVEEVVKHHDINFADRPTNTTSQIFYYNNQNVAWSSYGNYWRQIKKIVTLELLSVKKVRSFSSIRAEELTRAVKSVEPSVGSTINFRDLTSQTVNNMVSRATLGDVCKERHILLDTMNDILKTFNSFNVVNFFPSLQFLNVITGKKAKWLKIHKQLDHILENILEEHKSKPKGNQDDEDLIDVLLRVKDAGGQELPITNDNVKAITLEMLTAGTSSSSMTIEWAFCELMRHPEVMKKVQSDVRSAVKGNKVTEDDIQNMHYLKLVVKETLRLHGVPILVPRQNREDCNVLGYHIPAKTKILINAWACGTDPDTWEDPESFIPERFEKSSVSYFGTDFQLIPFGTGRRICPGVNFGIGTVEAVLSNFLYHFDWKLPDGVKPQDIDMTEVTGISTLPKYPLHIVPVSTVSQQK

Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis)

FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:29086444). Hydroxylates germacrene A acid to 8-beta-hydroxy-germacrene A and 8-alpha-hydroxy-germacrene A acids (PubMed:29086444). Unlike 8-alpha-hydroxy-germacrene A acid with is spontaneously converted into inunolide (12, 8-alpha), 8-beta-hydroxy-germacrene A cannot undergo spontaneous lactonization (PubMed:29086444). {ECO:0000269|PubMed:29086444}.

1.14.14.168; 1.14.14.170

CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8beta-hydroxygermacra-1(10),4,11(13)-trien-12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57964, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301, ChEBI:CHEBI:142464; EC=1.14.14.168; Evidence={ECO:0000269|PubMed:29086444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57965; Evidence={ECO:0000269|PubMed:29086444}; CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8-epi-inunolide + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57968, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301, ChEBI:CHEBI:142470; EC=1.14.14.170; Evidence={ECO:0000269|PubMed:29086444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57969; Evidence={ECO:0000269|PubMed:29086444}; CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8alpha-hydroxygermacra-1(10),4,11(13)-trien-12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:58032, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301, ChEBI:CHEBI:142490; Evidence={ECO:0000269|PubMed:29086444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58033; Evidence={ECO:0000269|PubMed:29086444};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29086444}.

Glycoprotein;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Signal-anchor;Transmembrane;Transmembrane helix

response to jasmonic acid [GO:0009753]; sesquiterpene biosynthetic process [GO:0051762]; terpenoid biosynthetic process [GO:0016114]

membrane [GO:0016020]

germacrene A acid 8beta-hydroxylase activity [GO:0102614]; heme binding [GO:0020037]; iron ion binding [GO:0005506]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.

IPR001128;IPR017972;IPR002401;IPR036396;

1.10.630.10;

A0A2I0BVG8

MGCSQSSNVKDFKTRRSKFTNGNNYGKSGNNKNSEDLAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCREKHGHGEKAIKVIKKSQFDKMKYSITNKIECDDKIHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKHSLLNIKIVDFGLSSFFSKDNKLRDRLGTAYYIAPEVLRKKYNEKCDVWSCGVILYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISEEAKELIKLMLTYDYNKRITAKEALNSKWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNILRSFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRDAFNLFDTDKSGKITKEELANLFGLTSISEQMWNEVLGEADKNKDNMIDFDEFVNMMHKICDNKSS

Plasmodium falciparum (isolate NF54)

FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:27923926). By phosphorylating various proteins, required for microneme secretion and thus merozoite egress from and invasion of host erythrocytes (By similarity). During gametogenesis, essential for the development of both male and female gametes (PubMed:29311293). Phosphorylates SERA5 p50 which enhances SERA5 p50 protease activity; however, SERA5 p50 protease activity has been shown in other studies to be controversial. Probably by phosphorylating SERA5 p50, plays a role in merozoite egress from host erythrocytes. Probably prior or during merozoite invasion of host erythrocytes, phosphorylates rhoptry protein RhopH3 which is required for RhopH3 localization to rhoptries and for its secretion. Probably in late schizonts, phosphorylates myosin A tail domain-interacting protein MTIP and glideosome-associated protein 45 GAP45, both of which are components of the motor complex that generates the force required by the parasite to invade host cells. In late schizonts, phosphorylates inner membrane complex protein IMC1g. In late schizonts, phosphorylates PKA regulatory subunit PKAr in a calcium-dependent manner, which may contribute to the dissociation of regulatory PKAr and catalytic PKAc subunits and promote the activation of PKAc. May phosphorylate raf kinase inhibitory protein RKIP which in turn may regulate CDPK1 catalytic activity (By similarity). May phosphorylate proteins of the host erythrocyte membranes (By similarity). {ECO:0000250|UniProtKB:P62343, ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:27923926, ECO:0000269|PubMed:29311293}.

