Datasets:

lhallee

/

exp_new_unprocessed

like 0

A0A3Q1LRR9

MALRRSMGRSGLPPLPRPPPPPLLLLAGLAVLLLPEPAAAGLKLMGAPVKLTVSQGQPVKLNCSVEGMEEPEIQWVKDGAVVHSMDQVYIPVSEQHWIGFLSLKSVERSDAGRYWCQVEDGDETETSQPVWLTVEGVPFFTVEPKDLAVPPNAPFQLFCEAVGPPEPVTIIWWRGGTQVGEPAPSPSVLNVTGVTQSTVFSCEAHNPKGLASSRTATVHLQALPAAPFNITVTKLSSSNVSVAWMPGADGRALIQSCTVQVTQAPGDWEVLAVMVPVPPFTCLLRDLTPATNYSLRVRCANALGPSPYADWVPFRTKGLAPASAPKNLRAIRTDSGLILEWEEVIPEGPSEGPLGPYKMSWAQDNGTQGELTVEGTRANLTGWDPQKDLTVRVCVANAVGCGPWSQPLVVSSHDHAGQQGAPHSRTSWVPVVLGVLTALVTAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKDKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLSSRIGENPFNLPLQTLVRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVHSDVWAFGVTMWEIVTRGQTPYAGIENAEIYNYLIGGNRLKQPPECMEDVYELMYQCWSADPKQRPSFTCLRMELETVLGRLSVLSASQDPLYINLEGAQEPTEGGDLELPGGDQASSGAGDGSGLGAVGGTPSDYRYILSPGELTEQPGHGEQQPESPVSESQRLLLLQQGLLPHSSC

Bos taurus (Bovine)

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;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

apoptotic cell clearance [GO:0043277]; cell migration [GO:0016477]; establishment of localization in cell [GO:0051649]; forebrain cell migration [GO:0021885]; natural killer cell differentiation [GO:0001779]; negative regulation of inflammatory response [GO:0050728]; negative regulation of innate immune response [GO:0045824]; negative regulation of lymphocyte activation [GO:0051250]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; nervous system development [GO:0007399]; neuron apoptotic process [GO:0051402]; neuron cellular homeostasis [GO:0070050]; neuron migration [GO:0001764]; neuropeptide signaling pathway [GO:0007218]; ovulation cycle [GO:0042698]; phagocytosis [GO:0006909]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; platelet aggregation [GO:0070527]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of viral life cycle [GO:1903902]; 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]

cell surface [GO:0009986]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphatidylinositol 3-kinase binding [GO:0043548]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; virus receptor activity [GO:0001618]

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}.

IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR013151;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;

2.60.40.10;1.10.510.10;

A0A3Q1LVP1

MSGVSEALSRVKVGTLRRPEGPPEPMVVVPVDVEKEDVRILKVCFYGNSFNSGKNFKLVKCTVQTEIRDVIASILLSGRIGPNIQLADCYGLRLKHMKSDEIHWLHPLMTVGEVQDKYECLHVEAEWRYDLQVRYLPEDFMESLKEDKTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNLELLEREVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIKSIRCLPLEEGQAVLQLGIEGAPQSLSIKTSSLAEAENMADLVDGYCRLQGEHKGSLIIRTKKDGEKRNSLPQIPTLNLEARRPHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEVINVAVKTCKKNCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEEYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPILYTLMTRCWDYDPSERPRFTELVCSLSDIYQMEKDIALEQERNARYRPPKILEPTAFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFVRPSSREEAQQLWEAERLKMRQLLDKQQKQMVEDYQWLRQEEKALDPMVYMNDKSPLTPEKEAGYTEFTAPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLDLKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLARPLAE

Bos taurus (Bovine)

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};

ATP-binding;Cell junction;Cell membrane;Cell projection;Kinase;Membrane;Nucleotide-binding;Reference proteome;Transferase;Tyrosine-protein kinase

bone resorption [GO:0045453]; cellular response to fluid shear stress [GO:0071498]; cellular response to retinoic acid [GO:0071300]; chemokine-mediated signaling pathway [GO:0070098]; cortical cytoskeleton organization [GO:0030865]; endothelin receptor signaling pathway [GO:0086100]; epidermal growth factor receptor signaling pathway [GO:0007173]; integrin-mediated signaling pathway [GO:0007229]; marginal zone B cell differentiation [GO:0002315]; negative regulation of apoptotic process [GO:0043066]; negative regulation of bone mineralization [GO:0030502]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of potassium ion transport [GO:0043267]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell chemotaxis [GO:2000538]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of JNK cascade [GO:0046330]; positive regulation of neuron projection development [GO:0010976]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; regulation of cell adhesion [GO:0030155]; regulation of cell shape [GO:0008360]; regulation of macrophage chemotaxis [GO:0010758]; regulation of postsynaptic density assembly [GO:0099151]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; signal complex assembly [GO:0007172]; sprouting angiogenesis [GO:0002040]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]

cell cortex [GO:0005938]; cytoskeleton [GO:0005856]; dendritic spine [GO:0043197]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density, intracellular component [GO:0099092]; presynapse [GO:0098793]

ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein self-association [GO:0043621]

SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.

IPR019749;IPR041390;IPR049385;IPR041784;IPR014352;IPR035963;IPR019748;IPR000299;IPR036137;IPR005189;IPR011009;IPR011993;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR029071;

1.20.80.10;1.20.120.330;2.30.29.30;1.10.510.10;

A0A3Q1M0F0

MGAEEVGRLATVTLARTGARRRGAREPAPRSGWWGRSRRRRRRRRRSRGAAARGPLLARAAEDRRRPPACRPEPSTASMIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLLDIMNRFKKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEQNQAVHMESEVYDTPENIMHGSGSQLFDHVAECLGDFMEKKKIKDKKLPVGFTFSFPCRQSRIDEAILITWTKRFKASGVEGTDVVKLLDKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCVNTEWGAFGDDGALEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVAVQHVCTIVSFRSANLVAATLGAILSRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDCDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFSLTKEMLLEVKKRMRAEMELGLGKQTHDKAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRSVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPKMPLGFTFSFPCKQTSLDAGILITWTKGFKATDCVGHDVATLLREAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVETLEGNQGQMCINMEWGAFGDNGCLDDIRTIYDKLVDEFSLNSGKQRYEKMISGMYLGEIVRNILIDFAKRGFLFRGQISEPLKTRGLFQTKYLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRLRQEMSS

Bos taurus (Bovine)

2.7.1.1

CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00001397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000256|ARBA:ARBA00001397}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+); Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00043797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949; Evidence={ECO:0000256|ARBA:ARBA00043797}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00000435}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000256|ARBA:ARBA00000435}; CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00000417}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000256|ARBA:ARBA00000417}; CATALYTIC ACTIVITY: Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00043834}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; Evidence={ECO:0000256|ARBA:ARBA00043834};

PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000256|ARBA:ARBA00004888}.; PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000256|ARBA:ARBA00005028}.

Allosteric enzyme;ATP-binding;Glycolysis;Immunity;Inflammatory response;Innate immunity;Kinase;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Transferase

canonical glycolysis [GO:0061621]; carbohydrate phosphorylation [GO:0046835]; establishment of protein localization to mitochondrion [GO:0072655]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intracellular glucose homeostasis [GO:0001678]; maintenance of protein location in mitochondrion [GO:0072656]; positive regulation of cytokine production involved in immune response [GO:0002720]; positive regulation of interleukin-1 beta production [GO:0032731]

cytosol [GO:0005829]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]

ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; mannokinase activity [GO:0019158]; peptidoglycan binding [GO:0042834]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004450}.

IPR043129;IPR001312;IPR019807;IPR022673;IPR022672;

3.30.420.40;3.40.367.20;

A0A3Q1M2R1

MPVQAPQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQTTINTDIELLPVNSALLQLVGAQVPEQQPITLCSGVEDTKHYEEAKKCVEELALYLKPLSSARGVGLNSTTQSVLSRPMQRKLVTLVHCQLVEEEGRIRAMRAARSLGERTVTELILQHQNPQQLSSNLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQTPASFAQSVQELTIALQRTGDPANLNRLRPHLELLANIDPSPDAPPPTWEQLENGLVAVRTVVHGLVDYIQNHSKKGTDQQQPPQHSKYKTYMCRDMKQRGGCPRGASCTFAHSQEELEKFRKMNKRLVPRRPLSASLGQLNEVGLPSTAILQEEGAVDLPSRKTPALPNGIVSAGNAVTQLIPRGTDPSYESSLKPGKIDHLSSSAPGSPPDLLESVPKSISTLPVNPHPVPPRGPTELPPMPVTKPLQMVARGSQLYPAQQADVYYQDPRGAAPPFESAPYQQGMYYAPPPQCVSRFVRPPPSAPEPGAPYLDHYPPYLQDRVVNSQYGTQPQQYPPMYPPHYDGRRVYPAQSYAREEIFRESPIPIEIPPAAVPPYVPEPRERYQQMEGYYPVAAHPTQIRPSYNREPPYSRLPPPPQPHPSLDELHRRRKEIMAQLEERKVISPPPFAPSPTLPSAFHQEEFLDEDLKVAGKYKGNDYSQYSPWSCDTIGSYIGTKDAKPKDVVAAGSVEMMNVESKGMRDQRLDLQRRAAETSDDDLIPFGDRPTVSRFGAISRTSKTIYQGAGPMQAMAPQGAPTKSINISDYGPYGTHGGWGGSPYSPHQNIPSQGHFSERERISMSEVASHGKPLPSAEREQLRLELQQLNHQISQQTQLRGLEREANTLAGQSQPPPPPPPKWPGMISSEQLSLELHQVEREIGKRTRELSMENQCSLDVKSKLNTSKQAENGQPEPQNKVPAEDLTLTFSDVPNGSALTQENISLLSNKTSSLNLSEDPEGGGDNNDSQRSGVTSSSTP

Bos taurus (Bovine)

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

3'-UTR-mediated mRNA destabilization [GO:0061158]; B cell homeostasis [GO:0001782]; lymph node development [GO:0048535]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of germinal center formation [GO:0002635]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; P-body assembly [GO:0033962]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; protein polyubiquitination [GO:0000209]; regulation of miRNA metabolic process [GO:2000628]; regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900151]; regulation of T cell receptor signaling pathway [GO:0050856]; 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]

cytoplasmic stress granule [GO:0010494]; P-body [GO:0000932]

CCR4-NOT complex binding [GO:1905762]; double-stranded RNA binding [GO:0003725]; miRNA binding [GO:0035198]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; RNA stem-loop binding [GO:0035613]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]

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;

A0A3Q1M6K1

MTRGGGSGSRRGRGSRDPGAARQGWAPLAPPCEAPRRPGTRSPRRSRAGLRRVAAAAAAAMSPGKPGAGGAGTRRTGGRRRRRRRRLEAVTQAPGLGRTAGPGSRVPGTFQGARGMKPAAREARPPPRSPGLRWALPPLLLLLRLGQILCADNCTSKSPWTAAPENLVTTVMHSNGQFTQADSRTFSPLDPESSPVKAVTTSPSSVTATWKNSTTASDSMGGIKSTNENLHTSFANQTGDNSMDSGPGGNGTSGDTTVEPHPVMDLRAAFVGVTHVTLTWKTDNITDTCRMLLEGSQELTTNLTVNIFDLKPGSQYTVTLYPLGLNETQGSPLSTENGLDAGNTDSLPGGPAAPGSKYRLERAGPSSDASLAPHTMEVLLLRLKPGTQYKATVYPQADKGAEGQPQATEFKTNSSQVFDIKFVNISATSLTMTWKINDNESSSVYTYKIQVVDETDSFNLIVNETHAVITELSSGTLYNITVYPVLEDGSEGTPGFIQVYTPPSPVSDFRVTSVSTREVGLAWNSNDTHSFEIHITPHEAGEPRIITTTEQSIVFGGLYPGTMYRFDIYPQGPNGTKGDSQTVSTTTDCSAVFDIRVINVTTTDMQLAWQNTDNASEYIYSVEIQSEHSSDRKNSSHTGIAFHDLTPGTLYKITVTPQMDFVQGLANSTLQYTRPSKVSSIEIMTNTTAATLNWQNVDEASSNYTYCLLIRQDGSSSNFPPIVTDVGVTHATVTNLIPGSSYTVEIFTRMGDVKSLGPSRQSFCTDPESVASFDCEAVPKKATLVLRWACPLGTSTGFELEVSHGYWKNKTTLEGCSLNNGSEFMTEVTHLNFSTLYDISIATHSCNKTAPPAQNTCLSGITDPPLPDGSPNITSVSHNSVKVKFSGFEASHGPIKAYALVLTTVDADRPSADVLRFTYGDFKRGASNTYVTYLITTEAKRRAQGLSEVLKYEVDVGNESTTHGYYNGKLEPLGSYRACVAGFTNIAFNPRNAGLIDGNESYVSFSPCSEAVFLPQDPGVICGAVFGCIFGALVIVAVGGFIFWRRRSRKGVKNNDVTFSQIKPKKSKLIKVENFEAYFKKQQADSNCGFAEEYEDLKLVGINLPKYAAELAENRGKNRYNNVLPYDVSRVKLSVQTHSTDDYINANYMPGYHSKEDFIATQGPLPNTLKDFWRMVWEKNVYAVVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNTPTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHCSAGVGRTGTFVAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIRSQKDSKVDLIYQNTTAMTIYENLSPITTFGKTNGYIA

Bos taurus (Bovine)

5.2.1.8

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}; CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|PROSITE-ProRule:PRU00277};

Glycoprotein;Hydrolase;Isomerase;Membrane;Protein phosphatase;Reference proteome;Rotamase;Signal;Transmembrane

B cell differentiation [GO:0030183]; blood coagulation [GO:0007596]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; dephosphorylation [GO:0016311]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of vascular permeability [GO:0043116]; oligodendrocyte differentiation [GO:0048709]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive chemotaxis [GO:0050918]; positive regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060369]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of platelet activation [GO:0010572]; positive regulation of tumor necrosis factor production [GO:0032760]; vasculogenesis [GO:0001570]

cell surface [GO:0009986]; cell-cell junction [GO:0005911]; immunological synapse [GO:0001772]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]

beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; delta-catenin binding [GO:0070097]; gamma-catenin binding [GO:0045295]; mitogen-activated protein kinase binding [GO:0051019]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; platelet-derived growth factor receptor binding [GO:0005161]; protein tyrosine phosphatase activity [GO:0004725]

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}.

IPR003961;IPR036116;IPR013783;IPR001179;IPR029021;IPR000242;IPR041201;IPR016130;IPR003595;IPR000387;

2.60.40.10;3.90.190.10;

A0A3Q1M6Q8

MKTLLLLALIMAFALPALLQVRGNLVDFQKKIKYMTGGEPVTTDGFLDCSCVVVAEDPPKDAMDRCCAVNDCCYKKLKNHRCGTTSLKYNFTLCWGLIDYCKHQVCECDQIAILCSARNKKTYNKKLQYYSNRQCKGSTPKCLRSP

Bos taurus (Bovine)

3.1.1.4

CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) + hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829, ChEBI:CHEBI:75158; Evidence={ECO:0000256|ARBA:ARBA00036461}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473; Evidence={ECO:0000256|ARBA:ARBA00036461}; 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-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:77016; Evidence={ECO:0000256|ARBA:ARBA00036719}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232; Evidence={ECO:0000256|ARBA:ARBA00036719}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000256|ARBA:ARBA00036113}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000256|ARBA:ARBA00036113}; 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-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-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; Evidence={ECO:0000256|ARBA:ARBA00043731}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525; Evidence={ECO:0000256|ARBA:ARBA00043731}; 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}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; Evidence={ECO:0000256|ARBA:ARBA00036775}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605; Evidence={ECO:0000256|ARBA:ARBA00036775};

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};

Antimicrobial;Bacteriolytic enzyme;Calcium;Disulfide bond;Hydrolase;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal

arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]

extracellular region [GO:0005576]; mitochondrial outer membrane [GO:0005741]

calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]

SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004450}. Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361236}.

IPR001211;IPR033112;IPR016090;IPR036444;

1.20.90.10;

A0A3Q1M739

MLSHGLPAPRWFHRDLSGLDAETLLKGRGVHGSFLARPSRKNQGDFSLSVRVGDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGVLQDRDGTIIHLKYPLNCSDPTSERWYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPLRVTHIKVMCEGGRYTVGGSETFDSLTDLVEHFKRTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEETAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVVLQGRDSNIPGSDYINANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMVWQENTCVIVMTTREVEKGRNKCVPYWPEVGSQRVYGPYTVTNCGEHDTTEYKLRNLQVSPLENENLIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMESISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEVMQSQKGRESEYGNITYPPAMKNAHAKASRTSSKEDVYENVHSKNKKEEKVKKQRSADKEKNKGSLKRK

Bos taurus (Bovine)

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

B cell receptor signaling pathway [GO:0050853]; cell differentiation [GO:0030154]; cellular response to organic substance [GO:0071310]; dephosphorylation [GO:0016311]; epididymis development [GO:1905867]; hematopoietic progenitor cell differentiation [GO:0002244]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; megakaryocyte development [GO:0035855]; mitotic cell cycle [GO:0000278]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002924]; negative regulation of inflammatory response to wounding [GO:0106015]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of mast cell activation involved in immune response [GO:0033007]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of tumor necrosis factor production [GO:0032720]; platelet aggregation [GO:0070527]; platelet formation [GO:0030220]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of B cell differentiation [GO:0045577]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]

alpha-beta T cell receptor complex [GO:0042105]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]

cell adhesion molecule binding [GO:0050839]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; phosphorylation-dependent protein binding [GO:0140031]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]

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

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

3.90.190.10;3.30.505.10;

A0A3Q1M8B3

MESAWETRPRVAFEAPASKRVQEGSKSQRRRRWRKARAKASRLLQRMDLRTMTQSLVTLAEDNMAFFSSQGPGETARRLTGVFAGIREQALGLEPALGRLLSVAHLFDLDTETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALAYYAQRLLTTNQPGRLFFEGDERVIADFLREYVTLHKGCFYGRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGISVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIQVLSSLANMASTTVRVSRLLSLPPVAFEMPLTSDPELTVTISPPLAHTGPGPVLVRLISYDLREGQDSKELSSFVRSEGPRSLELRLRPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKSWAQELGAPILSIDYSLAPEAPFPRALEECFYAYCWAVKHCALLGSTGERICLAGDSAGGNLCFTVSLRAAAYGVRVPDGIMAAYPATMLQSTASPSRLLSLMDPLLPLSVLSKCVSAYAGAETEDHPASDQKALGVMGLVQRDTALLLRDLRLGASSWLNSFLELGGQKSHLKSVSKTEPMRRSVSEAALTRPEGPLGTDSLKSLKLHDLGLRNSSDTTDTPELSLSAETLGPSAPSTINFLLGSEDGSEMSEAPEELNNKDRVRGVGAAFPEGFHPRRCSQGAMWMPLYSAPIVKNPFMSPLLAPNSMLQTLPPVHIVACALDPMLDDSVMFARRLRGLGQPVTLRVVEDLPHGFLSLAALCRETRQAAALCVERIRLILNLPGPPV