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:27923926}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:27923926};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27923926};

ATP-binding;Calcium;Cell membrane;Cell projection;Cilium;Cytoplasm;Flagellum;Host cell membrane;Host membrane;Kinase;Lipoprotein;Magnesium;Membrane;Metal-binding;Myristate;Nucleotide-binding;Palmitate;Phosphoprotein;Repeat;Serine/threonine-protein kinase;Transferase

female gamete generation [GO:0007292]; intracellular signal transduction [GO:0035556]; male gamete generation [GO:0048232]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]

cytoplasm [GO:0005737]; host cell plasma membrane [GO:0020002]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]; symbiont-containing vacuole membrane [GO:0020005]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]

SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:29311293}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cytoplasm {ECO:0000269|PubMed:29311293}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29311293}. Host cell membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Note=Localizes to the host erythrocytic membrane at low level (By similarity). Localizes to the cell membrane in the nascent merozoites contained within the late-stage schizonts and in free merozoites. Colocalizes with MTIP around developing merozoites in segmented schizonts, also localizes in membranes around the mature food vacuole/residual body of the schizonts. Ser-64 phosphorylated form localizes at the apical pole in punctate structures in merozoites within late schizonts in free merozoites. In trophozoites and schizonts, localizes to the parasitophorous vacuole (PV) and in membranous systems derived from the PV including intraparasitic vacuoles and the tubovesicular system, an extension of the parasitophorous vacuole membrane into the host cell cytoplasm. Localization to the cytoplasm in trophozoite or schizonts is minimal (By similarity). In female stage V gametocytes and gametes, localizes to the cell membrane. In stage V male gametocytes, localizes to the cell membrane and in the cytoplasm. In male gametes, localizes to the residual body, cell membrane and in the flagella (PubMed:29311293). Calcium and/or autophosphorylation does not affect membrane localization (By similarity). {ECO:0000250|UniProtKB:P62343, ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:29311293}.

PTM: Myristoylated. Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Palmitoylated. Palmitoylation increases in merozoites in response to low level of extracellular K(+) in the host blood. Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Phosphorylation at Ser-64 occurs at late schizont stage and regulates CDPK1 protein-protein interaction. Phosphorylated at Ser-28, Ser-34 and Ser-64 in merozoites in response to low extracellular level of K(+). Phosphorylation at Thr-231 may regulate CDPK1 kinase activity. Phosphorylation increases in response to an increase in intracellular Ca(2+) levels (By similarity). Autophosphorylated in vitro (PubMed:27923926). Autophosphorylation does not affect membrane localization in vitro (By similarity). {ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:27923926}.

DOMAIN: The junction domain (J domain) is composed of 2 motifs that maintain the kinase inactive. The N-terminal autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic domain while the C-terminal motif binds the EF-hand domains. {ECO:0000250|UniProtKB:P62344}.

IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR017441;IPR008271;

1.10.238.10;1.10.510.10;

A0A2I0C265

MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLVKREKASDNKSNVFERINFEGIVGLAFPEMLSTGKSTLYENLMSSYKLQHNEFSIYIGKDSKYSALIFGGVDKNFFEGDIYMFPVVKEYYWEIHFDGLYIDHQKFCCGVNSIVYDLKKKDQENNKLFFTRKYFRKNKFKTHLRKYLLKKIKHQKKQKHSNHKKKKLNKKKNYLIFDSGTSFNSVPKDEIEYFFRVVPSKKCDDSNIDQVVSSYPNLTYVINKMPFTLTPSQYLVRKNDMCKPAFMEIEVSSEYGHAYILGNATFMRYYYTVYRRGNNNNSSYVGIAKAVHTEENEKYLSSLHNKINNL

Plasmodium falciparum (isolate NF54)

FUNCTION: During the asexual blood stage, initiates the proteolytic maturation of several rhoptry proteins and thus, is required for merozoite invasion of host erythrocytes and probably the subsequent development of the ring-stage (PubMed:29074774). Cleaves rhoptry associated protein 1 RAP1 and apical sushi protein ASP during schizont maturation (PubMed:29074774). Also cleaves rhoptry protein RON3 (By similarity). {ECO:0000250|UniProtKB:Q8ILG2, ECO:0000269|PubMed:29074774}.

3.4.23.-

Aspartyl protease;Cytoplasmic vesicle;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zymogen

entry into host cell by a symbiont-containing vacuole [GO:0085017]; protein processing [GO:0016485]

cytoplasmic vesicle [GO:0031410]; membrane [GO:0016020]; rhoptry [GO:0020008]

aspartic-type endopeptidase activity [GO:0004190]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:29074774}. Note=In schizonts, localizes to the bulb of rhoptries. {ECO:0000269|PubMed:29074774}.

PTM: Autocleaved into a p55 mature form. {ECO:0000250|UniProtKB:Q8ILG2}.

IPR001461;IPR034164;IPR033121;IPR021109;

2.40.70.10;

A0A2I2U0F4

MSLALNDLLICCRQLEHDRATERRKEVEKFKRLIRDPETVQHLDRHSDSKQGKYLNWDAVFRFLQKYVQKETECLRTAKAGVSASTQATRQKKMQEISSLVKYFIKCANKRAPRLKCQELLNYIMDTVKDSFNGAVYGADCSNILLKDILSVRKYWCEITQQQWLELFSVYFNLYLKPAQDINRVLVARIIHAVARGCCSQTDGLNSKLLDFFSKAIHHARQEKSSAGLNHILAAFVIFLKTLAVNFRICVCQLGDEVLPTLLYIWTQHRLNDCLKEVIIELFQLQIYIRHPKGAKTQEKGAYESNKWKSILYNLYDLLINEISHIGSRGKYSSGSRNVAVKENLIDLMADICHQVFNEDTRSLEISQSYTITQRELNDYGATCKKRKIELGWDVIKDHLQKSQNDFDLVPWLQIATQLISKYPSSLPNYELSPLLMILYQLLPQQRHGERTPYVLRCLVELASCQGKKSDLESSQKSDLLKLWTKIWSITFRGISSERIQAENFGLLGAIIQGGLIEVDREFWKLFTGSACRPSCPAVCCLTLALTTCVVPETVKTGVEQNTCEVNRRFSLKELIMKWLLFYQLEDDFEDSTEPPPVLHSNFPHLALEKILVSLTMKNSKAAMNFFQRVPECEQHHKDAEESSFSEIEELFLQTTFDKMDFLTIVKECPVEKLQSSGRISVHQNLKESLDRCLLGLSEQLLNNYSFESTDAETLIRCSSLVVGVLGCYCYMGVIAEEEAYKSELFQKAKSLMQCAGESITVFKNKPHEESRIVSLRNLMHLCTRCLSNCTRPSPSKIASGFFLRLLTSKLMNDIADICRSLASFSRKPFDYGEVESVEDDPDESLMEAEDQSSMSLFSDYPAGSVSDANVSGEGQSTIGAMNPLAEEHLSKQDLLFLDMLKFLCMCVTTAQTSTVSFRAADIRRRLLMLIDSSMLDPAKSLHLHMYLVLLKELPGEEHPLPMEEVVELLKPLSNVCSLYRRDQDVCRTVLNHVVHIVMNLCQGSMDAENTRDAQGQFLTVIGAFWHLAKEGKCTFSVRMALVKCLKTLLEADPSSKWAILNVMGKEFPVNEVFPHFLADNHHQVSMLAAESINRLFQDMKHGGSSTFLKALPLKLQQTAFENAYSKAQEGMREVAHRAENAELVDEVYNRKSVLLMTMAVILCCSPVCEKQALFALCKAMKESGLEPHLIKKVLEKVSETFGYRHLEDFMASHLDYLVLEWLNLQDTEHSLCSFPFILLNYTNVEDFYRSCYKVLIPHLVIRSRFDEVKSIANQIQEDWKTLLTHCFPKILVNILPYFAYEGTGESETAQQRETATKVYDTLKDENLLGKQIDHLFLSNLPEIVVELLMTLHEPATSGGSQSTDLGDFSGDLDPAPNPPHFPSHVIKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSTLGGAWAFVLRDVIYTLIHYINKRPSRFMDVSLRSFSLCCDLLSRVCHTAVTYCKDALENHLHVIVGTLIPLVDDQMEVQEQVLDLLKYLVIDNKDNENLYMTIKLLDPFPDHDVFKDLRLTQQKIKYSKGPFSLLEEINHFLSVSVYDALPLTRLEGLKDLRRQLAQHKDQMMDLMRASQENPQDGIMVKLIVSLLQLCKMAVSHTGEREVLEAVGSCLGEVGPIDFSTIAIQHSRDTSSTKALEFFEDKELQWTFLTLTYLNNTLVEDCVKVRSAAVTCLKSILATKTGHTFWEIYKTTTDPMLIYLQPFRTSRKKFLEVPRLDKESPLEGLDDTSLWTPQSGNHDSWIKRLTCAFLDSGGTKSEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRTLLSTHIQGFFTNCFRHSSQTSRSTTPANLDSDPEHFFRCCVDKKSQRTMLAVVDYMRRQRRPSLGTVFDDAFWLELNYLEVAKVAQSCAAHFTALLYAEIYADKKSTDDQEKRCALVTNRSLMFEEASQNTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPLTRLRTYEHEAMWGKALVTYDLETAISSSTRQAGIIQALQNLGLCHILSVYLKGLDLENKEWCAELQELCYQAAWRNMQWDHCVSANKGMEGTSYHESVYNALQSLRDREFSTFYESLKYARVREVEELCRGSLESVYSLYPTLSRLQAIGELENIGELFSRSVPGRQPSEVYAKWRKHSQLLKDSDFSFQEPIMALRTVILEILMEKEMENSQRECFKDILTTHLVELSILARTFKNTQLPERAIFHIKQYNPPGRGVSEWQLEEAQVFWARNEQSLALSVLKQMIKKLDSSGAENDPSLRLLYTECLRVCGTWLAETCLENPAVIMQTYLEKAVEVAGNYDGESSDELRNGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTTRYTIKVQRELELDECALRALKEDRKRFLCKAVENYISCLLSGEAHDMWIFRLCSLWLENSGVSEVNGMMKSKGMNIPSYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISTIAMDHPHHTLFIILALANANKDEFLTKPEAARRSRISKNAPKQSSQLDEDRTEAANRIICTIRSRRPHMVRSVEALCDAYIILANLDATQWRTQRKGINIPADQPITKLKNLEDVVVPTMEIKVDPTGEYGNLVTIQSFKAEFHLAGGLNLPKIIDCLGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNENGAHKRYRPKDFSALQCQKKMMDVQKKSFEEKYKTFTDICQNFQPVFRYFCMEKFLDPAVWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRSSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDDAELHSTPSADDQECRRGLGDIDQSLNKVAERVLMRLQEKLKGVEEGTVLSVRGQVNLLIQQAMDPKNLSRLFPGWKAWV

Felis catus (Cat) (Felis silvestris catus)

FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9, UBQLN4 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks. {ECO:0000256|RuleBase:RU365027}.