Bos taurus (Bovine)

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;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]; 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;

A0A3Q1ME99

MGTSHWALLVLGCLFTGPSLILCQLSLPSILPNENERVVQLNSSFSLRCFGESEVSWQYPMSEEEYPDVEIRNEENNSGLFVTVLEVVSASAAHTGLYTCYYNHTQMDENEIEGRHIYIYVPDPDVAFVPLGMTDSLVIVEDEDSVIIPCRTTDPETPVTLLSSEGIVPASYDSRQGFKGTFSVGLYICEATVRGKKFQTIPFNVYAYTATSKLDLEMESPKTVYKAGESIVVTCTVFNNEVVDFQWTYPGQMKGKGITRLEETKFPSIKLVYTLRVPEATVKDSGDYECAAHQATKEVKKMRNVTISVHEKGFIEIKPNFNLLEAVNLHEVKHFVVDVQAYPPPKITWLKDNLTLIENLTEITTDIEKIQEISYRSKLKLIRAKEEDSGHYTIVVQNEDDVKSYTFELLTQVPSSILDLVDDHHGSNGGQTVRCTAEGTPLPDIEWMVCKDIKKCNNETSWTVLANNVSNIITGVHPRDRSTVEGQVTFAKVEETIAVRCLAKNLLGVESRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRALYDRPASYKKKSMLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHRIFLSLPHSVDYIKIFKQKHIASEKAMASYSSTLAWKIPWMEEPGRLQSMGLLRVRHD

Bos taurus (Bovine)

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;

A0A3Q1MFM9

MTVFFKTLRNHWKKTTAGICLLTWGGHWVYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGYFVVFMNCLVLETASSVLHDGWSRAVGRKTGRQGQGHLLCFMDTSVPLCSISFSDHNNKTSLSFSSRQATFSKIPIGFIPLGQTSSLSQTLFAESGNKVQRITDATLAIVKGETVPLDVLQIKGEKEQPVFALTGLRWGSFRDAGVSVSRYWYLGPLKTKAAHFFSTLKEWPQTHQASISYTGPTERPPSGAEETPPRPSLYRRILRRLASYWAQPQGALQEVNPEVWKEVQLSTLELSITTRNSQLDLASKEDFMNICMEPNTVSKGDFITIGSKKVRDPKLHVEGTECLQASRCTLLLPEGTGGAFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQLLQSPAQ

Bos taurus (Bovine)

2.7.1.107; 2.7.1.138; 2.7.1.94

CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43328, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:34071, ChEBI:CHEBI:74938, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43329; Evidence={ECO:0000256|ARBA:ARBA00024483}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41079, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024505}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41080; Evidence={ECO:0000256|ARBA:ARBA00024505}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43308, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57518, ChEBI:CHEBI:75542, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43309; Evidence={ECO:0000256|ARBA:ARBA00024636}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43316, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52392, ChEBI:CHEBI:78209, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024556}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43317; Evidence={ECO:0000256|ARBA:ARBA00024556}; CATALYTIC ACTIVITY: Reaction=ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate; Xref=Rhea:RHEA:43312, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63867, ChEBI:CHEBI:82959, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024616}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43313; Evidence={ECO:0000256|ARBA:ARBA00024616}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:33747, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024512}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33748; Evidence={ECO:0000256|ARBA:ARBA00024512}; CATALYTIC ACTIVITY: Reaction=a 2-acylglycerol + ATP = a 2-acyl-sn-glycerol 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:39847, ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:30616, ChEBI:CHEBI:64982, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00044480}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39848; Evidence={ECO:0000256|ARBA:ARBA00044480}; CATALYTIC ACTIVITY: Reaction=a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate; Xref=Rhea:RHEA:19293, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:30616, ChEBI:CHEBI:77589, ChEBI:CHEBI:456216; EC=2.7.1.94; Evidence={ECO:0000256|ARBA:ARBA00024567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19294; Evidence={ECO:0000256|ARBA:ARBA00024567}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674, ChEBI:CHEBI:456216; EC=2.7.1.138; Evidence={ECO:0000256|ARBA:ARBA00024607}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930; Evidence={ECO:0000256|ARBA:ARBA00024607};

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

PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000256|ARBA:ARBA00005175}.

Membrane;Mitochondrion;Mitochondrion inner membrane;Reference proteome

ceramide biosynthetic process [GO:0046513]; glycerolipid metabolic process [GO:0046486]; lipid phosphorylation [GO:0046834]; protein insertion into mitochondrial inner membrane [GO:0045039]; sphingosine biosynthetic process [GO:0046512]

mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; TIM22 mitochondrial import inner membrane insertion complex [GO:0042721]

acylglycerol kinase activity [GO:0047620]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; ceramide kinase activity [GO:0001729]; D-erythro-sphingosine kinase activity [GO:0017050]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.

IPR045579;IPR001206;IPR016064;

A0A3Q1MHB0

MRLSGAGRAALLVLLAAHFQTSLALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYMQSSYNLSFLKTIQEVAGYVLIALNTVEKIPLENLQIIRGNVLYENTHALAVLSNYGANKTGLRELPLRNLQEILQGAVRFSNNPVLCNVETIQWRDIVNPDFLSNMTGDFQNQQGNCPKCDPACLNRSCWGAGEENCQKLTKIICAQQCSGRCRGRSPSDCCHNQCAAGCTGPRESDCLVCRRFRDEATCKDTCPPLMLYDPTTYEMKVNPLGKYSFGATCVKKCPRNYVVTDHGSCVRACSSDSQEVEEDGVRKCKKCDGPCGKVCNGIGIGEFKDTLSINATNIKHFRNCTSISGDLHILPVAFRGDSFTRTAPLDPKELDILRTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVGLDITSLGLRSLKEISDGDVIISGNRNLCYADTIRWKKLFGTSTQKTKILNNRSEKQCKAAGHICHPLCSSEGCWGPGPKYCMSCQNFSRGKECVGKCNILEGEPREFVENSECVQCHPECLPQAMNVTCTGRGPGNCVKCAHYIDGPHCVKTCPAGVAGENGTLIWKFADANHVCLLCHPNCTYGCEGPGLEGCPQKGPKIPSIATGIVGGLLLVVVLALSVGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKVKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNVGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISTVLEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMEDVVDADEYLVPQQGFFHSPTTSRTPLLSSLSTSSNTPTVTCVDRNGQSYPLKEDSFLQRYSSDPTGALIEDSMDDTFLPVPEYVNQSVPKRPAGSVQNPVYHNQPLYPAPGRDPQYQNSLSNAVDNPEYLNTTHPACINGVLDGPALWAQKGSHQFSLDNPDYQQAFFPKEAKSNGIFKGPAAENAEYLRAAPAGSDFTGA

Bos taurus (Bovine)

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

cell-cell adhesion [GO:0098609]; cellular response to cadmium ion [GO:0071276]; cellular response to estradiol stimulus [GO:0071392]; cellular response to reactive oxygen species [GO:0034614]; ERBB2-EGFR signaling pathway [GO:0038134]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiocyte differentiation [GO:1905208]; negative regulation of protein catabolic process [GO:0042177]; neurogenesis [GO:0022008]; phosphorylation [GO:0016310]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of JNK cascade [GO:0046328]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; response to UV-A [GO:0070141]

basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell junction [GO:0030054]; cell surface [GO:0009986]; early endosome membrane [GO:0031901]; membrane raft [GO:0045121]; multivesicular body, internal vesicle lumen [GO:0097489]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]

actin filament binding [GO:0051015]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; epidermal growth factor binding [GO:0048408]; epidermal growth factor receptor activity [GO:0005006]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activator activity [GO:0030296]; ubiquitin protein ligase binding [GO:0031625]

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

IPR044912;IPR006211;IPR006212;IPR032778;IPR009030;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR049328;IPR008266;IPR020635;IPR016245;

6.10.250.2930;3.80.20.20;1.10.510.10;

A0A3Q1MHG9

MGDGANNLPFFFGNITREEAEDYLVQGGMSDGLYLLRQSRNYLGGFALSVAHDRKAHHYTIERELNGTYAITGGRAHGSPAELCHYHTQELDGLVCLLKKPFNRPPGVQPKTGPFEDLKENLIREYVKQTWNLQGQALEQAIISQKPQLEKLIATTAHEKMPWFHGKISRDESEQIVLIGSKTNGKFLIRAKDNGSYALCLLHEGKVLHYRIDKDKTGKLSIPGGKNFDTLWQLVEHYSYKSDGLLRVLTVPCQKIGGQSGNINFRPQLPSSHPGTWSAGGIISRIKSYSFPKRDHRKTRTSSGNQVDSSTTFNPYEPDRGPWANEREAQREALPMDTEVYESPYADPEEIRPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEECNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPYRGMKGSEVSAMLEKGERMGCPPGCPREMYELMTLCWTYDVENRPGFVAVELRLRNYYYDVVN

Bos taurus (Bovine)

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:PIRNR000604};

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

adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell receptor signaling pathway [GO:0050853]; beta selection [GO:0043366]; blood vessel morphogenesis [GO:0048514]; calcium-mediated signaling [GO:0019722]; cell differentiation [GO:0030154]; cellular response to lipid [GO:0071396]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to molecule of fungal origin [GO:0071226]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; defense response to bacterium [GO:0042742]; gamma-delta T cell differentiation [GO:0042492]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; interleukin-3-mediated signaling pathway [GO:0038156]; leukocyte cell-cell adhesion [GO:0007159]; leukotriene biosynthetic process [GO:0019370]; lymph vessel development [GO:0001945]; macrophage activation involved in immune response [GO:0002281]; mast cell degranulation [GO:0043303]; neutrophil activation involved in immune response [GO:0002283]; neutrophil chemotaxis [GO:0030593]; phosphorylation [GO:0016310]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of bone resorption [GO:0045780]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-3 production [GO:0032752]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of killing of cells of another organism [GO:0051712]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of mast cell degranulation [GO:0043306]; positive regulation of monocyte chemotactic protein-1 production [GO:0071639]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of receptor internalization [GO:0002092]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type I interferon production [GO:0032481]; protein import into nucleus [GO:0006606]; receptor internalization [GO:0031623]; regulation of arachidonic acid secretion [GO:0090237]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of neutrophil degranulation [GO:0043313]; regulation of phagocytosis [GO:0050764]; regulation of platelet aggregation [GO:0090330]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; serotonin secretion by platelet [GO:0002554]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

B cell receptor complex [GO:0019815]; cytosol [GO:0005829]; early phagosome [GO:0032009]; nucleus [GO:0005634]; T cell receptor complex [GO:0042101]

ATP binding [GO:0005524]; integrin binding [GO:0005178]; interleukin-15 receptor binding [GO:0016170]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatase binding [GO:0019902]; phospholipase binding [GO:0043274]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]; SH2 domain binding [GO:0042169]; signaling receptor binding [GO:0005102]; Toll-like receptor binding [GO:0035325]

IPR011009;IPR023420;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR035838;IPR008266;IPR020635;IPR012234;

3.30.505.10;1.10.510.10;

A0A3Q1MIK4

MTIPYASMPMAVLNLGQIDPFQRGFFCKDNSIQYPYHDGTITTTVLSTVGLGLPISSMIVGETLSVYFSLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIENYICRGNAQKVKEGRLSFYSGHSSFSMYCMMFVALYLQARMKGDWARLLRPTLQFGLVAASIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKKRSSPFKERKEEDSHTTLHETPTTGNHYRNSHQP

Bos taurus (Bovine)

3.1.3.106; 3.1.3.4; 3.6.1.75

CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000256|ARBA:ARBA00000974}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000256|ARBA:ARBA00000974}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000256|ARBA:ARBA00000980}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000256|ARBA:ARBA00000980}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000256|ARBA:ARBA00001611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000256|ARBA:ARBA00001611}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000256|ARBA:ARBA00000235}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000256|ARBA:ARBA00000235}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466; Evidence={ECO:0000256|ARBA:ARBA00023681}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256; Evidence={ECO:0000256|ARBA:ARBA00023681}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000256|ARBA:ARBA00001542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000256|ARBA:ARBA00001542}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000256|ARBA:ARBA00001710}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000256|ARBA:ARBA00001710}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000256|ARBA:ARBA00001476}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000256|ARBA:ARBA00001476}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000256|ARBA:ARBA00001716}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000256|ARBA:ARBA00001716}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000256|ARBA:ARBA00001180}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; Evidence={ECO:0000256|ARBA:ARBA00035886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450; Evidence={ECO:0000256|ARBA:ARBA00035886}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683; EC=3.1.3.106; Evidence={ECO:0000256|ARBA:ARBA00001472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156; Evidence={ECO:0000256|ARBA:ARBA00001472}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000256|ARBA:ARBA00023977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000256|ARBA:ARBA00023977};

PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000256|ARBA:ARBA00005074}.; PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.

Cell membrane;Hydrolase;Lipid metabolism;Membrane;Reference proteome

phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]

apical plasma membrane [GO:0016324]; caveola [GO:0005901]; plasma membrane [GO:0005886]

lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane raft {ECO:0000256|ARBA:ARBA00004314}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004314}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004189}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004189}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR036938;IPR000326;IPR043216;

1.20.144.10;

A0A3Q1MIR9

MAEVVSPVPGAGRREPGEVGRARGPPVADPGAALSPQGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTALPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW

Bos taurus (Bovine)

2.3.1.48

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000256|RuleBase:RU361211};

Acetylation;Acyltransferase;DNA damage;DNA repair;Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase;Zinc;Zinc-finger

apoptotic process [GO:0006915]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucose starvation [GO:0042149]; cellular response to glucose stimulus [GO:0071333]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair via homologous recombination [GO:0000724]; establishment of mitotic spindle orientation [GO:0000132]; lipid droplet disassembly [GO:1905691]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube development [GO:0021915]; neurogenesis [GO:0022008]; nucleotide-excision repair [GO:0006289]; positive regulation of aggrephagy [GO:1905337]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of mitotic sister chromatid segregation [GO:0062033]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of protein acetylation [GO:1901985]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of triglyceride biosynthetic process [GO:0010867]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of hematopoietic stem cell differentiation [GO:1902036]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ionizing radiation [GO:0010212]; sperm DNA condensation [GO:0035092]

cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic spindle pole [GO:0097431]; MSL complex [GO:0072487]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleolus [GO:0005730]; nucleosome [GO:0000786]; nucleus [GO:0005634]; piccolo histone acetyltransferase complex [GO:0032777]; site of double-strand break [GO:0035861]; Swr1 complex [GO:0000812]; transcription regulator complex [GO:0005667]

chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; histone H2AK5 acetyltransferase activity [GO:0043999]; histone H4K16 acetyltransferase activity [GO:0046972]; peptide butyryltransferase activity [GO:0140065]; peptide crotonyltransferase activity [GO:0140064]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.

IPR016181;IPR016197;IPR000953;IPR002717;IPR025995;IPR036388;IPR040706;

2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10;

A0A3Q1MLT2

MSEAGGPAPGAPPLPPAPPQGPPGAAAGGAGSCGPAAAGAAAGAAEGPGGGCSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHREEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPPKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETAQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVISPPPVAGTVSYNSSSASLEQQNGGSASPSCRGASGLEANPGEKRKMNESHVLEETKKPRVMGDIPLELIHEVMSTITDPTAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLSQKPNKKVLMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGRERSKEARDPDQLYSTLRSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCASILEKFFFSKIKEAGLIDK

Bos taurus (Bovine)

2.3.1.48

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000256|ARBA:ARBA00024456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000256|ARBA:ARBA00024456}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000256|PIRNR:PIRNR003048};

Acyltransferase;Bromodomain;Cytoplasm;Cytoskeleton;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase

cellular response to insulin stimulus [GO:0032869]; chromatin remodeling [GO:0006338]; gluconeogenesis [GO:0006094]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of centriole replication [GO:0046600]; negative regulation of rRNA processing [GO:2000233]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of glycolytic process [GO:0045821]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]

A band [GO:0031672]; actomyosin [GO:0042641]; ATAC complex [GO:0140672]; centrosome [GO:0005813]; cytosol [GO:0005829]; I band [GO:0031674]; kinetochore [GO:0000776]; nucleoplasm [GO:0005654]

chromatin binding [GO:0003682]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K9 acetyltransferase activity [GO:0043992]; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0004468]; protein kinase binding [GO:0019901]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription coactivator activity [GO:0003713]

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003048}.

IPR016181;IPR001487;IPR036427;IPR018359;IPR037800;IPR016376;IPR000182;IPR009464;

3.40.630.30;1.20.920.10;

A0A3Q1MRR6

MAPFLRISFNSYELGSLKAADEASQPFCAVKMKEALSTDRGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPMSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRGEDEAKFPTMNRRGAIKQAKIHYIRHHEFIATFFGQPTFCSVCREFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVYNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCQMKVANLCGINQKLLAEALNQVSQAAPPNPHPLLQRSVKKETETQDTVGIYQNFEKKPGVSGDDLTGKETGTYGKIWESSTKCNIDNFTFIKVLGKGSFGKVLLAELKGKKEFFAIKALKKDVVLIDDDVECTMVEKRVLALAGDHPFLTHLFCTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELSRATFYAAEIVCGLQFLHQKGIIYRDLKLDNVLLDHSGHIKIADFGMCKENMSGDRQASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRLDSPYYPRWITKESKDILEKLLERDVSKRLGVTGNIKIHPFFKTINWVLLEKRAVEPPFKPKVKSPGDFSNFDQEFLNEKPRLSYSDKNLIESMDQTAFAGFSFVNPKFERLLEN

Bos taurus (Bovine)

FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression. {ECO:0000256|PIRNR:PIRNR000551}.