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775, ECO:0000256|RuleBase:RU365027};

ATP-binding;Cytoplasmic vesicle;DNA damage;Kinase;Nucleotide-binding;Nucleus;Reference proteome;Serine/threonine-protein kinase;Transferase

brain development [GO:0007420]; cellular response to gamma radiation [GO:0071480]; cellular response to nitrosative stress [GO:0071500]; cellular response to reactive oxygen species [GO:0034614]; cellular response to retinoic acid [GO:0071300]; cellular response to X-ray [GO:0071481]; determination of adult lifespan [GO:0008340]; DNA damage checkpoint signaling [GO:0000077]; double-strand break repair via homologous recombination [GO:0000724]; establishment of protein-containing complex localization to telomere [GO:0097695]; establishment of RNA localization to telomere [GO:0097694]; female meiotic nuclear division [GO:0007143]; heart development [GO:0007507]; histone mRNA catabolic process [GO:0071044]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lipoprotein catabolic process [GO:0042159]; male meiotic nuclear division [GO:0007140]; meiotic telomere clustering [GO:0045141]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic spindle assembly checkpoint signaling [GO:0007094]; multicellular organism growth [GO:0035264]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of telomere capping [GO:1904354]; negative regulation of TORC1 signaling [GO:1904262]; neuron apoptotic process [GO:0051402]; oocyte development [GO:0048599]; ovarian follicle development [GO:0001541]; pexophagy [GO:0000425]; phosphorylation [GO:0016310]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of telomerase catalytic core complex assembly [GO:1904884]; positive regulation of telomere maintenance via telomerase [GO:0032212]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-embryonic development [GO:0009791]; pre-B cell allelic exclusion [GO:0002331]; regulation of autophagy [GO:0010506]; replicative senescence [GO:0090399]; somitogenesis [GO:0001756]; telomere maintenance [GO:0000723]; thymus development [GO:0048538]; V(D)J recombination [GO:0033151]

centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; cytoplasmic vesicle [GO:0031410]; DNA repair complex [GO:1990391]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; site of double-strand break [GO:0035861]; spindle [GO:0005819]

1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; DNA-dependent protein kinase activity [GO:0004677]; histone H2AXS139 kinase activity [GO:0035979]; identical protein binding [GO:0042802]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]

SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000256|RuleBase:RU365027}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.

IPR016024;IPR038980;IPR003152;IPR011009;IPR000403;IPR036940;IPR018936;IPR003151;IPR014009;IPR044107;IPR021668;

1.10.1070.11;

A0A2I2U103

MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEEE

Felis catus (Cat) (Felis silvestris catus)

2.7.1.77; 3.1.3.5; 3.1.3.99

CATALYTIC ACTIVITY: Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036349}; CATALYTIC ACTIVITY: Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592, ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00036204}; CATALYTIC ACTIVITY: Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714, ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036695}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715; Evidence={ECO:0000256|ARBA:ARBA00036695}; CATALYTIC ACTIVITY: Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584, ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036089}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000256|ARBA:ARBA00036953}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719; Evidence={ECO:0000256|ARBA:ARBA00036953}; CATALYTIC ACTIVITY: Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530, ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57464; Evidence={ECO:0000256|ARBA:ARBA00036213}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531; Evidence={ECO:0000256|ARBA:ARBA00036213}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside; Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274, ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77; Evidence={ECO:0000256|ARBA:ARBA00036260}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000256|ARBA:ARBA00035871}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485; Evidence={ECO:0000256|ARBA:ARBA00035871}; CATALYTIC ACTIVITY: Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate; Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57673; Evidence={ECO:0000256|ARBA:ARBA00036911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380; Evidence={ECO:0000256|ARBA:ARBA00036911}; CATALYTIC ACTIVITY: Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP; Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596, ChEBI:CHEBI:57673, ChEBI:CHEBI:58053; Evidence={ECO:0000256|ARBA:ARBA00036593}; CATALYTIC ACTIVITY: Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate; Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194; Evidence={ECO:0000256|ARBA:ARBA00036191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384; Evidence={ECO:0000256|ARBA:ARBA00036191}; CATALYTIC ACTIVITY: Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572, ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053, ChEBI:CHEBI:61194; Evidence={ECO:0000256|ARBA:ARBA00036258}; CATALYTIC ACTIVITY: Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588, ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865, ChEBI:CHEBI:58053; Evidence={ECO:0000256|ARBA:ARBA00036826};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR017434-2}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};

Allosteric enzyme;ATP-binding;Cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Reference proteome;Transferase

adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; dGMP metabolic process [GO:0046054]; GMP metabolic process [GO:0046037]; IMP catabolic process [GO:0006204]; IMP metabolic process [GO:0046040]; negative regulation of defense response to virus by host [GO:0050689]; protein K48-linked ubiquitination [GO:0070936]

cytosol [GO:0005829]

5'-nucleotidase activity [GO:0008253]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; IMP 5'-nucleotidase activity [GO:0050483]; metal ion binding [GO:0046872]; nucleoside phosphotransferase activity [GO:0050146]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.

IPR036412;IPR008380;IPR023214;IPR016695;

3.40.50.1000;

A0A2I2U3H7

MSAPPVLRPPSPLLPVAAAAAAAAAALGSGPGPAPFLAPVAAPAGGISFHLQIGLSREPVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKTASDIQEGDLIEVVLSASATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGLSTIRTASAELSTSAPDEPLLSPVSPGFEQKSPSESFIGREKRSNSQSYIGRPIQLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCRFNCHKRCASKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDMEEAMVQDTEVVMAECQNDSGEMQDPDPDPEESNRTISPSTSNNIPLMRVVQSVKHTKRKSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPAKPSALIPNGANPHCFEITTANVVYYVGENVVNPSSPPPNSSVLTSGVGVDVARMWEMAIQHALMPVIPKGSTVGSGTNSHREISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELECKIGERYITHESDDLRWEQYAGLGSEPPQFCNEVPKSCCSRGRSLKPGKVLAWWAFSGDWRSLKSSVLALAR

Felis catus (Cat) (Felis silvestris catus)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569, ECO:0000256|PIRNR:PIRNR000552};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR000552};

ATP-binding;Cytoplasm;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc

cellular response to amino acid starvation [GO:0034198]; cellular response to hydroperoxide [GO:0071447]; defense response to Gram-negative bacterium [GO:0050829]; Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; intracellular signal transduction [GO:0035556]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of autophagy [GO:0010508]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [GO:0038033]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of keratinocyte proliferation [GO:0010837]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]

autophagosome membrane [GO:0000421]; cell cortex [GO:0005938]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]

ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatidylinositol 3-kinase activator activity [GO:0141038]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000552}. Membrane {ECO:0000256|ARBA:ARBA00004370}.

IPR046349;IPR020454;IPR011009;IPR002219;IPR011993;IPR001849;IPR000719;IPR017441;IPR015727;IPR008271;

3.30.60.20;2.30.29.30;1.10.510.10;

A0A2I2U469

MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISSTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEVTLMDANYVMDETLGTATFPISSIRVGEKKEVPFIFNQVTEMFLEMSLEVCSSPDLRFSMALCDQEKTFRQQRKENIKENMKKLLGPEKSGGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYIESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNSAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAEHIVSNDSSDSDDESQEPKGTENEDAKREYQNDNQASWVHRMLMALVSDSTLFNTREGRAGKVHNFMLGLNLNTSYPISPLKDFTTQESLDEDELDTAVADPDEFEQIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPNVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRNYKAPGVPRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKNAIVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLSKPAA

Felis catus (Cat) (Felis silvestris catus)

3.1.1.4

CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:60657, ChEBI:CHEBI:74344; Evidence={ECO:0000256|ARBA:ARBA00036248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41076; Evidence={ECO:0000256|ARBA:ARBA00036248}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:41123, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72828, ChEBI:CHEBI:75163; Evidence={ECO:0000256|ARBA:ARBA00036487}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41124; Evidence={ECO:0000256|ARBA:ARBA00036487}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41271, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:77695, ChEBI:CHEBI:77696; Evidence={ECO:0000256|ARBA:ARBA00036365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272; Evidence={ECO:0000256|ARBA:ARBA00036365}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41071, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:77694; Evidence={ECO:0000256|ARBA:ARBA00035962}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41072; Evidence={ECO:0000256|ARBA:ARBA00035962}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:55430, ChEBI:CHEBI:64496; Evidence={ECO:0000256|ARBA:ARBA00036736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068; Evidence={ECO:0000256|ARBA:ARBA00036736}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000256|ARBA:ARBA00023922}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000256|ARBA:ARBA00023922}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000256|ARBA:ARBA00023408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000256|ARBA:ARBA00023408}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000256|ARBA:ARBA00000597}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000256|ARBA:ARBA00000597}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:40451, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:74565, ChEBI:CHEBI:77091; Evidence={ECO:0000256|ARBA:ARBA00036986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40452; Evidence={ECO:0000256|ARBA:ARBA00036986}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; Evidence={ECO:0000256|ARBA:ARBA00036574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; Evidence={ECO:0000256|ARBA:ARBA00036574}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41099, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:75612; Evidence={ECO:0000256|ARBA:ARBA00035999}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41100; Evidence={ECO:0000256|ARBA:ARBA00035999}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387, ChEBI:CHEBI:73858, ChEBI:CHEBI:78022; Evidence={ECO:0000256|ARBA:ARBA00036797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41308; Evidence={ECO:0000256|ARBA:ARBA00036797}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41087, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:75610, ChEBI:CHEBI:78022; Evidence={ECO:0000256|ARBA:ARBA00036898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41088; Evidence={ECO:0000256|ARBA:ARBA00036898}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphocholine + H2O = H(+) + prostaglandin E2 + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:137585, ChEBI:CHEBI:606564; Evidence={ECO:0000256|ARBA:ARBA00036679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53693; Evidence={ECO:0000256|ARBA:ARBA00036679}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphoethanolamine + H2O = H(+) + prostaglandin E2 + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:53704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:137581, ChEBI:CHEBI:143890, ChEBI:CHEBI:606564; Evidence={ECO:0000256|ARBA:ARBA00036609}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53705; Evidence={ECO:0000256|ARBA:ARBA00036609}; CATALYTIC ACTIVITY: Reaction=2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:78836, ChEBI:CHEBI:137582; Evidence={ECO:0000256|ARBA:ARBA00036785}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53689; Evidence={ECO:0000256|ARBA:ARBA00036785}; CATALYTIC ACTIVITY: Reaction=2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:78837, ChEBI:CHEBI:137583; Evidence={ECO:0000256|ARBA:ARBA00035771}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53697; Evidence={ECO:0000256|ARBA:ARBA00035771}; CATALYTIC ACTIVITY: Reaction=2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:57409, ChEBI:CHEBI:137584; Evidence={ECO:0000256|ARBA:ARBA00036533}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53701; Evidence={ECO:0000256|ARBA:ARBA00036533}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000256|ARBA:ARBA00023422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000256|ARBA:ARBA00023422}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000256|ARBA:ARBA00000150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000256|ARBA:ARBA00000150};

PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000256|ARBA:ARBA00037916}.; PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. {ECO:0000256|ARBA:ARBA00004716}.; PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702}.; PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000256|ARBA:ARBA00037925}.