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};

Apoptosis;ATP-binding;Cell cycle;Cytoplasm;Kinase;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger

apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; cell chemotaxis [GO:0060326]; cell cycle [GO:0007049]; 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]; perinuclear region of cytoplasm [GO:0048471]; 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|PIRNR:PIRNR000551}. Cytoplasm, perinuclear region {ECO:0000256|PIRNR:PIRNR000551}. Nucleus {ECO:0000256|PIRNR:PIRNR000551}. 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;

A0A3Q1MVZ1

MAESSDKLYRVEYAKSGRASCKKCKESIPKDSIRMAFMVQSPMFDGKIPHWYHLSCFWKVGFSIWHPDVEVEGFSELRWDDQQTIKKMAETGGATDVSGKGQDGVGSKTEKTLIDFGAGYAKSNRSTCKSCMEKIDKGQVRLSKKVVYPDKPQLGMVDCWYHPKCFVQKREELGFRPEFSASQLMGFSVLTAEDQETLKKQLPAIKGERKRKGDEVDGIDEVTKKKSKKEKDKEIKLEKALKAQNDLIWNVKDELKKACSTNDLKELLIFNKQEVPSGESAILDRVADGMVFGALLPCEECSGQLVFKGDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYFKKLKIKKQDRIFPPESSTPVGAAAPPSAASAPAAVHSGPPDKPLSNMKILTLGKLSQNKDEVKATIEKLGGKLTGTANKASLCISTKKEVDKMNKKMEEVKEANIRVVSEDFLQDISASTKSLQELLSTHLLSPWGAEVKVEPVEAVAPKGKSGAAPSKKSKGPVKEEGTNKSEKRMKLTLKGGAAVDPDSGLEHNAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKHPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQNLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQALSQGSSDSHILDLSNRFYTLIPHDFGMKKPPLLNNANSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDKDSEEAEIIRKYVKNTHATTHNAYDLEVVDIFKIEREGESQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEDTVLGFVCLLNVYTDLISLDRFRHVSTNRIPSAFCPAGLGKTTPDPSASITVDGVEVPLGTGISSGVNDTCLLYNEYIVYDIAQVHLKYLLKLKFNFKTSLW

Bos taurus (Bovine)

FUNCTION: This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis. {ECO:0000256|ARBA:ARBA00034299}.

2.4.2.-

CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000256|ARBA:ARBA00024164}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; Evidence={ECO:0000256|ARBA:ARBA00024164}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence={ECO:0000256|ARBA:ARBA00024159}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; Evidence={ECO:0000256|ARBA:ARBA00024159}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + NAD(+) = H(+) + N(tele)-(ADP-D-ribosyl)-L-histidyl-[protein] + nicotinamide; Xref=Rhea:RHEA:72071, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:18085, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29979, ChEBI:CHEBI:57540, ChEBI:CHEBI:191398; Evidence={ECO:0000256|ARBA:ARBA00034220}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72072; Evidence={ECO:0000256|ARBA:ARBA00034220}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540, ChEBI:CHEBI:142556; Evidence={ECO:0000256|ARBA:ARBA00024165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233; Evidence={ECO:0000256|ARBA:ARBA00024165}; CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540, ChEBI:CHEBI:142557; Evidence={ECO:0000256|ARBA:ARBA00024171}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237; Evidence={ECO:0000256|ARBA:ARBA00024171}; CATALYTIC ACTIVITY: Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30; Evidence={ECO:0000256|ARBA:ARBA00033987};

ADP-ribosylation;Allosteric enzyme;Chromosome;DNA damage;DNA repair;DNA-binding;Glycosyltransferase;Metal-binding;NAD;Nucleotidyltransferase;Nucleus;Reference proteome;Repeat;Transferase;Zinc;Zinc-finger

apoptotic process [GO:0006915]; ATP generation from poly-ADP-D-ribose [GO:1990966]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxidative stress [GO:0034599]; cellular response to UV [GO:0034644]; DNA ADP-ribosylation [GO:0030592]; double-strand break repair [GO:0006302]; innate immune response [GO:0045087]; mitochondrial DNA repair [GO:0043504]; negative regulation of ATP biosynthetic process [GO:2001170]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of innate immune response [GO:0045824]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of single strand break repair [GO:1903518]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein auto-ADP-ribosylation [GO:0070213]; protein localization to chromatin [GO:0071168]; regulation of base-excision repair [GO:1905051]; regulation of protein localization [GO:0032880]; replication fork reversal [GO:0071932]

chromatin [GO:0000785]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nuclear envelope [GO:0005635]; nuclear replication fork [GO:0043596]; nucleolus [GO:0005730]; site of double-strand break [GO:0035861]; transcription regulator complex [GO:0005667]

damaged DNA binding [GO:0003684]; NAD binding [GO:0051287]; NAD DNA ADP-ribosyltransferase activity [GO:0140294]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+- protein-aspartate ADP-ribosyltransferase activity [GO:0140806]; NAD+-histone H2BS6 serine ADP-ribosyltransferase activity [GO:0140816]; NAD+-histone H3S10 serine ADP-ribosyltransferase activity [GO:0140817]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; NAD+-protein-glutamate ADP-ribosyltransferase activity [GO:0140807]; NAD+-protein-histidine ADP-ribosyltransferase activity [GO:0140815]; NAD+-protein-tyrosine ADP-ribosyltransferase activity [GO:0140808]; nucleosome binding [GO:0031491]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; zinc ion binding [GO:0008270]

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

IPR001357;IPR036420;IPR038650;IPR008288;IPR049296;IPR012982;IPR012317;IPR004102;IPR036616;IPR036930;IPR008893;IPR001510;IPR036957;

1.10.20.130;2.20.25.630;3.90.228.10;3.40.50.10190;1.20.142.10;3.30.1740.10;

A0A3Q1MW77

MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCKENDSIQSRKNEESQEIQKKLYTLEEHLSTEIQAKEELEQKCKSVNTRLEKVAKELEEEITLRKNVESTLRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSVLESERRDRTHGSEIINDLQGRISGLEEDVKNGKILLAKVELEKRQLQERFTDLEKEKNNMEIDMTYQLKVIQQSLEQEETEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLSEERTLKQKVENLLLEAEKRCSILDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLLEMKMSLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLCKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKEAQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDTEADDGFPVHITQSHTMESMSFTYQRSSTSLNIATKPSSSHMLLDSDSDSEEESVPYLPISSEPNESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS

Bos taurus (Bovine)

2.7.11.1

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

ATP-binding;Biological rhythms;Cell membrane;Coiled coil;Cytoplasm;Cytoskeleton;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger

actomyosin structure organization [GO:0031032]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to testosterone stimulus [GO:0071394]; centrosome duplication [GO:0051298]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; mitotic cytokinesis [GO:0000281]; modulation by host of viral process [GO:0044788]; negative regulation of angiogenesis [GO:0016525]; negative regulation of bicellular tight junction assembly [GO:1903347]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of protein localization to lysosome [GO:0150033]; phosphorylation [GO:0016310]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of centrosome duplication [GO:0010825]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of gene expression [GO:0010628]; positive regulation of protein localization to early endosome [GO:1902966]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stress fiber assembly [GO:0051496]; protein localization to plasma membrane [GO:0072659]; regulation of cell junction assembly [GO:1901888]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of keratinocyte differentiation [GO:0045616]; Rho protein signal transduction [GO:0007266]; rhythmic process [GO:0048511]; smooth muscle contraction [GO:0006939]

centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; metal ion binding [GO:0046872]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; small GTPase binding [GO:0031267]

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

IPR000961;IPR046349;IPR011072;IPR011009;IPR002219;IPR011993;IPR001849;IPR000719;IPR017441;IPR037311;IPR015008;IPR008271;

1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10;

A0A3Q1MZ56

MVLVLHHILIAVVQFFRRGQQVFLKPDEPPPPPQPCADSLQPAGTSLHRSQCPQGVETAHCSPCAGNWGTAEMDQTLKTEPNTVMGPSSEAVGETHAREEQTERERQTWRIQEGREGNRVQDALLSLGSVIDVAGLQQAVKEALSAVLPKVETVYTYLLDGESRLVCEEPPHELPQEGKVREAVISRKRLGCNGLGPSDLPGKPLARLVAPLAPDTQVLVIPLVDKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALKRVQALQQRESSVAPEATQNPPEEAAGDQKGGVAYTDQDRKILQLCGELYDLDASSLQLKVLQYLQQETQASRCCLLLVSEDNLQLSCKVIGDKVLEEEISFPLTTGRLGQVVEDKKSIQLKDLTSEDMQQLQSMLGCEVQAMLCVPVISRATDQVVALACAFNKLGGDLFTDQDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVEDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNFASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMHAFSVSHFCYLLYKNLELTNYLEDMEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDRTNKQHHSLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSHKFTIRGLPSNNSLDFLDEEYEVPDLDGARAPINGCCSLDAE

Bos taurus (Bovine)

3.1.4.-

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000256|RuleBase:RU363067}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};

cGMP;Hydrolase;Metal-binding;Reference proteome;Signal

adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cAMP-mediated signaling [GO:0019933]; cellular response to 2,3,7,8-tetrachlorodibenzodioxine [GO:1904613]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cGMP catabolic process [GO:0046069]; cGMP-mediated signaling [GO:0019934]; negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106072]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of cGMP-mediated signaling [GO:0010754]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular permeability [GO:0043116]; positive regulation of gene expression [GO:0010628]; positive regulation of vascular permeability [GO:0043117]; regulation of mitochondrion organization [GO:0010821]

cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; synaptic membrane [GO:0097060]

3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; cGMP-stimulated cyclic-nucleotide phosphodiesterase activity [GO:0004118]; magnesium ion binding [GO:0000287]; phosphate ion binding [GO:0042301]; protein homodimerization activity [GO:0042803]; TPR domain binding [GO:0030911]; zinc ion binding [GO:0008270]

IPR003018;IPR029016;IPR003607;IPR023088;IPR002073;IPR036971;IPR023174;

3.30.450.40;1.10.1300.10;

A0A3Q1N8K2

MSPCGRARRHTSRGAMAVLAWKFPRTRLPVGASALCVVVLCWLYVFPVYRLPDEKEIVQGVLQQGTAWRRNRTAAGIFRKQMEDCCDPAHLFAMTKMNSPMGKSLWYDGEFLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEADFVMRCNLPPLSSEYTKDVGSKSHLVTANPSIIRQRFQNLLWSRKTFVDHMKVYNHSYIYMPAFSMKTGTEPSLRVYYTLSDVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSVNMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDNSLQPTS

Bos taurus (Bovine)

2.4.3.8

CATALYTIC ACTIVITY: Reaction=[alpha-N-acetylneuraminyl-(2->8)](n)-alpha-N-acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + CMP-N-acetyl-beta-neuraminate = [alpha-N-acetylneuraminyl-(2->8)](n+1)-alpha-N-acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + CMP + H(+); Xref=Rhea:RHEA:77371, Rhea:RHEA-COMP:18881, Rhea:RHEA-COMP:18935, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:197322; Evidence={ECO:0000256|ARBA:ARBA00044457}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77372; Evidence={ECO:0000256|ARBA:ARBA00044457}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1a (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GT1a (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41768, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78445, ChEBI:CHEBI:78447; Evidence={ECO:0000256|ARBA:ARBA00043743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769; Evidence={ECO:0000256|ARBA:ARBA00043743}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GT3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41764, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78436, ChEBI:CHEBI:78438; Evidence={ECO:0000256|ARBA:ARBA00043833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765; Evidence={ECO:0000256|ARBA:ARBA00043833}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD3 + CMP-N-acetyl-beta-neuraminate = a ganglioside GT3 + CMP + H(+); Xref=Rhea:RHEA:77295, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:79214, ChEBI:CHEBI:79216; Evidence={ECO:0000256|ARBA:ARBA00044471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77296; Evidence={ECO:0000256|ARBA:ARBA00044471}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD1c (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:47576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78568, ChEBI:CHEBI:87787; Evidence={ECO:0000256|ARBA:ARBA00043723}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577; Evidence={ECO:0000256|ARBA:ARBA00043723}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41760, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377, ChEBI:CHEBI:78436; Evidence={ECO:0000256|ARBA:ARBA00043813}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761; Evidence={ECO:0000256|ARBA:ARBA00043813}; CATALYTIC ACTIVITY: Reaction=a ganglioside GT1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GQ1b (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41772, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78452, ChEBI:CHEBI:78455; Evidence={ECO:0000256|ARBA:ARBA00043792}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773; Evidence={ECO:0000256|ARBA:ARBA00043792}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+); Xref=Rhea:RHEA:19313, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140308, ChEBI:CHEBI:140309; EC=2.4.3.8; Evidence={ECO:0000256|ARBA:ARBA00036589};

PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004760}.; PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922}.; PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.

Disulfide bond;Glycoprotein;Golgi apparatus;Lipid metabolism;Membrane;Reference proteome;Signal-anchor;Sphingolipid metabolism;Transferase;Transmembrane;Transmembrane helix

cellular response to heat [GO:0034605]; epithelial cell proliferation [GO:0050673]; N-glycan processing [GO:0006491]; oligosaccharide metabolic process [GO:0009311]; positive regulation of epithelial cell proliferation [GO:0050679]; protein glycosylation [GO:0006486]; sphingolipid metabolic process [GO:0006665]

Golgi membrane [GO:0000139]

alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity [GO:0003828]

SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.

IPR001675;IPR038578;IPR012163;

3.90.1480.20;

A0A3Q1N8M5

MASELGAGDDGGCTELAKPLYLQYLERALRLDHFLRQTSAIFNRNISSDESEDGLDDSNPLLPQSGDPLIQVKEEPPNSLLGETSGASTSEMLNTYSLNGVLQSESKFDKGNLYNFSKLKKSRKWLKSILLSDESSEADSHSEDNDEGEEEDDDEEEELSLSREDLHNMLRLHKYKKLHQNKYSKEKELQQYQYYSAGLLSTYDPFYEQQRHLLGPKKKKFKEEKKLKAKLKKVKKKRRRDEELSSEESPRRHHHQTKVFAKFSHDAPPPGTKKKHLSIEQLNARRRKVWLSIVKKELPKANKQKASARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMREAKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSAQRQIDIGGGVVVNITQEDYDSNHFKAQALKNAENAYHIHQARTRSFDEDAKESRAAALRAANKSGTGFGESYSLANPSIRAGEDIPQPTIFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRRIKKDVENELSDKIEILMYCQLTSRQKLLYQALKNKISIEDLLQSSMGSTQQAQTTTSSLMNLVMQFRKVCNHPELFERQETWSPFHISLKPYQISKFIYRHGQIRVFNHSRDRWLRVLLSPFAPDYIQQSLFHRKGVNEESCFSFLRFIDVSPAEMANLMLQGLLARWLALFLSLKASYRLHQLRSWGEPEGESQEKYLRNKDFLLGVNFPLSFPNLSSCPLLKSLVFSSHCKAVSGYSDQVIHQRRSATSSLRCCLLTELPSFLCVASPRLLTFHLKNMGPKFLYNSNVTAVPLDSYCNDRSAEYERRVLKEGGSLAAKQCLLNGAPELAADWLNRRSQFFPEPAGGLWSIRPQNGWSFIRIPGKESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRNDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRMVISGGNFKPDTLKPKEVVSLLLDDEELEKKLRLRQEEKRQQEETNRVKERKRKREKYAEKKKKEDELDGKRRKEGMNLVIPFVPSADNSNLSADGDDSFISVDSAMPSPFSEISISSELHTGSIPPDESSSDMLVIVDDPASSAPQSRATNSPASMTGSVSDTVNGISIQEMPAAGRGHSARSRGRPKGSGSTAKGAGKGRSRKSTAGSAAAMAGAKAGAAAASAAAYAAYGYNVSKGISASSPLQTSLVRPAGLADFGPSSASSPLSSPLGKGNNLPGTPKSLHLTSSLAPDSLVRKQGKGAKPSGGR

Bos taurus (Bovine)

FUNCTION: ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair. {ECO:0000256|RuleBase:RU368001}.

3.6.4.-

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|RuleBase:RU368001};

ATP-binding;Coiled coil;DNA damage;DNA repair;DNA-binding;Hydrolase;Nucleotide-binding;Phosphoprotein;Reference proteome

cellular response to ionizing radiation [GO:0071479]; DNA repair [GO:0006281]; DNA-templated transcription [GO:0006351]; double-strand break repair via homologous recombination [GO:0000724]; mitotic sister chromatid segregation [GO:0000070]; positive regulation of cell growth [GO:0030307]; positive regulation of DNA repair [GO:0045739]; positive regulation of nuclear cell cycle DNA replication [GO:0010571]; positive regulation of telomere maintenance in response to DNA damage [GO:1904507]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA strand elongation [GO:0060382]; regulation of embryonic development [GO:0045995]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; spindle assembly [GO:0051225]; telomere maintenance [GO:0000723]; UV-damage excision repair [GO:0070914]

cytosol [GO:0005829]; Ino80 complex [GO:0031011]; nuclear body [GO:0016604]

alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; histone binding [GO:0042393]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368001}.

DOMAIN: The DBINO region is involved in binding to DNA. {ECO:0000256|RuleBase:RU368001}.

IPR020838;IPR031047;IPR014001;IPR001650;IPR027417;IPR038718;IPR049730;IPR000330;

3.40.50.300;3.40.50.10810;

A0A3Q1N9F5

MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLSPVAAPAGGISFHLQIGLSREPVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKTASDIQEGDLIEVVLSASATFEDFQIRPHTLFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGLSTVRTASAELSTSALDEPLLSPVSPGFEQKSPSESFIGREKRSNSQSYIGRPIQLDKILLSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDMEEAMVQDAEMVMAECQNDSGEMQDPDPDHEDSNRTISPSTSNNIPLMRVVQSVKHTKRKSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPAKPSALIPSGANPHCFEITTANIVYYVGENVVNPSSPPPNSSVLTSGVGADVARMWEMAIQHALMPVIPKGSSVGSGTSVHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELECKIGERYITHESDDSRWEQFAGEQGLQYPTHLIDPSAGHSDSPEAEETEMKALSERVSIL

Bos taurus (Bovine)

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;

A0A3Q1N9G5

MSGHRSTRKRCGDSHPESPLGFGHMSTPGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVPSWIAPNLITIIGLSINICTTVLLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGILDVTESQIIIIICQLLTGTLGPWFWNFTIPVLNIQMKLFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH

Bos taurus (Bovine)

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;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;

A0A3Q1ND98

MGDMANNSVAYGGVKNSLKEANHDGDFGITLAELRALMELRSTDALRKIQESYGDVYGICTRLKTSPNEGLSGNPVDIERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIVSLGLSFYQPPEGDNALCGDVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGAGGEEEEKKDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYINEKHYKKIPDPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRHVGNKTECALLGFLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSYRIFSKGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEPEPEWDNENDIVTGLTCIAVVGIEDPVRPEVPDAIKKCQRAGITVRMVTGDNINTARAIATKCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTVSEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGRNAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQIIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEEIPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQMDVVNAFQSGSSIQGALRRQPSIASQHHDIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNSSPPPSPNKNNNAVDSGIYLTIEMNKSATSSSPGSPLHSLETSL

Bos taurus (Bovine)

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 across plasma membrane [GO:1990034]; negative regulation of cytokine production [GO:0001818]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; positive regulation of bone mineralization [GO:0030501]; positive regulation of calcium ion transport [GO:0051928]; regulation of blood pressure [GO:0008217]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of vascular associated smooth muscle contraction [GO:0003056]

basolateral plasma membrane [GO:0016323]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; intracellular membrane-bounded organelle [GO:0043231]; lateral plasma membrane [GO:0016328]; nucleoplasm [GO:0005654]; photoreceptor ribbon synapse [GO:0098684]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type calcium transporter activity [GO:0005388]; PDZ domain binding [GO:0030165]

SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane {ECO:0000256|ARBA:ARBA00004124}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}. Presynaptic cell membrane {ECO:0000256|ARBA:ARBA00034107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034107}. Synaptic cell membrane {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034099}.

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;

A0A3Q1NG39

MSSSTRVALVTGANKGLGFAIVRDLCRRFPGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDITDLQSIHALRDFLRKEYGGLDVLVNNAAIAFQLSDPTPTPIKAEMTMKTNFFGTRDICTELLPLMKPQGRVVNMSSGWGFKALESCSPELQQKLRSETITEEELVGLMNKFVEDTKNGVHRKEGWPDNNIYGVAKIGITALSRIQARKLSEQRGGDKILLNACCPGWVRTDMGGSKAFKSLEEGIETPMYLALLPSDAEGPHGQFVHEKKVLTHSSPMGPFISLSQIHQTDTYTVTNLPTQTKERKKNQSIPFKFSLGNGC

Bos taurus (Bovine)

1.1.1.184; 1.1.1.189; 1.1.1.196; 1.1.1.197; 1.1.1.71

CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + S-nitrosoglutathione = NADP(+) + sulfinamide glutathione; Xref=Rhea:RHEA:63500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145544, ChEBI:CHEBI:145547; Evidence={ECO:0000256|ARBA:ARBA00036526}; CATALYTIC ACTIVITY: Reaction=H(+) + menadione + NADPH = menadiol + NADP(+); Xref=Rhea:RHEA:63492, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378, ChEBI:CHEBI:28869, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00036452}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin D2 = 15-oxoprostaglandin D2 + H(+) + NADPH; Xref=Rhea:RHEA:20744, ChEBI:CHEBI:15378, ChEBI:CHEBI:57406, ChEBI:CHEBI:57408, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.196; Evidence={ECO:0000256|ARBA:ARBA00035796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20745; Evidence={ECO:0000256|ARBA:ARBA00035796}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:11636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.197; Evidence={ECO:0000256|ARBA:ARBA00036088}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11637; Evidence={ECO:0000256|ARBA:ARBA00036088}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:63476, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:606564; Evidence={ECO:0000256|ARBA:ARBA00035975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63477; Evidence={ECO:0000256|ARBA:ARBA00035975}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin F2alpha = 15-oxoprostaglandin F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:63480, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00036086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63481; Evidence={ECO:0000256|ARBA:ARBA00036086}; CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin E2; Xref=Rhea:RHEA:24508, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:606564; EC=1.1.1.189; Evidence={ECO:0000256|ARBA:ARBA00036291}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24510; Evidence={ECO:0000256|ARBA:ARBA00036291}; 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=1.1.1.71; Evidence={ECO:0000256|ARBA:ARBA00036223}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000256|ARBA:ARBA00024539}; CATALYTIC ACTIVITY: Reaction=corticosterone + H(+) + NADPH = 20beta-dihydrocorticosterone + NADP(+); Xref=Rhea:RHEA:70219, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:189050; Evidence={ECO:0000256|ARBA:ARBA00036700}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70220; Evidence={ECO:0000256|ARBA:ARBA00036700}; CATALYTIC ACTIVITY: Reaction=cortisol + H(+) + NADPH = 20beta-dihydrocortisol + NADP(+); Xref=Rhea:RHEA:70215, ChEBI:CHEBI:15378, ChEBI:CHEBI:17650, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:139311; Evidence={ECO:0000256|ARBA:ARBA00036300}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70216; Evidence={ECO:0000256|ARBA:ARBA00036300}; CATALYTIC ACTIVITY: Reaction=daunorubicin + H(+) + NADPH = 13-dihydrodaunorubicin + NADP(+); Xref=Rhea:RHEA:63504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64677, ChEBI:CHEBI:75296; Evidence={ECO:0000256|ARBA:ARBA00036732}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63505; Evidence={ECO:0000256|ARBA:ARBA00036732};

Cytoplasm;NADP;Oxidoreductase;Phosphoprotein;Reference proteome

cytoplasm [GO:0005737]

carbonyl reductase (NADPH) activity [GO:0004090]

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

IPR045313;IPR036291;IPR020904;IPR002347;

3.40.50.720;

A0A3Q1NH91

MNSKKGLLIRESEISGFVGPAQLFLSPVLFPFGIVLDAGSSHTSLYIYRWPAEKENDTGVVTQIEECKLKGPGISGFAKKVNEINVYLTACMERAQKVIPSIQHMETPVYLGATAGMRLLRMENKQMADKILAAVASSISKYPFDFQGARIISGQEEGAYGWITVNYLLGKFTQKLSWFNLKPSKDDTQETYGALDLGGASTQITFVPQNETTESPNNNLYFRLYGKNYSVYTHSFLCYGKDQALLQKLALGLQGTNGIIHEPCFHSRYMRKIKMSVLNEGFCTKRHELNSSFYPLVDIEIRGAGNFQRCRQSIIQLFNTSYCPYSSCSFNGVFLPPLHGQFGAFSAFYYVMEFLNLTSEESVSVEQLTEKLEEFCAQRWEEVQKNFGEVKEKYLSEYCFSGTYILVLLLNGYHFTAESWKNIHFMNKVRSTSVGWTLGYMLNLTNKIPAEEPMSPPLPHSTYVFLMVLFSLILLAVIIVGIVVFHKPSYFWKDMV

Bos taurus (Bovine)

3.6.1.5

CATALYTIC ACTIVITY: Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate; Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; Evidence={ECO:0000256|ARBA:ARBA00043682}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736; Evidence={ECO:0000256|ARBA:ARBA00043682}; CATALYTIC ACTIVITY: Reaction=2 H2O + UTP = 2 H(+) + 2 phosphate + UMP; Xref=Rhea:RHEA:64896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; Evidence={ECO:0000256|ARBA:ARBA00043678}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897; Evidence={ECO:0000256|ARBA:ARBA00043678}; 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=ATP + 2 H2O = AMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:20988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00043702}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989; Evidence={ECO:0000256|ARBA:ARBA00043702}; 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=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00043676}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000256|ARBA:ARBA00043676}; CATALYTIC ACTIVITY: Reaction=CTP + 2 H2O = CMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:64908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00043680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909; Evidence={ECO:0000256|ARBA:ARBA00043680}; CATALYTIC ACTIVITY: Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069; Evidence={ECO:0000256|ARBA:ARBA00043776}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388; Evidence={ECO:0000256|ARBA:ARBA00043776}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; Evidence={ECO:0000256|ARBA:ARBA00043654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000256|ARBA:ARBA00043654}; CATALYTIC ACTIVITY: Reaction=GTP + 2 H2O = GMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:64904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00043766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905; Evidence={ECO:0000256|ARBA:ARBA00043766}; 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; Evidence={ECO:0000256|ARBA:ARBA00001702}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000256|ARBA:ARBA00001702}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; Evidence={ECO:0000256|ARBA:ARBA00043688}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000256|ARBA:ARBA00043688}; CATALYTIC ACTIVITY: Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58280, ChEBI:CHEBI:61402; Evidence={ECO:0000256|ARBA:ARBA00043752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331; Evidence={ECO:0000256|ARBA:ARBA00043752}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; Evidence={ECO:0000256|ARBA:ARBA00043716}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000256|ARBA:ARBA00043716}; CATALYTIC ACTIVITY: Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223; Evidence={ECO:0000256|ARBA:ARBA00043661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901; Evidence={ECO:0000256|ARBA:ARBA00043661}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; Evidence={ECO:0000256|ARBA:ARBA00043714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000256|ARBA:ARBA00043714}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000256|ARBA:ARBA00043753}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796; Evidence={ECO:0000256|ARBA:ARBA00043753}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; Evidence={ECO:0000256|ARBA:ARBA00043686}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681; Evidence={ECO:0000256|ARBA:ARBA00043686};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00001913}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix

nucleoside diphosphate catabolic process [GO:0009134]

plasma membrane [GO:0005886]

ATP binding [GO:0005524]; GDP phosphatase activity [GO:0004382]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]

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

IPR000407;

3.30.420.40;3.30.420.150;

A0A3Q2GST7

MRKEELHLKFFMCVIQSRQLVRTPQRTAGEASTSSMLIQKPPPETDASKILDTMDAPDTMEGIHVLKNEWIMTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKLGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATKSNYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIIEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEDHLCRRLSETRTRGSRLNIIIVAEGAIDRNGKPITSESIKDLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEATPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMAERKFDEAMKLRGRSFMNNWEVYKLLAHIRPPVSKSGSHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPRKSFEQISANITKFNIQGLIIVGGFEAYTGGLELMEGRKQYDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICMTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYSTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELKEQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSEHAHLEHISRKRSGEAPA

Equus caballus (Horse)

FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000256|HAMAP-Rule:MF_03184}.

2.7.1.11

CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-Rule:MF_03184};

PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}.

Acetylation;Allosteric enzyme;ATP-binding;Cytoplasm;Glycolysis;Hydroxylation;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase

canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glucose homeostasis [GO:0042593]; glycogen catabolic process [GO:0005980]; glycolysis from storage polysaccharide through glucose-1-phosphate [GO:0093001]; muscle cell cellular homeostasis [GO:0046716]; positive regulation of insulin secretion [GO:0032024]; positive regulation of transcription by RNA polymerase II [GO:0045944]

6-phosphofructokinase complex [GO:0005945]; apical plasma membrane [GO:0016324]; membrane [GO:0016020]; nucleus [GO:0005634]; sperm principal piece [GO:0097228]

6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}.

IPR009161;IPR022953;IPR041914;IPR015912;IPR000023;IPR035966;

3.40.50.450;3.40.50.460;

A0A3Q2GTP0

MGIKGLPLLFQAAPKCSFSAVRFQELAEGTEGTMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSGADGGTSVQAEASLPRNLLFKHSANSKEVIGVVSKEYIPKGTRFGPLIGEIYNNDTVPKNANRKYFWRIYSRGELHHFIDGFKEEKSNWMRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTMMNLTQTQSHPKQQSTEKNELCPKSVPKREYSVKEILKLDSNPSKGKDFYRSNISPFTSEKDTDDFRKNGSPEVPFYPRVVYPIRAPLPEDFLKASLAYGMERPTYITHSPIPSSTTPSPSARSSPDQSLKSSSPHSSPGTTVSPLAPGFQEPRDSYSYLNAPYGTEGLGSYPGYAPPPHLSSAFIPSYNAPYPKFLLPPYGMNCNGLSTVGNINSINNFGLFPRLYPVYSNFLGGGSLPHPMLNPASLPSSLPSEGARRLLQPEHPREVLVPAPHSAFSLTGAAASMKDKACSPTSGSPTAGTAATSEHVVQPKATSVAMAAPSSDEAMNLIKNKRNMTGYKTLPYPLKKQNGKIKYECNVCAKTFGQLSNLKVHLRVHSGERPFKCQTCNKGFTQLAHLQKHYLVHTGEKPHECQVCHKRFSSTSNLKTHLRLHSGEKPYQCKVCPAKFTQFVHLKLHKRLHTRERPHKCAHCHKSYIHLCSLKVHLKGNCPVAPAAGLPLEDLTRINEEIEKFDLSDNADRLEDMEDNIDVTSVVEKEILAVVRKEKEETGLKVSLQRNMGNGLLSGCGLYESSDPSLMKLPHSNPLPLGPVKVKQETVEPMDP

Equus caballus (Horse)

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;

A0A3Q2GTT8

MSSSNDQVSIPMSQRNTNGLPKKTPKGVKAFTEGAVLSFHNICYRVKEKSGFLLCRKTVEKEILSNINGIMRPGLNAILGPTGGGKSSLLDVLAARKDPHGLSGDVLINGATRPANFKCSSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMRNHEKNERINRIIQELGLEKVADSKIGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLMFHGPAQEALGYFASAGSLGEMNLRVRLRAKLSSDDHAARSGGYHCEPYNNPADFFLDVINGDSSAVLLNREDPEGEARETEEPSQRDLSLLEKLAEFYGNSTFFRETKAELDQLSGAQKSKKSIAFKEITYVSSFFHQLKWISKRSFKNLLGNPQASIAQIIITAILGLVIGAIFYDLKMDSAGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCITYFLLGLKPKVEAFFIMMFTLMMVAYSASSMALAIAAGQSVVSIATLLMTICFVFMMIFSGLLVNLRTVVAWLSWLQYFSIPRYGYAALQHNEFLGQNFCPGLNVTANDTCSYATCTGEEFLENQGIDLSPWGLWRNHVALACMIVIFLTIAYLKLLFLKKYS

Equus caballus (Horse)

7.6.2.2

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=4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144582, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61373; Evidence={ECO:0000256|ARBA:ARBA00001510}; CATALYTIC ACTIVITY: Reaction=4-methylumbelliferone sulfate(in) + ATP + H2O = 4-methylumbelliferone sulfate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144581, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001548}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61369; Evidence={ECO:0000256|ARBA:ARBA00001548}; CATALYTIC ACTIVITY: Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144584, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001235}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61385; Evidence={ECO:0000256|ARBA:ARBA00001235}; CATALYTIC ACTIVITY: Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144583, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61377; Evidence={ECO:0000256|ARBA:ARBA00001144}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl sulfate(out) + phosphate; Xref=Rhea:RHEA:61332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144643, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00000732}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333; Evidence={ECO:0000256|ARBA:ARBA00000732}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) + phosphate; Xref=Rhea:RHEA:61356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:50681, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001597}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61357; Evidence={ECO:0000256|ARBA:ARBA00001597}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00001865}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; Evidence={ECO:0000256|ARBA:ARBA00001865}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57986, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00000226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353; Evidence={ECO:0000256|ARBA:ARBA00000226}; 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 + urate(in) = ADP + H(+) + phosphate + urate(out); Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024265}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462; Evidence={ECO:0000256|ARBA:ARBA00024265}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00034018}; CATALYTIC ACTIVITY: Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034009}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; Evidence={ECO:0000256|ARBA:ARBA00034009}; CATALYTIC ACTIVITY: Reaction=ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61348, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00000044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349; Evidence={ECO:0000256|ARBA:ARBA00000044};

ATP-binding;Disulfide bond;Membrane;Mitochondrion;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix;Transport

transmembrane transport [GO:0055085]

mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]

ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; efflux transmembrane transporter activity [GO:0015562]; riboflavin transmembrane transporter activity [GO:0032217]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.

IPR003593;IPR013525;IPR003439;IPR043926;IPR027417;

3.40.50.300;

A0A3Q2GUW2

MFDKTRLPYVALDVLCVVLASMPMAVLNLGQIYPFQRGFFCKDNSIQYPYHDGTITTTVLSTVGLGLPISSMIIGETLSVYFNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIENYICRGNAQKVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKERNSPFKERKEEDSHTTLHETPTTGNHYRNNHQP

Equus caballus (Horse)

3.1.3.106; 3.1.3.4; 3.6.1.75

CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000256|ARBA:ARBA00000974}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000256|ARBA:ARBA00000974}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000256|ARBA:ARBA00000980}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000256|ARBA:ARBA00000980}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000256|ARBA:ARBA00001611}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000256|ARBA:ARBA00001611}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000256|ARBA:ARBA00000235}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000256|ARBA:ARBA00000235}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466; Evidence={ECO:0000256|ARBA:ARBA00023681}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256; Evidence={ECO:0000256|ARBA:ARBA00023681}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000256|ARBA:ARBA00001542}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000256|ARBA:ARBA00001542}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000256|ARBA:ARBA00001710}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000256|ARBA:ARBA00001710}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000256|ARBA:ARBA00001476}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000256|ARBA:ARBA00001476}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000256|ARBA:ARBA00001716}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000256|ARBA:ARBA00001716}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000256|ARBA:ARBA00001180}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; Evidence={ECO:0000256|ARBA:ARBA00035886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450; Evidence={ECO:0000256|ARBA:ARBA00035886}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683; EC=3.1.3.106; Evidence={ECO:0000256|ARBA:ARBA00001472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156; Evidence={ECO:0000256|ARBA:ARBA00001472}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000256|ARBA:ARBA00023977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000256|ARBA:ARBA00023977};

PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000256|ARBA:ARBA00005074}.; PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.