Calcium;Cytoplasm;Fatty acid biosynthesis;Fatty acid metabolism;Glycerol metabolism;Hydrolase;Leukotriene biosynthesis;Lipid biosynthesis;Lipid degradation;Lipid metabolism;Metal-binding;Phospholipid degradation;Phospholipid metabolism;Prostaglandin biosynthesis;Prostaglandin metabolism;Reference proteome

arachidonic acid metabolic process [GO:0019369]; glycerol metabolic process [GO:0006071]; glycerophospholipid catabolic process [GO:0046475]; leukotriene biosynthetic process [GO:0019370]; monoacylglycerol biosynthetic process [GO:0006640]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylglycerol catabolic process [GO:0034478]; positive regulation of platelet activation [GO:0010572]; prostaglandin biosynthetic process [GO:0001516]

cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]

calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; calcium-independent phospholipase A2 activity [GO:0047499]; ceramide 1-phosphate binding [GO:1902387]; lysophospholipase activity [GO:0004622]; O-acyltransferase activity [GO:0008374]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.

DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. {ECO:0000256|RuleBase:RU362102}.

IPR016035;IPR041847;IPR000008;IPR035892;IPR002642;

2.60.40.150;3.40.1090.10;

A0A2I2UA97

MQKEARAGGADGVNSAGNGDGPAAETPQPRGPPGAAPPRPRPLPGRRPRRSRDPARRPLGPEGAARGRGGLARRGPSGAGRSGPRAGGGSRRARPFPAPRGAHARSSCCPSLRAGTPGGRREDMASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRKEIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAAAARDAPQSPGAGSQACSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRAGQLESQAAPDDAQGSADLGSVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVCEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAVASSAAFSARLAGPFPPTHYNTLCKPAPLTGTLEVRVVGCRDLPETVPWSSSPSVGVPGTPDSRTTFLSRPARGLYSRSGSLSGRGSLKVEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKTFQRARQMNIDVATWVRLLRRLIPNATATGTFSPGASPGPEARSTGDVSMEKLNLGADLDSLPQKSPLGPPSSPSSLSSPIQETTTTPELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTRAAHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWDTLLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTATEQAAFRDFDFVAGGC

Felis catus (Cat) (Felis silvestris catus)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};

ATP-binding;Coiled coil;Cytoplasm;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase

B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; epithelial cell migration [GO:0010631]; hyperosmotic response [GO:0006972]; intracellular signal transduction [GO:0035556]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of protein phosphorylation [GO:0001933]; phosphorylation [GO:0016310]; post-translational protein modification [GO:0043687]; regulation of cell motility [GO:2000145]; regulation of germinal center formation [GO:0002634]; regulation of immunoglobulin production [GO:0002637]; regulation of transcription by RNA polymerase II [GO:0006357]; renal system process [GO:0003014]; spleen development [GO:0048536]

cleavage furrow [GO:0032154]; endosome [GO:0005768]; midbody [GO:0030496]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; histone H3T11 kinase activity [GO:0035402]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR000008;IPR035892;IPR037784;IPR011072;IPR036274;IPR011009;IPR017892;IPR037317;IPR037313;IPR000719;IPR017441;IPR008271;

1.10.287.160;1.10.510.10;

A0A2I2UBF8

MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDECALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQALLQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLTDQTSGDQSPLPPCTPTPSCAEMREDNARVYENVGLMQQQKSFR

Felis catus (Cat) (Felis silvestris catus)

3.1.3.48

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000256|ARBA:ARBA00001490, ECO:0000256|PIRNR:PIRNR000929};

Cytoplasm;Hydrolase;Protein phosphatase;Reference proteome;SH2 domain

atrioventricular canal development [GO:0036302]; axonogenesis [GO:0007409]; Bergmann glial cell differentiation [GO:0060020]; cellular response to epidermal growth factor stimulus [GO:0071364]; cerebellar cortex formation [GO:0021697]; dephosphorylation [GO:0016311]; DNA damage checkpoint signaling [GO:0000077]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; face morphogenesis [GO:0060325]; fibroblast growth factor receptor signaling pathway [GO:0008543]; genitalia development [GO:0048806]; glucose homeostasis [GO:0042593]; homeostasis of number of cells within a tissue [GO:0048873]; hormone metabolic process [GO:0042445]; hormone-mediated signaling pathway [GO:0009755]; inner ear development [GO:0048839]; integrin-mediated signaling pathway [GO:0007229]; intestinal epithelial cell migration [GO:0061582]; megakaryocyte development [GO:0035855]; microvillus organization [GO:0032528]; multicellular organism growth [GO:0035264]; multicellular organismal reproductive process [GO:0048609]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of cortisol secretion [GO:0051463]; negative regulation of growth hormone secretion [GO:0060125]; negative regulation of insulin secretion [GO:0046676]; negative regulation of type I interferon production [GO:0032480]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ growth [GO:0035265]; platelet formation [GO:0030220]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of glucose import [GO:0046326]; positive regulation of hormone secretion [GO:0046887]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of ossification [GO:0045778]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of protein export from nucleus [GO:0046825]; regulation of protein-containing complex assembly [GO:0043254]; triglyceride metabolic process [GO:0006641]

cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

cadherin binding [GO:0045296]; cell adhesion molecule binding [GO:0050839]; insulin receptor binding [GO:0005158]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; peptide hormone receptor binding [GO:0051428]; phosphotyrosine residue binding [GO:0001784]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor complex adaptor activity [GO:0030159]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000929}.