Cell membrane;Hydrolase;Lipid metabolism;Membrane;Reference proteome;Transmembrane;Transmembrane helix

ceramide metabolic process [GO:0006672]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; sphingosine metabolic process [GO:0006670]

apical plasma membrane [GO:0016324]; caveola [GO:0005901]; plasma membrane [GO:0005886]

ceramide-1-phosphate phosphatase activity [GO:0106235]; diacylglycerol diphosphate phosphatase activity [GO:0000810]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane raft {ECO:0000256|ARBA:ARBA00004314}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004314}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004189}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004189}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR036938;IPR000326;IPR043216;

1.20.144.10;

A0A3Q2GY53

MSLALNDLLICCHQLGHDRATERRKEVEKFKRLIRDPETVKQLDQHLDNKQGKYLNWDAVFRFLQKYIQKEIEHLRTAKPNVSASTQAGRQKKMQEISSLVKYFIKCANKRAPKLKCQELLNYIMDTMKDSSNGAISGADCSNILLKDILSVRKYWCEISQQQWLELLSVYFRLYLKPSQDINRVLVARIIQAVTKGCCSQTDGLNSKFLEYFSKAIQHARQEKSSAGLSHILAAFILFLKTLAVNFRIQVCELGDEILPTLLYVWTQHRLNDSLKEVMIELFQLQIYIHHPKGAKTQEKGAYESRKWKSILYNLYDLLVNEISRIGSRGKYSSGSRNIAVKENLIELMADICHQVFSEDTKSLEISQSYATTQRECNDSSVSCKKRKIELGWEVINDRLQKSQNDFDLVPWLQIATQLISKYPASLPNCELSPLLMILCQLLPQQRRGERTPYVLRCLMEVALCQGKKSNLESSQKSDLLKLWNKIWCITFRGISSEQIQAENFGLLGAIIQGSLIEVDREFWKLFTGSACKPSFPAVCCLTLALTICVVPETVKTGMEQNICEVNRSSSLKELIMKWLLFYQLEDDFEDSTELPPILHSNFPHLALEKILVSLTMKNCQAAMSFFQSVPECEKHQKDQDEPSFSEVEDLFLQTTFDKMDFLTIGKEHATEKHQPSIGFSVHQNLKESLNRCLLGLSEQLLNNYSSETTNSETLVRCSSLLVGVLGCYRYVGVIAEEEAYKSELFQKAKSLMQCAGESITLFKNKTNEESRIVSLRNMMHLCTSCLCNCTKHSPNKIASGFFLRLLTSKLMNDIADICRSLASFTKKPFDYGEVESMRDDTDKNLMETEDQSSMNLFDDCPTVSVGDANESGENQSTVGAINPLAEEHLSKQDLLFLDMLKFLCMCVTSAQTNTVSFRAADIRRKLLMLLDSSMLDPAKSLHLHMYLVLLKELPGEEYSLPMEDVVELLKPLSNVCSFYRRDQDVCKTVLNHVLHVVMNLRQGNMDAENTKDAQEQFLRVIEVFWRLTKEGKYAFSVRMALVKCLKTLLEADPYSKWAILKVKGNNFPVNEIFPQFLADDHHQVRMLAAESINRLFQDMEQGSSSRLLKALPLKLQQTAFENAYLKAQEGMRQVSQRAENPELLDDIYNRKAVLLMMIAVVLCCSPVCEKQALFALCKSVKDDGLEPHLVKKVLEKVSETFGYRNLEDFMASHLDYLILEWLNLRDNEYSLSSFPFILLNYANVEDFYRSCYKVLIPHLVIRSDFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEDTGDSGMAQQRETATKVYDMLKDENVLGKQIDHLFRSNLPEIVVELLMTLHEPATSGASQSTDLCDFSGDLDPAPNPPHFPSHVIKATFAYISSCHKTKLKSIVEILSKSPDSYQKILLAICVQAAETNNIYKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINKRPSRFRDVSLRSFSLCCDLLSQVCHTAVTYCKDALESHLHVIVGTLIPLVDDQMEVQKQVLDLLKYLVIDNKDNENLYMTIKLLDPFPDHVVFKDLRITQQKIKYSGGPFSLLEEINHFLSVSKYDALPLTRLEGLKDLRRQLEQHKDQMMDLMRASQDNPQGGIMVKLVVGLLQLSKMAINHTGEREVLEAVGSCLGELGPIDFSTIAVQHSKDTSYTKALELFEDKELQWTFIMLTYLNNTLVEDCVKVRSAAVTCLKNILATKTGHSFWEIYKKTTDPMLIYLHPFRTSRKKFLEVPRIDKENPLEGLDDTSLWIPQSKNHDIWIKTLTCAVLDSGGTKSEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRNLLSTHIQGFFTNCFRHSSQTSRSTTPANLDSESEHIFRGCLDKKSQRTMLAIVDYMRRQKSNSGQPILSLWSMDPLVENRPSSGTVFDEAFWLELNYLEVAKVAQSCAAHFTALLYAEIYADKKSMEDQEKRSTLVTNRSLTFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPLTRLRTYEHEAMWGKALVTYDLETAISSSTRQAGIIQALQNLGLCHILSVYLKGLDHENKEWCAELQELHYQAAWRNMQWDHCICVNKGAEGASYHKSLYNALQSLRDREFSTFYESLKYARVKEVEELCKGSLESVYSLYPTLSRLQTIGELENIGELFSRSVTDRQPSEVYIKWRKHSQLLKDSDFSFQEPIMALRTVILEILMEKEMESSQRQCFKDILTKHLVELSTLARTFKNTQLPERAIFQIKQYNSASCGVSEWQLEEAQVFWAKEEQSLALSILKQMIKKLDASCTENDPNLKLMYTECLRICGNWLAETCLENPAVIMQTYLEKAVEVAGNCDGESNDELRNGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNRYTIKVQRELELDECALRALKEDRKRFLCKAVENYISCLLSGEGHDMWIFRLCSLWLENSGVSEVNGMMKANGIKIPSYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANKDEFLTKPEAARRSRITKSAPKQSSQLDEDRTEAANKIIHTIRTRRPQMIRSVEALCDAYIILANLDATQWRTQRQGINIPADQPITKLQNLEDVVVPTMEIKVDPTGEYENLVTIQSFKAEFRLAGGLNLPKIIDCLGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNENGAHKRYRPEDFSALQCQKKMMDVQKKSFEEKYATFMDICQNFQPVFRYFCMEKFLDPAVWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDETELHSTPHADDQECKRNLSDVDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAMDPKNLSRLFPGWKAWV

Equus caballus (Horse)

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;Coiled coil;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;

A0A3Q2H348

MTEARAARGALAGPLRALCVLGCLLGRAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQSTIETMRKPRCGNPDVANYNFFPRKPKWEKTQITYRIIGYTPDLDPETVDDAFARAFRVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYTSCTDTGRSDGFLWCSTTYNFDKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKHEGCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKHFRLSHDDIKGIQELYGGSPDTGTGPTPTLGPVTPEICKQDIVFDGISQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKTDWLGC

Equus caballus (Horse)

3.4.24.24

CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.; EC=3.4.24.24; Evidence={ECO:0000256|ARBA:ARBA00000178};

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

blood vessel maturation [GO:0001955]; bone trabecula formation [GO:0060346]; cellular response to amino acid stimulus [GO:0071230]; 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]; face morphogenesis [GO:0060325]; intramembranous ossification [GO:0001957]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; proteolysis [GO:0006508]; response to amyloid-beta [GO:1904645]; response to hypoxia [GO:0001666]; tissue remodeling [GO:0048771]

extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; sarcomere [GO:0030017]

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;IPR036365;

3.40.390.10;2.10.10.10;2.110.10.10;

A0A3Q2H4E6

MELAAWCRWGLLLALLPPGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPASASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDLLDNATSATGAVPGGLRELQLRSLTGEILKGGVLIQRNPQLCHQDTILWEDIFHKNNQLTLTLIDTNRSRACQPCSPACRPSHCWGESSEDCQNLTRTVCAGGCARCKGPRPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPSLVIYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQDFAGCKKIFGSLAFLPESFEGDPASNTAPLQPEQLRVFETLEEITGYLYISAWPDSLPDLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLQELGSGLALVHHNARLCFVHTVPWAQLFRNPHQALLHSANRPEDECVGEGLACYPLCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCLPCHPECQPQNGSVTCFGSEADQCVACTHYKDPPFCVARCPSGVKPDLSFMPIWKFPDEEGTCQPCPINCTHSCLDLDDRGCPAEQRASPVTSIIAAVVGILLVVVIGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGTAHRRHRSSSSRSGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPQHDPSPLQRYSEDPTVPLPPETDGYVAPLSCSPQPEYVNQPEVRPQPPSPLEGPLSPCRPDGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLAPRSRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV

Equus caballus (Horse)

FUNCTION: In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth. {ECO:0000256|ARBA:ARBA00037619}.

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;Cytoplasm;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transcription;Transcription regulation;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

cellular response to epidermal growth factor stimulus [GO:0071364]; ERBB2-EGFR signaling pathway [GO:0038134]; ERBB2-ERBB3 signaling pathway [GO:0038133]; ERBB2-ERBB4 signaling pathway [GO:0038135]; heart development [GO:0007507]; immature T cell proliferation in thymus [GO:0033080]; motor neuron axon guidance [GO:0008045]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066]; negative regulation of immature T cell proliferation in thymus [GO:0033088]; neurogenesis [GO:0022008]; neuromuscular junction development [GO:0007528]; neuron differentiation [GO:0030182]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; oligodendrocyte differentiation [GO:0048709]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of translation [GO:0045727]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of microtubule-based process [GO:0032886]; Schwann cell development [GO:0014044]; semaphorin-plexin signaling pathway [GO:0071526]; wound healing [GO:0042060]

apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; ERBB3:ERBB2 complex [GO:0038143]; myelin sheath [GO:0043209]; neuromuscular junction [GO:0031594]; nucleoplasm [GO:0005654]; presynaptic membrane [GO:0042734]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]; semaphorin receptor complex [GO:0002116]

ATP binding [GO:0005524]; coreceptor activity [GO:0015026]; ErbB-3 class receptor binding [GO:0043125]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; receptor tyrosine kinase binding [GO:0030971]; RNA polymerase I core binding [GO:0001042]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]

SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR006211;IPR006212;IPR032778;IPR009030;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR049328;IPR008266;IPR020635;IPR016245;

1.20.5.100;4.10.1140.10;3.80.20.20;1.10.510.10;

A0A3Q2H7S2

MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISSTPDSRKRTRHFNNNINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPISSMKVGEKKEVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINKELMKNVSYNPLLLLTPQKIKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDESQEPKGTENEDAERDYQNDNQASWVHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLRNFTTQESLDEDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVPRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKNAIVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLNKPTA

Equus caballus (Horse)

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;

A0A3Q2H8N6

MRMSFGLTFRTAKGHWLVNLSRQCSHGSTGLFVPPSPPLDPEKVKELQRFITLSKRLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHGDFIRSAPIRQRYWARNFVGWPQFSSHQPNPAHLALSNWERLGKLYWLVTQNVDALHTKAGSQRLTELHGCMHRVLCLHCGEQTPRGVLQERFEVLNPTWSAEAHGLAPDGDVFLTEEEVQNFQVPSCARCGGPLKPDVVFFGDTVSADKVDFVHRRVKEADSLLVVGSSLQVSDLVAGGNCPFWGIGSPGEAPLLVSLFMHLESSYLALLLVQVYSGYKFILTAWEKKLPIAILNIGPTRSDGLACLKLDSRCGELLPLIDPH

Equus caballus (Horse)

FUNCTION: Acts as NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels. Down-regulates insulin secretion. {ECO:0000256|HAMAP-Rule:MF_03161}.

2.3.1.-; 2.3.1.286; 2.4.2.-

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NAD(+) = 2''-O-lipoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:63640, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10474, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:83099, ChEBI:CHEBI:189572; Evidence={ECO:0000256|HAMAP-Rule:MF_03161}; 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:0000256|HAMAP-Rule:MF_03161}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-biotinyl-L-lysyl-[protein] + NAD(+) = 2''-O-biotinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70479, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:83144, ChEBI:CHEBI:189573; Evidence={ECO:0000256|HAMAP-Rule:MF_03161}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540, ChEBI:CHEBI:140607; Evidence={ECO:0000256|HAMAP-Rule:MF_03161};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_03161}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03161};

Metal-binding;Mitochondrion;NAD;Reference proteome;Transferase;Transit peptide;Zinc

DNA damage response [GO:0006974]; glutamine metabolic process [GO:0006541]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of insulin secretion [GO:0046676]; positive regulation of lipid biosynthetic process [GO:0046889]; regulation of glutamine family amino acid metabolic process [GO:0000820]; tricarboxylic acid metabolic process [GO:0072350]

mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]

histone deacetylase activity [GO:0004407]; lipoamidase activity [GO:0061690]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ binding [GO:0070403]; NAD+- protein-cysteine ADP-ribosyltransferase activity [GO:0140803]; NAD-dependent protein biotinidase activity [GO:0106420]; NAD-dependent protein deacetylase activity [GO:0034979]; NAD-dependent protein lipoamidase activity [GO:0106419]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-Rule:MF_03161}.

IPR029035;IPR003000;IPR026591;IPR026587;IPR026590;

3.30.1600.10;3.40.50.1220;

A0A3Q2HBN5

MGQQPGKVLGDQRRPSLPALHFIKGAGKKESSRHGGPHCNVFVEHALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFSTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSERPSFAEIHQAFETMFQESSISDEVEKELGKKGVRGAAGPLLQAPELPTKTRTSRRAAEHKDSTDGAETPHPKGPGETDPLDHEPAVSPLLPRKERGPQDGGLNEDERLLPKDKKTNLFSALIKKKKKTAPAPPKRSSSFREMDGQPERKVAGEEEGREVSNGALALAPSDTPEPAKSPKPSSGAGVPNGAFRESGGAGFRSPHLWKKSSTLTSSRLAASEEENGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRASETRSDQVTRGTVTPPPRLVKKTEEAVDEVLRDAAESSPGSSPPSLTPKLLRRQVVVAPSSGLPHKEEAGKSSAFGTPAAEPVPPTSRAGPGASGGTSKAPNEESRVRRHKPSSESPGRDKGKLSKLKPAPPPPPPASVGKAGKPSQSPSQEAAGEAGACGKAKPTALVVDAVNSDTAKPSQLGEGVKKAVLPAVPKSQSSTKPAGTPTSPVPAPSVLPSASSTLAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDGTEALCLAISKNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR

Equus caballus (Horse)

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};

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

actin cytoskeleton organization [GO:0030036]; activated T cell proliferation [GO:0050798]; 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;

A0A3Q2HCI1

MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQGGSGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQMRLSKKMLDPEKPQLGMIDRWYHPNCFVKNREELGFRPEYSASQLKGFSLLSPEDKEALKKQLPGVKTEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKACSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKIKKQDRIFPPETSAPAAAAPPPSAVSAPATVNASALPDKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTTSKASLCISTQKEVEKMNKKMEEVKEANLRVVSEDFLQDVSTSTKSLQELLSAHILSPWGAEVKAEPVEVAAPRGKSGAALPKKSKGPVKEEGSNKSEKRMKLTLKGGAAVDPDSGEQSGLCSPSSLGDRVGGSLPSPGSARLLWGTSRRWWSHIQAVVGPAPGDPLLPGRPGPSVGEKTVGAFSATGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGSNKREQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTLNPGTKSKLPKPVQELIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQALSQGSGDSQILDLSNRFYTLIPHDFGMKKPPLLNNTDSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDKDSEEAETIRKYVKNTHATTHNAYDLEVVDIFKIEREGESQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSASVTMDGVEVPLGTGISSGVSDTCLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW

Equus caballus (Horse)

2.4.2.-

CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000256|ARBA:ARBA00024164}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; Evidence={ECO:0000256|ARBA:ARBA00024164}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence={ECO:0000256|ARBA:ARBA00024159}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; Evidence={ECO:0000256|ARBA:ARBA00024159}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + NAD(+) = H(+) + N(tele)-(ADP-D-ribosyl)-L-histidyl-[protein] + nicotinamide; Xref=Rhea:RHEA:72071, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:18085, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29979, ChEBI:CHEBI:57540, ChEBI:CHEBI:191398; Evidence={ECO:0000256|ARBA:ARBA00034220}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72072; Evidence={ECO:0000256|ARBA:ARBA00034220}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540, ChEBI:CHEBI:142556; Evidence={ECO:0000256|ARBA:ARBA00024165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233; Evidence={ECO:0000256|ARBA:ARBA00024165}; CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540, ChEBI:CHEBI:142557; Evidence={ECO:0000256|ARBA:ARBA00024171}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237; Evidence={ECO:0000256|ARBA:ARBA00024171};

ADP-ribosylation;Chromosome;Coiled coil;DNA damage;DNA repair;DNA-binding;Glycosyltransferase;Metal-binding;NAD;Nucleotidyltransferase;Nucleus;Reference proteome;Transferase;Zinc;Zinc-finger

apoptotic process [GO:0006915]; ATP generation from poly-ADP-D-ribose [GO:1990966]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxidative stress [GO:0034599]; cellular response to UV [GO:0034644]; DNA ADP-ribosylation [GO:0030592]; double-strand break repair [GO:0006302]; innate immune response [GO:0045087]; mitochondrial DNA repair [GO:0043504]; negative regulation of ATP biosynthetic process [GO:2001170]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of innate immune response [GO:0045824]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of single strand break repair [GO:1903518]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein auto-ADP-ribosylation [GO:0070213]; protein localization to chromatin [GO:0071168]; regulation of base-excision repair [GO:1905051]; regulation of protein localization [GO:0032880]; replication fork reversal [GO:0071932]

chromatin [GO:0000785]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nuclear envelope [GO:0005635]; nuclear replication fork [GO:0043596]; nucleolus [GO:0005730]; site of double-strand break [GO:0035861]; transcription regulator complex [GO:0005667]

damaged DNA binding [GO:0003684]; NAD DNA ADP-ribosyltransferase activity [GO:0140294]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+- protein-aspartate ADP-ribosyltransferase activity [GO:0140806]; NAD+-histone H2BS6 serine ADP-ribosyltransferase activity [GO:0140816]; NAD+-histone H3S10 serine ADP-ribosyltransferase activity [GO:0140817]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; NAD+-protein-glutamate ADP-ribosyltransferase activity [GO:0140807]; NAD+-protein-histidine ADP-ribosyltransferase activity [GO:0140815]; NAD+-protein-tyrosine ADP-ribosyltransferase activity [GO:0140808]; nucleosome binding [GO:0031491]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; zinc ion binding [GO:0008270]

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

IPR001357;IPR036420;IPR038650;IPR049296;IPR012982;IPR012317;IPR004102;IPR036616;IPR036930;IPR008893;IPR001510;IPR036957;

1.10.20.130;2.20.25.630;3.90.228.10;3.40.50.10190;1.20.142.10;3.30.1740.10;

A0A3Q2HCI4

MNSPGGRGKKKGSGGASSPVPPRPPPPCLAAARPAPRPAPAPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSRATPAPASASPPAPVPGGEAERVRAFHKQAFEYISIALRIDEDEKGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPVLQFSKSQTDVYNDSTNLTCRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSTGLSGHHRAPSCSGLSMVSGVRQGPGPATATHKSTPKTNRTNKPSTPTTAARKKKDLKNFRNVDSSLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTKRVYVSLPNEETRLLLLKNLLGKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV

Equus caballus (Horse)

FUNCTION: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000256|HAMAP-Rule:MF_03021}.

5.6.1.1

CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00036378, ECO:0000256|HAMAP-Rule:MF_03021};

Allosteric enzyme;ATP-binding;Cell cycle;Cell division;Cytoplasm;Cytoskeleton;Developmental protein;Differentiation;Endoplasmic reticulum;Isomerase;Membrane;Microtubule;Neurogenesis;Nucleotide-binding;Nucleus;Reference proteome;Transmembrane;Transmembrane helix

axonogenesis [GO:0007409]; cytokinetic process [GO:0032506]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; metabolic process [GO:0008152]; microtubule severing [GO:0051013]; positive regulation of microtubule depolymerization [GO:0031117]; protein hexamerization [GO:0034214]

axon [GO:0030424]; centrosome [GO:0005813]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]

SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03021}. Midbody {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000256|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. {ECO:0000256|HAMAP-Rule:MF_03021}.

IPR003593;IPR041569;IPR003959;IPR003960;IPR027417;IPR015415;IPR017179;IPR035106;

1.10.8.60;3.40.50.300;1.20.58.80;

A0A3Q2HD01

MARGYVCVLALAAVLLLGIAAVSRSKGLRGKEPQRASRVPSEFSQGERVAMKEGLKGAIQIPTVSFSPNEFNTTALAEFGEYIHEVFPTVFKTSFIQHEVVGEYSHLFTVQGSDPNLQPYMLLAHIDVVPAPDEGWEVPPFSGLERDGFIYGRGTLDNKNSVMAILQALELLLIRSYVPRRSFFIALGHDEEVSGANGAQKISALLQARGIQLAFIVDEGSFILDGLVPNLKKPFAMVAVSEKGMLNLELQVNMTPGHSSAPPEETSIGILAAAVSRLEQTPMPNMFGGGPLKMALQQLADEFPFPINIVLSNLWLFRPLVSRLMERNKITSALVRTTTAVTMFKAGIKVNVIPSVAQATVNFRIHPAQTVQQVLELVKNIVADDRVQFHVLNAVDPLPNSPSDSQAFGYQLLCQTIQSVFPEVHIVVPGICIGNTDSRHYTNLTTGIYRFNPVYLQPQGSYGLRA

Equus caballus (Horse)

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;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;

A0A3Q2HFQ8

MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERNDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMNPPLLHHDLKTQNILLDNEFHVKPVILVFSVPSSCCSGLAIPGPQDQEFDIDTMHIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASVKHDIYSYAVITWEVLSRKQPFEEVTNPLQIMYSVSQGHRPDTNEESLPFDIPHRALMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSASSTVHLCDKKKMELSLNLSVNHGPQEESCGSSQLHKSSSSLRTSKSLSAQDNDFLSRKTEDYSVLHHCPVNHSCDSNIPAAQRATFCDHKTTPCALAIINSLSAEGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEIFMASRSPSLNLFQNKSL

Equus caballus (Horse)

FUNCTION: Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses. Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments. {ECO:0000256|PIRNR:PIRNR037921}.

2.7.10.2; 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, ECO:0000256|PIRNR:PIRNR037921}; 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|PIRNR:PIRNR037921}; 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|PIRNR:PIRNR037921};

Adaptive immunity;Apoptosis;ATP-binding;Cytoplasm;Immunity;Innate immunity;Isopeptide bond;Kinase;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase;Ubl conjugation

adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; cellular response to muramyl dipeptide [GO:0071225]; defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070427]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; protein homooligomerization [GO:0051260]; toll-like receptor 2 signaling pathway [GO:0034134]

cytoskeleton [GO:0005856]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; vesicle [GO:0031982]

ATP binding [GO:0005524]; CARD domain binding [GO:0050700]; caspase binding [GO:0089720]; JUN kinase kinase kinase activity [GO:0004706]; LIM domain binding [GO:0030274]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein tyrosine kinase activity [GO:0004713]; signaling adaptor activity [GO:0035591]; signaling receptor binding [GO:0005102]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037921}.

IPR001315;IPR042149;IPR011029;IPR011009;IPR000719;IPR017322;IPR001245;IPR008271;

1.10.533.10;1.10.510.10;

A0A3Q2HH33

MHVSCWAQIDCIRIWSGRETKECALLTKHFRIMTLDPPRRGLLMLLMALGLTQSDPVKPSRGPLLTCTCDSPHCSRPTCQGAWCTVVLVREEGSHPQEHRGCGNLHQELCRGRPTEFVNHYCCYSPLCNQNVSLVLEATPTPEQPQVDGQLPLILGPVLAFLALVALGTLGLWHVRRRQEKQRGLHSELGESSLILKASEQGDSMLGDLLDSDCTTGSGSGLPFLVQRTVARQVALVECVGKGRYGEVWRGLWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQGSDYLDIGNNPRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEITRRTTVNGIVEDYRPPFYDVVPNDPSFEDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLSNSLEKAKVIH

Equus caballus (Horse)

2.7.11.30

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};

ATP-binding;Kinase;Manganese;Membrane;Nucleotide-binding;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix

angiogenesis [GO:0001525]; blood vessel remodeling [GO:0001974]; BMP signaling pathway [GO:0030509]; cellular response to growth factor stimulus [GO:0071363]; dorsal aorta morphogenesis [GO:0035912]; dorsal/ventral pattern formation [GO:0009953]; endocardial cushion morphogenesis [GO:0003203]; endothelial tube morphogenesis [GO:0061154]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; lymphangiogenesis [GO:0001946]; lymphatic endothelial cell differentiation [GO:0060836]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell growth [GO:0030308]; negative regulation of endothelial cell differentiation [GO:0045602]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of gene expression [GO:0010629]; positive regulation of angiogenesis [GO:0045766]; positive regulation of bicellular tight junction assembly [GO:1903348]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of endothelial cell differentiation [GO:0045603]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of blood pressure [GO:0008217]; retina vasculature development in camera-type eye [GO:0061298]; transforming growth factor beta receptor signaling pathway [GO:0007179]; venous blood vessel development [GO:0060841]; wound healing, spreading of epidermal cells [GO:0035313]

BMP receptor complex [GO:0070724]; cell surface [GO:0009986]; plasma membrane [GO:0005886]

activin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; BMP receptor activity [GO:0098821]; protein kinase binding [GO:0019901]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]

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

IPR003605;IPR011009;IPR000719;IPR017441;IPR001245;IPR008271;IPR045860;IPR000333;

2.10.60.10;1.10.510.10;

A0A3Q2HJJ4

MKLRESLLGGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTSLQGGSNGAAAIGQPSRELRPPGAPPPLPWGASFQPRPGRDSSPDADSRPGPARNLTLAALSPGTAVSLPACPEESPLLVGPMMIEFNMAVDLNRVAEENPEVKLGGRYTPKDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQQSQLKEELLSVICLLLSTYLLFCTLHLLERERERSADLSTAVTAAAAATAAATLAGEAMFNRAKLLNVGFQEALKDYDYNCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKEQFLTINGFPNNYWGWGGEDDDIFNRLVFKGMSLSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMFLDGLNTLFYNVLDVQRYPLYTKVTVDIGTPS

Equus caballus (Horse)

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;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;

A0A3Q2HME7

MDVSADRVEEVQNVLNAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLRIIHAFELDTGLQFAHSYSFSKKENDSPERVKEEVSIIQSMGYRNRAKRHRQSEPENPTLQETSLSVHLSNLGIVRSLRTKQQIQPQNKSIYIELGSDSSEDTVNKASYCSLGDHELLQITPQGARAEASLNPTKKAACEFSEKAITNIEHHQSSNKDLTTTEKHAAEKHPEKYQGISVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLAKSQQSRRAESKETCNDRQAPNSEEKLVLNADPLYGREELNKQKPPRSDSPRDSQDVPWITLNSSIQKVNEWFSRSEEMLTSDDSCDGGPESNTEVAGAVEVPNEVRGYSGSSEKIDLMAGDPSSALICESERVRSKPVENNIEDRIFGKTYRRKASFPNLSHITEDLIIGASAIEPQITQERSLTNRVKHKRRTSSGLHPEDFIKKVDLAVVQKTPEKIIEGTDQIEQNSHVMNIIPNGHGNETKGDYVQNEKNANLTESLETESAFRTKAEPISSSIGNLELELNIHSSKAPKKNRLRRKSCTKQIHALELVVSKNPSPPNHTELQIDSCSSSEEMKKKNSDQMPVRHSKKLQLMEDKEPATGAKKSNKPNEQINKRLASDAFPELKLTNIPGFFTNCSSSNKLHEFVNPSLQREEIEQNLGANRLSNSAKDPKDLILSGGKCLQAERSVESSGISLVPDTDYGTQDSISLLEADTLGKAKTAPNQCANLCAAIENPKELTHDCSKDTRNDTQGVKDPLRREVNHTQETSIEMEESEFDTQYLQNMFKVSKRQSFALFSNPGSPEKKCATVSAHSRSLRKRSPKVTLKCGQKEGKEGKKESKIKNVQSVHTTVGFPVICQKDKKPGDYVKCSTKEASRLCQSSQFRGNETELITANKHGISQNPYYIPSLSPIRSSVKTVCQKNLPEGKLEEQSLSPERAMGNESIVQSTVSTISQNNIRESTLKEVSSSSINEVGSSINEVGSSGEHIQAELGRNRGPKLNAILRLGLMQPEVYKQSLPISNCKHLEIKRQGEKEVVQAVNADFSPCLISDNLEQPMGSSCASQVCSETPDDLLNDDEIKENISFAESGVKERSAVFSKSVQKGKFRRSPSPIGRTCLAQGHQRRARKLESSEENTSSEDEELPCFQHLLFGKVTNLPSQSTSHAAATEGLSKKTEESLVSLQNSLDDCSHQVALAEACQEHHLSEEARCSGSLFSSQCSALEDLPANTNTQEPVLMFDPPSKQVREQSENHEVVSDKELVSDDDEREPGLEEDSHHEEQSVDSILDEVASGYVSETNLSEDCSGLSSQSDILTTQQRDTMQDNLIKLQQKMAELEAVLEQHGSQPSNRSPSLIADCCASEDLLNPEQNTSERVLTSEKSSEYPISQNPENLSADKFQISLDSSTSKNREPEMERSSPSKSQLLDNRWCVHSHSRSLQNRNCPSQKEFIKAVDAEEQQLTKSEAQDLMEQSYLPRQDLEATPYLESGISLFSHEPESDPSEERALEAAHVCSMPASTSAMKSLQFRVEESAKSPAGAHTTNIVGSNVKEDSVSREKPEMISSTERVIRRISMVASGLTPKEFMLVHKFARKHHITLTNLVTEETTHVIMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKVLDEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCCGPFTNMPTDQLEWMVRLCGASVVKEPSSFTFSEGTHPVVVVQPDAWTEDSGFHMIGQMCEAPVVTRELLKDSCLRITPPGPGASPLSDPQPQP

Equus caballus (Horse)

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};

Acetylation;Activator;Cell cycle;Chromosome;Coiled coil;DNA damage;DNA recombination;DNA repair;DNA-binding;Fatty acid biosynthesis;Fatty acid metabolism;Isopeptide bond;Lipid biosynthesis;Lipid metabolism;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger

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]; fatty acid biosynthetic process [GO:0006633]; 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: Chromosome {ECO:0000256|ARBA:ARBA00004286, ECO:0000256|PIRNR:PIRNR001734}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {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;IPR018957;IPR001841;IPR013083;IPR017907;

3.40.50.10190;3.30.40.10;

A0A3Q2HQI2

MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDVLKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSGKRGPLLPNPAGGEGRHPQPAKPPRSREGRHPQPPQPPRSREGRSPEPPRSREGRRPQPPQPPWSREGHSPEIPRSREGRSPQPPLPPRSREGSHPQRPRSREGRRPQPPRSREGRRPQPPRSREGRRPQPPQPPWSREGRSPEPPRSREGRHPQPPQPPRSREGRHSEPPRSREGRHPEPPRSREGRHPEPPRSREGHHPEPPRSREGRSPEPPRSREGRSPEPPRSREGRSPEPPRSREGRSPEPPWQPLPWDCGLSPRVCGPAGAGLP

Equus caballus (Horse)

3.1.3.16

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001512}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001482, ECO:0000256|RuleBase:RU004273};

COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000256|ARBA:ARBA00001965}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

Calmodulin-binding;Hydrolase;Iron;Metal-binding;Reference proteome

calcineurin-NFAT signaling cascade [GO:0033173]; calcium ion transport [GO:0006816]; cardiac muscle hypertrophy in response to stress [GO:0014898]; dendrite morphogenesis [GO:0048813]; dephosphorylation [GO:0016311]; excitatory postsynaptic potential [GO:0060079]; G1/S transition of mitotic cell cycle [GO:0000082]; keratinocyte differentiation [GO:0030216]; multicellular organismal response to stress [GO:0033555]; negative regulation of angiotensin-activated signaling pathway [GO:0110062]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of gene expression [GO:0010629]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cardiac muscle hypertrophy in response to stress [GO:1903244]; positive regulation of cell migration [GO:0030335]; positive regulation of connective tissue replacement [GO:1905205]; positive regulation of endocytosis [GO:0045807]; positive regulation of gene expression [GO:0010628]; positive regulation of glomerulus development [GO:0090193]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of saliva secretion [GO:0046878]; positive regulation of transcription by RNA polymerase II [GO:0045944]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; protein import into nucleus [GO:0006606]; regulation of cell proliferation involved in kidney morphogenesis [GO:0061006]; renal filtration [GO:0097205]; response to calcium ion [GO:0051592]; skeletal muscle fiber development [GO:0048741]; transition between fast and slow fiber [GO:0014883]

calcineurin complex [GO:0005955]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; Schaffer collateral - CA1 synapse [GO:0098685]; Z disc [GO:0030018]

ATPase binding [GO:0051117]; calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; cyclosporin A binding [GO:0016018]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein dimerization activity [GO:0046983]

IPR004843;IPR029052;IPR041751;IPR043360;IPR006186;

3.60.21.10;

A0A3Q2HUA3

MTTTTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCMQYLDRAEKLKDYLRNKEKHSKKPVKENQSESKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIQELARKTEGYSGADISVIVRDSLMQPVRKVQSATHFKKVCGPSRTNPSIMIDDLLTPCSPGDPGAMEMTWMDVPSDKLLEPVVCMSDMLRSLATTRPTVNAEDLLKVKKFSEDFGQES

Equus caballus (Horse)

3.6.4.6

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

abscission [GO:0009838]; endosomal transport [GO:0016197]; endosomal vesicle fusion [GO:0034058]; intracellular cholesterol transport [GO:0032367]; late endosomal microautophagy [GO:0061738]; midbody abscission [GO:0061952]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic metaphase chromosome alignment [GO:0007080]; multivesicular body assembly [GO:0036258]; negative regulation of cytokinesis [GO:0032466]; nucleus organization [GO:0006997]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of viral budding via host ESCRT complex [GO:1903774]; protein targeting to lysosome [GO:0006622]; regulation of protein localization to plasma membrane [GO:1903076]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway [GO:0090611]; vacuole organization [GO:0007033]; vesicle budding from membrane [GO:0006900]; vesicle uncoating [GO:0072319]; viral budding from plasma membrane [GO:0046761]; viral budding via host ESCRT complex [GO:0039702]

centrosome [GO:0005813]; cytosol [GO:0005829]; early endosome [GO:0005769]; Flemming body [GO:0090543]; late endosome membrane [GO:0031902]; lysosome [GO:0005764]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; spindle pole [GO:0000922]; vacuolar membrane [GO:0005774]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; protein-containing complex binding [GO:0044877]

SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004633}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004633}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.

IPR003593;IPR041569;IPR003959;IPR003960;IPR007330;IPR036181;IPR027417;IPR015415;IPR045253;

1.10.8.60;3.40.50.300;1.20.58.80;

A0A3Q2HV27

MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFDQQWQLKYPKLILREAGSVPEELHKEVQEAFFALHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNAKYNEAEIAAACQSFLKLNDYLQTETIQALEELAAKDKANIDAVPVCIGPDFPRLGMGSSFDGQDEMDIKNRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVERSAVAVYSYSCEGPEEESEDDPQLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDYTVQGTSTQLCSLTRSWCGGGMVRDKDDLNATHQHCVLAGLPPRFSSTHRVAECSTGTLDYIVQRCQLALQNIRDETDNGDVSLKSLEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYKKCTDWWCQPMTQLEELWKKMEAVTNAVLHEVRQEGVPVEQRNEILTAILASLTTRQNLRREWHARCQCRIARTLPVDQKPECRPYWEKDDPSMPLPFDLTDIISELRGLLLEAKP

Equus caballus (Horse)

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;

A0A3Q2HV61

MENHMFSVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGQPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTRPLGPPTAAIDLSHQPSASKEQPLTVDGATGPGNGPQHAQDNRQEAGSLCHTNGLAPRPSSQEPAKKSAGIALQGSGKNNELLREIEPVLSLLASGGKGINGGGPAKMETKDAEVQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPASGKQSPTKNGSPSKCPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHIRRPEDVRTKQQLFPLAKEFIDQYYSSIKRSGSKAHMERLEEVNKEIETTSTYQLRDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHIKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSILGDPANVEFTEICTQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDLRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVHEERKYPEPLRFFPRKGPPLPRGDTEVHGLAAARDSQRRSYKVRFNSVSSYSDSRKSSGDGPDLRDNFESTGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTYVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGNQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQLVKVELLEERNTALGVISNWTDEHRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAVVSYRTRDGEGPIHHGVCSSWLNRIQADEGVPCFVRGAPSFRLPRNPLVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMSPCPMVLVFGCRQSKIDHIYKEETLQAKSKGVFRELYTAYSREPDKPKKYVQDVLQEQLAETVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSVEDAGVFISRLRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS

Equus caballus (Horse)

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;

A0A3Q2HWP9

MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVHLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG

Equus caballus (Horse)

3.6.4.6

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=3.6.4.6; Evidence={ECO:0000256|ARBA:ARBA00000161};

ATP-binding;Autophagy;Endoplasmic reticulum;Lipid-binding;Nucleotide-binding;Proteomics identification;Reference proteome

aggresome assembly [GO:0070842]; ATP metabolic process [GO:0046034]; autophagosome maturation [GO:0097352]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; cellular response to misfolded protein [GO:0071218]; double-strand break repair [GO:0006302]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; endosome to lysosome transport via multivesicular body sorting pathway [GO:0032510]; ERAD pathway [GO:0036503]; flavin adenine dinucleotide catabolic process [GO:0072389]; mitotic spindle disassembly [GO:0051228]; NADH metabolic process [GO:0006734]; negative regulation of protein localization to chromatin [GO:0120186]; negative regulation of smoothened signaling pathway [GO:0045879]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of mitochondrial membrane potential [GO:0010918]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of oxidative phosphorylation [GO:1903862]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein K63-linked deubiquitination [GO:1903006]; positive regulation of protein-containing complex assembly [GO:0031334]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; protein-DNA covalent cross-linking repair [GO:0106300]; retrograde protein transport, ER to cytosol [GO:0030970]; stress granule disassembly [GO:0035617]; translesion synthesis [GO:0019985]; viral genome replication [GO:0019079]

ATPase complex [GO:1904949]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; Derlin-1 retrotranslocation complex [GO:0036513]; lipid droplet [GO:0005811]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; proteasome complex [GO:0000502]; site of double-strand break [GO:0035861]; synapse [GO:0045202]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]; VCP-NSFL1C complex [GO:1990730]

ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; BAT3 complex binding [GO:1904288]; deubiquitinase activator activity [GO:0035800]; identical protein binding [GO:0042802]; K48-linked polyubiquitin modification-dependent protein binding [GO:0036435]; lipid binding [GO:0008289]; MHC class I protein binding [GO:0042288]; polyubiquitin modification-dependent protein binding [GO:0031593]; protein domain specific binding [GO:0019904]; protein phosphatase binding [GO:0019903]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-dependent protein binding [GO:0140036]; ubiquitin-specific protease binding [GO:1990381]

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR003593;IPR005938;IPR041569;IPR009010;IPR003959;IPR003960;IPR004201;IPR029067;IPR003338;IPR027417;IPR015415;

1.10.8.60;2.40.40.20;3.10.330.10;6.10.20.150;3.40.50.300;

A0A3Q2HXE5

MAALVLEDGSVLRGQPFGAAMSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLVGNYGIPPDEVDEFGLSKWFESSGIHVAGLVVGECCPTPSHWSAACTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQDGTDPAALPFLDPNARPLVPEVSIKAPRVFHAGGTPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHVLDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPVGWLPLFTNANDHSSEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLAERLCPRGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITSHYVTQVIRNERPDGVLLTFGGQTALNCGVELTRAGVLARYGVRVLGTPVKTIELTEDRRAFASRMAEIGEHIAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNKEELSALVATAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNNREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELSNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCAGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVERLYELTRIDRWFLHRMQRIIAHTQLLEQHRGQPLPQDLLHQAKRLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTSHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRILGTSPESIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEKVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADYYNEHGVKVTAVDWHFDEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGAAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLSAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQTVAAILMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSRDDLERLGPGKGQVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGPRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTVPSYMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLTPSAPAASEITTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAVFLLLGAGNPQGSREWAEEPKDKSARKAAEPELLGTLDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLHMPPNVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF

Equus caballus (Horse)

CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|ARBA:ARBA00000462}; CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|ARBA:ARBA00001777}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000256|ARBA:ARBA00043687}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000256|ARBA:ARBA00001062}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00001363};

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

PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|ARBA:ARBA00004812}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000256|ARBA:ARBA00004852}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|ARBA:ARBA00004880}.