IPR029021;IPR000242;IPR000980;IPR036860;IPR016130;IPR003595;IPR000387;IPR012152;

3.90.190.10;3.30.505.10;

A0A2I2UBG1

MNPASGTPINSPRMEGRGLQSPGELQKGVGWGGGSRASLPVTWFQTDQSRACPRLRLHISDHLTTPDTHVGARRARILCARVRRSQAGSRAGNAVKILLRWATWYRFRRAFATVMPKRGKKGAVAEDGEEPKIEPEAKKSKVGAKKNEKEAAGEGPVLYEDPPDQKTSPSGKSATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLEAVPLADSFRHLYPNTAYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL

Felis catus (Cat) (Felis silvestris catus)

FUNCTION: Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. {ECO:0000256|RuleBase:RU362131}.

3.1.-.-

CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000256|ARBA:ARBA00000493};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000256|PIRSR:PIRSR604808-2, ECO:0000256|RuleBase:RU362131}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

Cytoplasm;DNA damage;DNA recombination;DNA repair;DNA-binding;Endonuclease;Exonuclease;Hydrolase;Magnesium;Manganese;Metal-binding;Mitochondrion;Nuclease;Nucleus;Reference proteome

base-excision repair [GO:0006284]; cell redox homeostasis [GO:0045454]; DNA catabolic process [GO:0006308]; DNA recombination [GO:0006310]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488]; telomere maintenance via base-excision repair [GO:0097698]

centrosome [GO:0005813]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]

chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; double-stranded telomeric DNA binding [GO:0003691]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands [GO:0090580]; phosphoric diester hydrolase activity [GO:0008081]; site-specific endodeoxyribonuclease activity, specific for altered base [GO:0016890]; transcription coactivator activity [GO:0003713]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU362131}. Cytoplasm {ECO:0000256|RuleBase:RU362131}. Mitochondrion {ECO:0000256|RuleBase:RU362131}.

IPR004808;IPR020847;IPR020848;IPR036691;IPR005135;

3.60.10.10;

A0A2I2UCU6

MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNGDSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA

Felis catus (Cat) (Felis silvestris catus)

2.4.1.255

PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922}.

Glycosyltransferase;Reference proteome;Repeat;TPR repeat;Transferase

apoptotic process [GO:0006915]; cellular response to glucose stimulus [GO:0071333]; circadian regulation of gene expression [GO:0032922]; hemopoiesis [GO:0030097]; mitophagy [GO:0000423]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of proteolysis [GO:0045862]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]; positive regulation of translation [GO:0045727]; protein O-linked glycosylation [GO:0006493]; protein processing [GO:0016485]; regulation of gluconeogenesis [GO:0006111]; regulation of glycolytic process [GO:0006110]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of Rac protein signal transduction [GO:0035020]; regulation of synapse assembly [GO:0051963]; response to insulin [GO:0032868]

cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; NSL complex [GO:0044545]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122]

chromatin DNA binding [GO:0031490]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein O-acetylglucosaminyltransferase activity [GO:0097363]

IPR029489;IPR011990;IPR001440;IPR019734;

3.30.720.150;3.40.50.11380;3.40.50.2000;1.25.40.10;

A0A2I2UDJ9

MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRANGPDGAIGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRVVKEEEARGLAEKYGIPYFETSAANGTNINQAIEMLLDLIMKRMERCVDKSWIPEGVVRSNGHTSTDHLNEEKEKGICGC

Felis catus (Cat) (Felis silvestris catus)

3.6.5.2

CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000256|ARBA:ARBA00000249}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000256|ARBA:ARBA00000249};

Acetylation;Disulfide bond;Membrane;Nucleotide-binding;Reference proteome

antigen processing and presentation [GO:0019882]; blood coagulation [GO:0007596]; complement-dependent cytotoxicity [GO:0097278]; cytotoxic T cell degranulation [GO:0043316]; exocytosis [GO:0006887]; exosomal secretion [GO:1990182]; melanocyte differentiation [GO:0030318]; melanosome transport [GO:0032402]; multivesicular body organization [GO:0036257]; multivesicular body sorting pathway [GO:0071985]; natural killer cell degranulation [GO:0043320]; positive regulation of constitutive secretory pathway [GO:1903435]; positive regulation of exocytosis [GO:0045921]; positive regulation of gene expression [GO:0010628]; positive regulation of phagocytosis [GO:0050766]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of regulated secretory pathway [GO:1903307]; protein secretion [GO:0009306]

apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; exocytic vesicle [GO:0070382]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; melanosome [GO:0042470]; multivesicular body membrane [GO:0032585]; photoreceptor outer segment [GO:0001750]; secretory granule [GO:0030141]

G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; myosin V binding [GO:0031489]

SUBCELLULAR LOCATION: Endosome {ECO:0000256|ARBA:ARBA00004177}. Late endosome {ECO:0000256|ARBA:ARBA00004603}. Lysosome {ECO:0000256|ARBA:ARBA00004371}.