ATP-binding;Glutamine amidotransferase;Hydrolase;Ligase;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Pyrimidine biosynthesis;Reference proteome;Repeat;Transferase

'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UDP biosynthetic process [GO:0006225]; UTP biosynthetic process [GO:0006228]

carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear matrix [GO:0016363]

amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]

IPR006680;IPR006132;IPR006130;IPR036901;IPR002082;IPR006131;IPR011761;IPR013815;IPR006275;IPR005480;IPR036897;IPR006274;IPR002474;IPR036480;IPR005479;IPR005483;IPR029062;IPR035686;IPR002195;IPR017926;IPR011059;IPR032466;IPR011607;IPR036914;IPR016185;

3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380;

A0A3Q2I212

MPRRGTPPLGHRGPGFPRLSGRDLLSHVLFHLWTTWATAAAAASLSPAKGDLGVSMSRSGGHLDLQRLRRTEVAARMVLLGLLQASGSVLVQAMEQVTGGSLLSLLLIACAFTLCLVYLFRLAVGHLAPLPADTKSPPYISSPVPFLGHAIAFGKSPVEFLENAYDKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKILKSGLNIANFRQHVSIIEKETKEYFQSWGEGGEKNLFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKNIFYKAIQNRRQSEEKMNDILQTLLESTYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQEKCYLEQKTVCGEDLPPLTYDQLKDLSLLDRCIKETLRLRPPIMTMMRLAKTPQTVAGYTIPPGHQVCVSPTVNQRLRDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK

Equus caballus (Horse)

1.14.14.154

CATALYTIC ACTIVITY: Reaction=24,25-dihydrolanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:45960, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78904; Evidence={ECO:0000256|ARBA:ARBA00036094}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45961; Evidence={ECO:0000256|ARBA:ARBA00036094}; CATALYTIC ACTIVITY: Reaction=24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxy-24,25-dihydrolanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75079, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87057; Evidence={ECO:0000256|ARBA:ARBA00035879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75080; Evidence={ECO:0000256|ARBA:ARBA00035879}; CATALYTIC ACTIVITY: Reaction=32-hydroxy-24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxo-24,25-dihydrolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75087, 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:87057, ChEBI:CHEBI:87060; Evidence={ECO:0000256|ARBA:ARBA00036454}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75088; Evidence={ECO:0000256|ARBA:ARBA00036454}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, 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:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000256|ARBA:ARBA00036809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000256|ARBA:ARBA00036809}; CATALYTIC ACTIVITY: Reaction=32-oxo-24,25-dihydrolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75083, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78904, ChEBI:CHEBI:87060; Evidence={ECO:0000256|ARBA:ARBA00035773}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75084; Evidence={ECO:0000256|ARBA:ARBA00035773}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000256|ARBA:ARBA00036056}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000256|ARBA:ARBA00036056}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000256|ARBA:ARBA00036132}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000256|ARBA:ARBA00036132}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, 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:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000256|ARBA:ARBA00036638}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000256|ARBA:ARBA00036638}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000256|ARBA:ARBA00036116}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000256|ARBA:ARBA00036116}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, 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:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000256|ARBA:ARBA00035798}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000256|ARBA:ARBA00035798}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000256|ARBA:ARBA00036211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000256|ARBA:ARBA00036211}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000256|ARBA:ARBA00036569}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000256|ARBA:ARBA00036569};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|PIRSR:PIRSR602403-1};

PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. {ECO:0000256|ARBA:ARBA00037887}.

Cholesterol metabolism;Heme;Iron;Lipid metabolism;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Proteomics identification;Reference proteome;Steroid metabolism;Sterol metabolism;Transmembrane;Transmembrane helix

bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; sterol metabolic process [GO:0016125]

endoplasmic reticulum membrane [GO:0005789]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Microsome membrane {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004111}.

IPR001128;IPR017972;IPR002403;IPR036396;

1.10.630.10;

A0A3Q2I3K3

MGLYRVRASTGSSLHAGSNNQVQLWLVGQHREAALGKRLWPARGKEAEFKVDVPEFLGPLLFVKLRKWHLLNDDAWFCNWISVQGPGASGDEFRFPRYRWVEGDGVLSLPEGTGERGVGFLNGTNPMLLRRSTRLPARLVFPPGMEELQAQLEKELQGGMLFEADFSLLDGIKANVILCSQQYLAAPLVLLKLQPDGKLLPMVIQLQLPREGSPPPPLFLPTDPPMVWLLAKCWVRSSDFQLHELQSHLLRYTMEINIRARSGLVSNMGIFDQVVSTGGGGHVELLRRAGPFLTYRSFCPSDDLEDRGLLGVKSSFYAQDALRLWEVIFRRYVEGIVNLHYKTDRAVKEDLELQTWCREITEIGLLGAQDRGFPVSLESRDQVCHFVTMCIFTCTGQHSSVHLGQLDWYAWVPNAPCTMRLPPPTTKDATLETVMATLPNVHQSSLQMSITWQLGRRQPVMVALGQHEEEYFSGPGPKAVLKKFREDLAALDKEIEIRNAKLDMPYEYLRPSLVENSVAI

Equus caballus (Horse)

1.13.11.12; 1.13.11.31; 1.13.11.33

CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8S)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:50216, ChEBI:CHEBI:57444, ChEBI:CHEBI:132129; Evidence={ECO:0000256|ARBA:ARBA00036803}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50217; Evidence={ECO:0000256|ARBA:ARBA00036803}; CATALYTIC ACTIVITY: Reaction=(14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14R,15S)-epoxy-(5Z,8Z,10E)-eicosatrienoate; Xref=Rhea:RHEA:50276, ChEBI:CHEBI:15379, ChEBI:CHEBI:131965, ChEBI:CHEBI:132063; Evidence={ECO:0000256|ARBA:ARBA00036582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50277; Evidence={ECO:0000256|ARBA:ARBA00036582}; CATALYTIC ACTIVITY: Reaction=(14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (5S)-hydroperoxy-(14R,15S)-epoxy-(6E,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:50280, ChEBI:CHEBI:15379, ChEBI:CHEBI:131965, ChEBI:CHEBI:132067; Evidence={ECO:0000256|ARBA:ARBA00036208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50281; Evidence={ECO:0000256|ARBA:ARBA00036208}; CATALYTIC ACTIVITY: Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14S,15R)-epoxy-(5Z,8Z,10E)-eicosatrienoate; Xref=Rhea:RHEA:50284, ChEBI:CHEBI:15379, ChEBI:CHEBI:131964, ChEBI:CHEBI:132065; Evidence={ECO:0000256|ARBA:ARBA00036149}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50285; Evidence={ECO:0000256|ARBA:ARBA00036149}; CATALYTIC ACTIVITY: Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (8S)-hydroperoxy-(14S,15R)-epoxy-(5Z,9E,11Z)-eicosatrienoate; Xref=Rhea:RHEA:50288, ChEBI:CHEBI:15379, ChEBI:CHEBI:131964, ChEBI:CHEBI:132068; Evidence={ECO:0000256|ARBA:ARBA00035753}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50289; Evidence={ECO:0000256|ARBA:ARBA00035753}; CATALYTIC ACTIVITY: Reaction=(15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:50152, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:82626; Evidence={ECO:0000256|ARBA:ARBA00035941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50153; Evidence={ECO:0000256|ARBA:ARBA00035941}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (14S,15S)-epoxy-(5Z,8Z,10E,12E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:50140, ChEBI:CHEBI:15377, ChEBI:CHEBI:57446, ChEBI:CHEBI:132070; Evidence={ECO:0000256|ARBA:ARBA00036658}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50141; Evidence={ECO:0000256|ARBA:ARBA00036658}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + O2 = 14-hydroperoxy-(4Z,7Z,10Z,12E,16Z)-docosapentaenoate; Xref=Rhea:RHEA:50824, ChEBI:CHEBI:15379, ChEBI:CHEBI:77226, ChEBI:CHEBI:133799; Evidence={ECO:0000256|ARBA:ARBA00036369}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50825; Evidence={ECO:0000256|ARBA:ARBA00036369}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (11S)-hydroperoxy-(4Z,7Z,9E,13Z,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:64732, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:156131; Evidence={ECO:0000256|ARBA:ARBA00036202}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64733; Evidence={ECO:0000256|ARBA:ARBA00036202}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:41332, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:78048; Evidence={ECO:0000256|ARBA:ARBA00036495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41333; Evidence={ECO:0000256|ARBA:ARBA00036495}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate; Xref=Rhea:RHEA:50840, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:133795; Evidence={ECO:0000256|ARBA:ARBA00035958}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50841; Evidence={ECO:0000256|ARBA:ARBA00035958}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (14R,15S)-dihydroperoxy-(5Z,8Z,10E,12E)-eicosatetraenoate; Xref=Rhea:RHEA:50928, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:133900; Evidence={ECO:0000256|ARBA:ARBA00036568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50929; Evidence={ECO:0000256|ARBA:ARBA00036568}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (8S,15S)-dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:50924, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:133899; Evidence={ECO:0000256|ARBA:ARBA00036449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50925; Evidence={ECO:0000256|ARBA:ARBA00036449}; CATALYTIC ACTIVITY: Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,14S)-dihydroperoxy-(4Z,8E,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:64724, ChEBI:CHEBI:15379, ChEBI:CHEBI:156049, ChEBI:CHEBI:156082; Evidence={ECO:0000256|ARBA:ARBA00035888}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64725; Evidence={ECO:0000256|ARBA:ARBA00035888}; CATALYTIC ACTIVITY: Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,17S)-dihydroperoxy-(4Z,8E,10Z,13Z,15E,19Z)-docosahexaenoate; Xref=Rhea:RHEA:64728, ChEBI:CHEBI:15379, ChEBI:CHEBI:140349, ChEBI:CHEBI:156049; Evidence={ECO:0000256|ARBA:ARBA00036949}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64729; Evidence={ECO:0000256|ARBA:ARBA00036949}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 = 14-hydroperoxy-(7Z,10Z,12E,16Z,19Z)-docosapentaenoate; Xref=Rhea:RHEA:50836, ChEBI:CHEBI:15379, ChEBI:CHEBI:77224, ChEBI:CHEBI:133798; Evidence={ECO:0000256|ARBA:ARBA00036752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50837; Evidence={ECO:0000256|ARBA:ARBA00036752}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12; Evidence={ECO:0000256|ARBA:ARBA00035889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781; Evidence={ECO:0000256|ARBA:ARBA00035889}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-alanine; Xref=Rhea:RHEA:50172, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071, ChEBI:CHEBI:132074; Evidence={ECO:0000256|ARBA:ARBA00035947}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50173; Evidence={ECO:0000256|ARBA:ARBA00035947}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanine; Xref=Rhea:RHEA:50184, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071, ChEBI:CHEBI:132077; Evidence={ECO:0000256|ARBA:ARBA00036420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50185; Evidence={ECO:0000256|ARBA:ARBA00036420}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-gamma-aminobutanoate; Xref=Rhea:RHEA:50176, ChEBI:CHEBI:15379, ChEBI:CHEBI:132072, ChEBI:CHEBI:132075; Evidence={ECO:0000256|ARBA:ARBA00036852}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50177; Evidence={ECO:0000256|ARBA:ARBA00036852}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-gamma-aminobutanoate; Xref=Rhea:RHEA:50180, ChEBI:CHEBI:15379, ChEBI:CHEBI:132072, ChEBI:CHEBI:132078; Evidence={ECO:0000256|ARBA:ARBA00035867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50181; Evidence={ECO:0000256|ARBA:ARBA00035867}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-glycine; Xref=Rhea:RHEA:50168, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002, ChEBI:CHEBI:132073; Evidence={ECO:0000256|ARBA:ARBA00036768}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50169; Evidence={ECO:0000256|ARBA:ARBA00036768}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycine; Xref=Rhea:RHEA:50188, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002, ChEBI:CHEBI:132076; Evidence={ECO:0000256|ARBA:ARBA00036165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50189; Evidence={ECO:0000256|ARBA:ARBA00036165}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-taurine; Xref=Rhea:RHEA:50160, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060, ChEBI:CHEBI:132061; Evidence={ECO:0000256|ARBA:ARBA00036438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50161; Evidence={ECO:0000256|ARBA:ARBA00036438}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurine; Xref=Rhea:RHEA:50156, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060, ChEBI:CHEBI:132062; Evidence={ECO:0000256|ARBA:ARBA00036945}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50157; Evidence={ECO:0000256|ARBA:ARBA00036945};

COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000256|PIRSR:PIRSR601885-1}; Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR601885-1};

PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000256|ARBA:ARBA00037897}.

Calcium;Cytoplasm;Dioxygenase;Iron;Lipid droplet;Lipid metabolism;Lipid-binding;Membrane;Metal-binding;Oxidoreductase;Reference proteome

arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372]

cytosol [GO:0005829]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886]

arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; iron ion binding [GO:0005506]; lipid binding [GO:0008289]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lipid droplet {ECO:0000256|ARBA:ARBA00004502}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.

IPR000907;IPR013819;IPR036226;IPR001885;IPR001024;IPR036392;IPR042062;

3.10.450.60;2.60.60.20;

A0A3Q2I833

MRSCDNEFPAGARGKLAWGGVEEYGALSINLRPPHKVGLEPRQGRIRVLTATLTAGQLRSMSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQENKREYEKRVSAIVEQSWNDS

Equus caballus (Horse)

2.3.2.23

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000256|ARBA:ARBA00000485};

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

ATP-binding;Cell membrane;Membrane;Nucleotide-binding;Reference proteome;Transferase;Ubl conjugation pathway

apoptotic process [GO:0006915]; chiasma assembly [GO:0051026]; chromatin organization [GO:0006325]; DNA repair [GO:0006281]; ectopic germ cell programmed cell death [GO:0035234]; in utero embryonic development [GO:0001701]; meiotic telomere clustering [GO:0045141]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of developmental process [GO:0051093]; negative regulation of post-translational protein modification [GO:1901874]; negative regulation of reproductive process [GO:2000242]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of reciprocal meiotic recombination [GO:0010845]; postreplication repair [GO:0006301]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein stabilization [GO:0050821]; response to UV [GO:0009411]; response to xenobiotic stimulus [GO:0009410]; sperm axoneme assembly [GO:0007288]; synaptonemal complex organization [GO:0070193]

cytoplasm [GO:0005737]; HULC complex [GO:0033503]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; replication fork [GO:0005657]; XY body [GO:0001741]

ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase binding [GO:0031625]

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

IPR000608;IPR023313;IPR016135;

3.10.110.10;

A0A3Q2I8A3

MADPAAGPAPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIEREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGGEGSEELRQKFERAKISQGTKTPEEKTTNTISKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVNSEFLKPEVKS

Equus caballus (Horse)

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|PIRNR:PIRNR000550};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000550-4}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000256|PIRSR:PIRSR000550-4};

Adaptive immunity;ATP-binding;Calcium;Cytoplasm;Immunity;Kinase;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger

adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; calcium ion transport [GO:0006816]; cellular response to carbohydrate stimulus [GO:0071322]; intracellular calcium ion homeostasis [GO:0006874]; intracellular signal transduction [GO:0035556]; negative regulation of glucose transmembrane transport [GO:0010829]; phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway [GO:0007207]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of insulin secretion [GO:0032024]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; post-translational protein modification [GO:0043687]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of synaptic vesicle exocytosis [GO:2000300]; regulation of transcription by RNA polymerase II [GO:0006357]

calyx of Held [GO:0044305]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]; spectrin [GO:0008091]

ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; 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]; zinc ion binding [GO:0008270]

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

IPR000961;IPR046349;IPR000008;IPR035892;IPR034664;IPR020454;IPR011009;IPR002219;IPR017892;IPR000719;IPR017441;IPR014375;IPR008271;

3.30.60.20;2.60.40.150;1.10.510.10;

A0A3Q2I8D1

MRLGPAQGCWNPLKKCVVNSPYIIQKKKSSMEDPRGINGQSVRTSQTSSDVAVSSSCRSMEMQDLTSPHSRLSAGGESPSGPKLDNSHINSNSMTPNGTEVKTEPMSSSEIVSTTADGSLDNFSGSAIGSSSFSPRPTHQFSPPQIYPSNRPYPHILPTPSSQTMAAYGQTQFTTGMQQATAYAAYPQPGQPYGISSYGALWAGIKTEGGLSQSQSPGQTGFLSYGTSFGTPQPGQAPYSYQMQGSSFTTSSGLYTGNNSLTNSSGFNSSQQDYPSYPSFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGITSQAVTDPAAEYSTIHSPATPIKDSDSDRLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALTLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRISSHSDLMALHHALELEYL

Equus caballus (Horse)

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|RuleBase:RU362036};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR628472-2, ECO:0000256|RuleBase:RU362036}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR628472-2, ECO:0000256|RuleBase:RU362036};

Activator;Hydrolase;Magnesium;Metal-binding;Nucleus;Protein phosphatase;Reference proteome;Transcription;Transcription regulation

aorta morphogenesis [GO:0035909]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell differentiation [GO:0030154]; cochlea morphogenesis [GO:0090103]; double-strand break repair [GO:0006302]; embryonic skeletal system morphogenesis [GO:0048704]; epithelial cell proliferation [GO:0050673]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; mesodermal cell fate specification [GO:0007501]; metanephros development [GO:0001656]; middle ear morphogenesis [GO:0042474]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; neuron fate specification [GO:0048665]; otic vesicle morphogenesis [GO:0071600]; outer ear morphogenesis [GO:0042473]; outflow tract morphogenesis [GO:0003151]; pattern specification process [GO:0007389]; pharyngeal system development [GO:0060037]; positive regulation of DNA repair [GO:0045739]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of secondary heart field cardioblast proliferation [GO:0072513]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein sumoylation [GO:0016925]; regulation of neuron differentiation [GO:0045664]; response to ionizing radiation [GO:0010212]; semicircular canal morphogenesis [GO:0048752]; striated muscle tissue development [GO:0014706]

cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]

histone H2AXY142 phosphatase activity [GO:0140793]; metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]; RNA binding [GO:0003723]

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

IPR006545;IPR042577;IPR038102;IPR028472;

3.40.50.12350;