IPR027417;IPR041837;IPR005225;IPR001806;

3.40.50.300;

A0A2I2UE37

MGAGAGRGAATAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELANCSVIEGHLQILLMFKTRPEDFRDLSFPKLVMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVVFEMVHLKELGLYSLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHGHCQKVCPTVCKSHGCTADGLCCHSECLGNCSEPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCRDLHNKCKNSRRQGCHQYVIHNNRCIPECPSGYTMNSSNLMCTPCLGPCPKVCHILEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSYDKILLKWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELYELDYCLKGLKLPSRTWSPPFESEGSQKRNQSEYEESAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKSFSSPGAEDSRPSRKRRALADAGNVTAAVPTVPGFPNTSSSVPTSPEEHKPFEKVVNKESLVISGLRHFTGYRIELQACNQDAPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRRHFALERGCRLRGLPPGNYSVRVRATSLAGNGSWTEATYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVPREKITLLRELGQGSFGMVYEGNARDIVKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMVHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMHMCWQFNPKMRPTFLEIVDLLKDDLHPSFPEVSFFHSEENKAPESEELEMEFEDMESVPLDRASHSQREEAGGRDGVSSLGLKRNYEDHIPYTHMNGGKKNGRILTLPRSNPS

Felis catus (Cat) (Felis silvestris catus)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171, ECO:0000256|RuleBase:RU000312};

ATP-binding;Glycoprotein;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

adrenal gland development [GO:0030325]; cellular response to growth factor stimulus [GO:0071363]; epidermis development [GO:0008544]; exocrine pancreas development [GO:0031017]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; heart morphogenesis [GO:0003007]; male gonad development [GO:0008584]; male sex determination [GO:0030238]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of developmental growth [GO:0048639]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of glycolytic process [GO:0045821]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor internalization [GO:0002092]; positive regulation of respiratory burst [GO:0060267]; receptor internalization [GO:0031623]; regulation of embryonic development [GO:0045995]; regulation of female gonad development [GO:2000194]; symbiont entry into host cell [GO:0046718]

axon [GO:0030424]; caveola [GO:0005901]; insulin receptor complex [GO:0005899]; nuclear envelope [GO:0005635]; nuclear lumen [GO:0031981]

amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein-containing complex binding [GO:0044877]; PTB domain binding [GO:0051425]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR003961;IPR036116;IPR006211;IPR006212;IPR009030;IPR013783;IPR040969;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR008266;IPR020635;IPR016246;IPR002011;

2.60.40.10;3.80.20.20;1.10.510.10;

A0A2I2UEI7

MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGIYQGKQLFQCDEDCGVFVALDKLEILEDDDNGLESDYAGPGDTVQMELPPLEINSRVSLKLGETTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPDSVTQERRPPKLAFMSRGVADKGSSSHNKPKATGPTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISSDFGHASPPLQPPSMNSLSTENRFHSLPFSLTKMPNANGSIGHSPLSLSVQSVMGELNNAPVQESPPLAMASGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGNIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSPEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMRGNRGSLWVPKKREKQNCGMKVKNRFSLSATLG

Felis catus (Cat) (Felis silvestris catus)

3.4.19.12

CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};

Cell membrane;Cell projection;Cytoplasm;Cytoskeleton;Immunity;Innate immunity;Membrane;Microtubule;Reference proteome;Repeat;Ubl conjugation;Wnt signaling pathway

CD4-positive or CD8-positive, alpha-beta T cell lineage commitment [GO:0043369]; homeostasis of number of cells [GO:0048872]; innate immune response [GO:0045087]; necroptotic process [GO:0070266]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-18-mediated signaling pathway [GO:2000493]; negative regulation of JNK cascade [GO:0046329]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of p38MAPK cascade [GO:1903753]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of protein localization [GO:1903829]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T cell receptor signaling pathway [GO:0050862]; regulation of B cell differentiation [GO:0045577]; regulation of cilium assembly [GO:1902017]; regulation of intrinsic apoptotic signaling pathway [GO:2001242]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of mitotic cell cycle [GO:0007346]; regulation of necroptotic process [GO:0060544]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; ripoptosome assembly involved in necroptotic process [GO:1901026]; Wnt signaling pathway [GO:0016055]

centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; cytoplasmic microtubule [GO:0005881]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; midbody [GO:0030496]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]

cysteine-type deubiquitinase activity [GO:0004843]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked deubiquitinase activity [GO:0061578]; proline-rich region binding [GO:0070064]; protein kinase binding [GO:0019901]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.

IPR036859;IPR000938;IPR038765;IPR001394;IPR018200;IPR028889;

2.30.30.190;3.90.70.10;

A0A2I2UFY5

MENFQKVEKIGEGTYGVVYKAKNKVTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMHLVCTQHHARCCGEHRRNGRHSLCPLCSYLEVAASQGGGMTAVSTPHPVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL

Felis catus (Cat) (Felis silvestris catus)

2.7.11.22

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000256|ARBA:ARBA00000584}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000256|ARBA:ARBA00000875};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;DNA damage;DNA repair;Kinase;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase

centriole replication [GO:0007099]; DNA repair [GO:0006281]; DNA-templated transcription [GO:0006351]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phosphorylation [GO:0016310]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated DNA replication initiation [GO:0032298]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of heterochromatin formation [GO:0031453]; post-translational protein modification [GO:0043687]; potassium ion transport [GO:0006813]; Ras protein signal transduction [GO:0007265]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of gene expression [GO:0010468]; response to organic substance [GO:0010033]; signal transduction [GO:0007165]

Cajal body [GO:0015030]; centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; condensed chromosome [GO:0000793]; cyclin A1-CDK2 complex [GO:0097123]; cyclin A2-CDK2 complex [GO:0097124]; cyclin E1-CDK2 complex [GO:0097134]; cyclin E2-CDK2 complex [GO:0097135]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; endosome [GO:0005768]; male germ cell nucleus [GO:0001673]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]; X chromosome [GO:0000805]; Y chromosome [GO:0000806]

ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; histone kinase activity [GO:0035173]; magnesium ion binding [GO:0000287]; protein domain specific binding [GO:0019904]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, Cajal body {ECO:0000256|ARBA:ARBA00004408}.

IPR011009;IPR000719;IPR017441;IPR008271;

1.10.510.10;