A0A3Q2I9Y2

MPATALLDKQVHTSASSIPTSKPRPPKRNVLHLVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWLHSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFMVPIREIGTHKPLPGITVGDIGPKFGYDEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPVSNKLTYGTMVFVRSFLVGEAARSLSKACTIAIRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYLRINEGIGQGDLSELPELHALTAGLKAFTSWTSNAAIEACRMACGGHGYSHCSGLPNIYVTFTATCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPSVVDINSPDSLTEAYKLRAARLVEIAAKNLQTEVFHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFAEKLLKIQDKSVQAVLRNLCLLYSLYGISQNAGDFLQGSIMTESQITQVHQRVKELLTAIRPDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKKSPLNKTEVHDSYYKHLKPLQSKL

Equus caballus (Horse)

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;

A0A3Q2ID61

MSGAAEKQGSTPSALFLSPPAPAPKNGSSSDSSVGEKLGSVGTDAGTGRTEEYRRRRHTMDKDSRGAAATTTTTEHRFFRRSVICDSNATALELPGLPLPLPPPSVAAPVPQSAPPEPHREETSTAAAAAPGAQEPPAAAGPGEPPAAAPVAAPAPSGTSRDRPGAQPSHEGSKEEPPPARSGSGGASAKEPQEERSQQQDDIEELETKAVGMSNDGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLTKSERQRFKEEAEMLKGLQHPNIVRFYDSWESTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYSIKDLLNHAFFQEETGVRVELAEEDDGEKIAIKLWLRIEDIKKLKGKYKDNEAIEFSFDLERDVPEDVAQEMVESGYVCEGDHKTMAKAIKDRVSLIKRKREQRQLVREEQEKRKQEESSLKQQVEQQSSASQAGIKQLPSASTSVPAASTTSASVSTQVEPEEPEADQHQQLQYQQPSISVLSDGTIDSGQGSSVFTESRVSSQQTVSYGSQHEQAHSTGTLPGHTASVVQAQSQPHGVYPPSSMVRPSNDYRMLHPQSMAHPCGGTPTYPESQIFFPTIHERPVSFSPPPTCPPKVAISQRRKSTSFLEAQTHHFQPLLRTVGQNLLPPGGSSTNWTPEAIVMLGTTANRITGEPCEIQVHPMFEPTQVYSDYRPGLVLSEEAHYFIPQEAVYLAGAHYQTQVAEQYEGIPYNSPVLSSHMKQIPEQKPVQGGPTSSSVFEFPSGQAFLVGHLQNLRLDSGLSPGSPLSSISAPISTDATRLKFHPIFVPHSAPAVLTHNNESRSNCVFEFHVHTPSSSSGEGGVLPQRVYRNLQVAVDLNQEEPPPQSVGLHGGLQPVTEEQHNYHAPELTVSVVEPIGQNWPIGSPEYSSDSSQITSSDPSDFQSPPPTGGAAAPFGSDVSLPYIRLPQTVLQESPLFFCFPQGTTSQQVLSASVSSGGSALHPQAQGQSQGQPSSSSLTGIPSSQPIQHSQQQQGIQQTAPPQQTVQYSLPQTSTSSETTTAQPVSQPQAPQVLPQVSAGKQLPVSQPVPTVQGEPHIPVATQPSVVPVHSGAHFLPMGQPLPTSLLPQYPVSQIPISTPHVSAAQTGFSSLPITMAAGINQPLLTLASSATAATIPGGSTVVPSQLPTLLQPVTQLPSQVHPQLLQPAVQSMGIPANLGQAAEVPLPSGDVLYQGFPPRLPPQYPGDSNIAPSSSVASVCIPSTVLSPPMPTEALATPGYFPTVVQPYVESNILVPVGSIGGQVQVSQPAVSLAQALPTSSQQAALESTQGVAQVAPPEPIPVAQPQPTQPTTLVSSIDSAHSDVASGMSDGNENVPSSSGRHEGRTTKRHYRKSVRSRSRHEKTSRPKLRILNVSNKGDRVVECQLETHNRKMVTFKFDLDGDNPEEIATIMVNNDFILAIERESFVDQVREIIEKADEMLSEDVSVEPEGEQGLESLQGKDDYGFSGSQKLEGEFKQPIPSSSMPQQIGIPTSSLTQVVHSAGRRFIVSPVPESRLRESKVFTSETSDTVAASTSHGTGMNLSHSASSLSLQQAFSELRHTQMTEGPSTAPPNFSHTGPTFPVVPPSMTSIAGVPTTAAATPSVSVSATSCPLNDISTSVIQSEITVPTEKGIAGVATCTGVITSSGLPVPPASESPVLSSVVSSITIPAVVSISTTSQSVQAPTSGSIVSSIGTLPSVPVSTTSASTVGSAAAPGAKPPPVLSQQAAGSTTGIATLTSVSTTTPFPSIASQPAFQLSSSTSAPTLAETVVISAHSLDKTSHSSATGLALSLSASSSSPGAGVSSSISQPSGVHPLVIQSAVASTPVLPQAAGPTSTPLLPQVPSIPPLVQPVASVPAVQQTLIHSQPQPALLPNQPHTHCPEIDADTQPKAPGIDDIKTLEEKLRSLFSEHSSSGAQHASVSLETSLVVETTVTPGIPTTAVAPSKLMTSTTSTCLPPTSLPLGTTGLSVIPVVTPGQVSTPVSYVSAPVSSTPGVKPGTTPSKPSLTKAPVLPVGTELPAGTLPSDQLPPFPGPSLTQQPLEDLDAQLRRTLSPETVAVTSAVGPVSVVAPTAVTEAAAQPQKDVSQVTEGPVLATTSGTGVFKMGRFQVSVAMDDAQKEGQSKSEDAKSVHFESSTSESSVLSSSSPESTLVKPEPNSVTIHGISSDVPDSAHKTPLLAAKSETGQSTKVGRFQVTTTANKVGRFSVSRTEDKIAEAKKEGPMASPPFMDLEQATLPAVIPKKEKPELSEPSHLNGPSSDLEAAFLSRDVDDGSGSPHSPHQLSSKSLPVQNLSQSLSNSFNSSYMSSDNESDIEDEDLKLELRRLREKHLKEIQDLQSRQKHEIESLYTKLGKVPPAVIIPPAAPLSGRRRRPTKSKGSKSSRSSSLGNKSPQLSGNLSGQSSASVLHPQQTLHPPGHMPESGQNQLLQPLKPSPSSDNLYSAFTSDGAISVPSLSAPGQGTSSTNTVGGTVNSQAAQAQPPAMTSSRKGTFTDDLHKLVDNWARDAMNLSGRRGSKGHMNYEGPGMARKFSAPGQLCISMTSNLGGSAPISAASATSLGHFTKSMCPPQQYGFPAPPFGTQWSGTGGPAPQPLGQFQPVGTASLQNFNISNLQKSISNPPGSNLRTT

Equus caballus (Horse)

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;

A0A3Q2KTJ6

MVNYFLFSSRCSHSGGEERLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPHHAEWEKAGEVSRELWEKAGKQGLLGVNVAERHGGVGGDVYAAAVVWEEQAYSNCTGPGFSLHSNIVMPYIANYGSEEQIKHFIPQMTAGRCIGAIAMTEPGAGSDLQGVRTNARKDGSDWILNGSKVFITNGWLSDVVIVVAVTDREARSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDVRLPASALLGEENKGFYYLMRELPQERLLIADLGISASEFMFEETRTYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDSCLQLHEAGRLDSATASMAKYWTSELQNSVAYDCVQLHGGWGYMWEFPIAKAYVDARVQPIYGGTNEIMKELIAREIVSDKHSCFCSPVLSLCC

Equus caballus (Horse)

1.3.8.8

CATALYTIC ACTIVITY: Reaction=(5Z)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:84650, ChEBI:CHEBI:87701; Evidence={ECO:0000256|ARBA:ARBA00000392}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47449; Evidence={ECO:0000256|ARBA:ARBA00000392}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553; Evidence={ECO:0000256|ARBA:ARBA00000571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301; Evidence={ECO:0000256|ARBA:ARBA00000571}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; Evidence={ECO:0000256|ARBA:ARBA00001337}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; Evidence={ECO:0000256|ARBA:ARBA00001337}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; Evidence={ECO:0000256|ARBA:ARBA00001483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465; Evidence={ECO:0000256|ARBA:ARBA00001483}; CATALYTIC ACTIVITY: Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:71412; Evidence={ECO:0000256|ARBA:ARBA00000364}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241; Evidence={ECO:0000256|ARBA:ARBA00000364}; CATALYTIC ACTIVITY: Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62242; Evidence={ECO:0000256|ARBA:ARBA00001547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181; Evidence={ECO:0000256|ARBA:ARBA00001547}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence={ECO:0000256|ARBA:ARBA00001765}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233; Evidence={ECO:0000256|ARBA:ARBA00001765}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405; Evidence={ECO:0000256|ARBA:ARBA00001236}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; Evidence={ECO:0000256|ARBA:ARBA00001236}; CATALYTIC ACTIVITY: Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721, ChEBI:CHEBI:83727; EC=1.3.8.8; Evidence={ECO:0000256|ARBA:ARBA00001740}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722; Evidence={ECO:0000256|ARBA:ARBA00001740}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence={ECO:0000256|ARBA:ARBA00000121}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177; Evidence={ECO:0000256|ARBA:ARBA00000121}; CATALYTIC ACTIVITY: Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65059, ChEBI:CHEBI:74692; Evidence={ECO:0000256|ARBA:ARBA00000286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229; Evidence={ECO:0000256|ARBA:ARBA00000286}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; Evidence={ECO:0000256|ARBA:ARBA00001486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297; Evidence={ECO:0000256|ARBA:ARBA00001486}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; Evidence={ECO:0000256|ARBA:ARBA00000733}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; Evidence={ECO:0000256|ARBA:ARBA00000733};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|RuleBase:RU362125};

PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000256|ARBA:ARBA00005198}.

Acetylation;FAD;Flavoprotein;Oxidoreductase;Proteomics identification;Reference proteome;Transit peptide

carnitine metabolic process, CoA-linked [GO:0019254]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; leucine catabolic process [GO:0006552]; long-chain fatty acid catabolic process [GO:0042758]

cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]

flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; palmitoyl-CoA oxidase activity [GO:0016401]

SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.

IPR006089;IPR006091;IPR046373;IPR036250;IPR009075;IPR013786;IPR037069;IPR009100;IPR034179;

1.10.540.10;2.40.110.10;1.20.140.10;

A0A3Q2KTV4

MAEVVSPVPGAGRREPGEVGRARGPPVADPGAALSPQGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVTLDLSLQPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPTSVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW

Equus caballus (Horse)

2.3.1.48

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000256|RuleBase:RU361211};

Acetylation;Acyltransferase;DNA damage;DNA repair;Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase;Zinc;Zinc-finger

apoptotic process [GO:0006915]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucose starvation [GO:0042149]; cellular response to glucose stimulus [GO:0071333]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair via homologous recombination [GO:0000724]; establishment of mitotic spindle orientation [GO:0000132]; lipid droplet disassembly [GO:1905691]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube development [GO:0021915]; neurogenesis [GO:0022008]; nucleotide-excision repair [GO:0006289]; positive regulation of aggrephagy [GO:1905337]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of mitotic sister chromatid segregation [GO:0062033]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of protein acetylation [GO:1901985]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of triglyceride biosynthetic process [GO:0010867]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of hematopoietic stem cell differentiation [GO:1902036]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ionizing radiation [GO:0010212]; sperm DNA condensation [GO:0035092]

cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic spindle pole [GO:0097431]; MSL complex [GO:0072487]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleolus [GO:0005730]; nucleosome [GO:0000786]; nucleus [GO:0005634]; piccolo histone acetyltransferase complex [GO:0032777]; site of double-strand break [GO:0035861]; Swr1 complex [GO:0000812]; transcription regulator complex [GO:0005667]

chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; histone H2AK5 acetyltransferase activity [GO:0043999]; histone H4K16 acetyltransferase activity [GO:0046972]; peptide butyryltransferase activity [GO:0140065]; peptide crotonyltransferase activity [GO:0140064]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.

IPR016181;IPR016197;IPR000953;IPR002717;IPR025995;IPR036388;IPR040706;

2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10;

A0A3Q2KVK7

MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTPEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRSMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY

Equus caballus (Horse)

CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; Evidence={ECO:0000256|ARBA:ARBA00035887};

ATP-binding;Ion transport;Membrane;Metal-binding;Nucleotide-binding;Potassium;Potassium transport;Reference proteome;Sodium;Sodium transport;Translocase;Transmembrane;Transmembrane helix;Transport

adult locomotory behavior [GO:0008344]; amygdala development [GO:0021764]; ATP metabolic process [GO:0046034]; behavioral fear response [GO:0001662]; cellular response to steroid hormone stimulus [GO:0071383]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; L-ascorbic acid metabolic process [GO:0019852]; locomotion [GO:0040011]; locomotory exploration behavior [GO:0035641]; membrane depolarization [GO:0051899]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; negative regulation of heart contraction [GO:0045822]; negative regulation of striated muscle contraction [GO:0045988]; neuronal action potential propagation [GO:0019227]; neurotransmitter uptake [GO:0001504]; olfactory cortex development [GO:0021989]; potassium ion import across plasma membrane [GO:1990573]; proton transmembrane transport [GO:1902600]; regulation of blood pressure [GO:0008217]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of smooth muscle contraction [GO:0006940]; regulation of the force of heart contraction [GO:0002026]; regulation of vasoconstriction [GO:0019229]; response to auditory stimulus [GO:0010996]; response to glycoside [GO:1903416]; response to potassium ion [GO:0035864]; sodium ion export across plasma membrane [GO:0036376]; visual learning [GO:0008542]

cell projection [GO:0042995]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; neuronal cell body [GO:0043025]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; potassium ion binding [GO:0030955]; protein-folding chaperone binding [GO:0051087]; sodium ion binding [GO:0031402]; steroid hormone binding [GO:1990239]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR006068;IPR004014;IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR005775;IPR001757;IPR044492;

3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;

A0A3Q2KXA7

MASSDTHPQSGPRPVHIPFPAYLAWTSPLVLVAGSGVCRPDGHGAGPRGALPSSPAGPGARLPPRGARPRPRSFGLCIPLRQSRKCRERAAADQSHPVGWRRRSYFQGCAFCCQGKDQPIKAIKQDKLFSTNKRRPRSMSGHRSARKRCGDSHPESPVGFGHMSSPGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVPSWIAPNLITIIGLSINICTTVLLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIFDVTESQIIIIICQLLTGTLGPWFWNFTIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH

Equus caballus (Horse)

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;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;

A0A3Q2L095

MCPGVFFCLLVLLFSLGRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKASHKETSQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFMDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENSEEDEMDSGTMVRAAGDEMGTVRVASTMSDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKVPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF

Equus caballus (Horse)

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;Phosphoprotein;Reference proteome;Signal;Transferase

branching involved in blood vessel morphogenesis [GO:0001569]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation involved in embryonic placenta development [GO:0060706]; cell morphogenesis [GO:0000902]; 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]; keratinocyte differentiation [GO:0030216]; 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]; 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 hepatocyte apoptotic process [GO:1903945]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of substrate-dependent cell migration, cell attachment to substrate [GO:1904237]; primitive hemopoiesis [GO:0060215]; protein import into nucleus [GO:0006606]; 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]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]

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

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

1.10.287.4270;4.10.170.10;1.10.510.10;

A0A3Q2L2I2

MMIISLQSYRSYKTSRDGVNWDLSEAVPRLPGETHVADKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRHAFPLAHSLPIFAFLNEEKFNVDGWMVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPSLLVVPYRASDEDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYLDVIRETNRQISKLTIYDARPNVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLITILDHLYSCRFGTFLYNCESARERQKVTERTVSLWSLINSNKDRFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYLELLALRDEYIKRLEELQLANSAKLSDPSTSPSSPSQMMPHVQTHF

Equus caballus (Horse)

3.1.3.64; 3.1.3.95

CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994, ChEBI:CHEBI:84968; Evidence={ECO:0000256|ARBA:ARBA00023672}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; Evidence={ECO:0000256|ARBA:ARBA00023732}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911, ChEBI:CHEBI:85342; Evidence={ECO:0000256|ARBA:ARBA00023712}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57923; EC=3.1.3.95; Evidence={ECO:0000256|ARBA:ARBA00001669}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000256|ARBA:ARBA00001291};

Cell membrane;Endosome;Hydrolase;Lipid metabolism;Membrane;Protein phosphatase;Reference proteome

mitochondrion distribution [GO:0048311]; mitochondrion organization [GO:0007005]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of autophagosome assembly [GO:1902902]; phosphatidylinositol dephosphorylation [GO:0046856]

cytoplasm [GO:0005737]; filopodium [GO:0030175]; late endosome [GO:0005770]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; sarcomere [GO:0030017]

phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoprotein phosphatase activity [GO:0004721]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.

IPR004182;IPR010569;IPR030564;IPR011993;IPR029021;IPR016130;IPR003595;IPR000387;

2.30.29.30;

A0A3Q2L420

MSEAGGAGPGGGGAGAGLGALPAQPPAPPQGSPGAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPSKEQQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTKVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSNSSSLEQPNGGSTSPSCKASSGLEANPGEKRKMNDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPKDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK

Equus caballus (Horse)

2.3.1.48

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000256|ARBA:ARBA00024456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000256|ARBA:ARBA00024456}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000256|PIRNR:PIRNR003048};

Acyltransferase;Bromodomain;Cytoplasm;Cytoskeleton;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase

cellular response to insulin stimulus [GO:0032869]; chromatin remodeling [GO:0006338]; gluconeogenesis [GO:0006094]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of centriole replication [GO:0046600]; negative regulation of rRNA processing [GO:2000233]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of glycolytic process [GO:0045821]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]

A band [GO:0031672]; actomyosin [GO:0042641]; ATAC complex [GO:0140672]; centrosome [GO:0005813]; cytosol [GO:0005829]; I band [GO:0031674]; kinetochore [GO:0000776]; nucleoplasm [GO:0005654]

chromatin binding [GO:0003682]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K9 acetyltransferase activity [GO:0043992]; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0004468]; protein kinase binding [GO:0019901]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription coactivator activity [GO:0003713]

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003048}.

IPR016181;IPR001487;IPR036427;IPR018359;IPR037800;IPR016376;IPR000182;IPR009464;

3.40.630.30;1.20.920.10;

A0A3Q2LA46

MISPFLVLAIGTCLTNSLVPEKEKDPKYWRAQAQQTLQNALRLQKLNTNVAKNIIMFLGDGMGVSTVTAARILKGQLHNSPGEESRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQRTQCNTTQGNEVTSILHWAKEAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPSEALSQGCKDIAYQLVHNIKDIEVIMGGGRKYMFPKNRTDVEYEMDEKARGTRLDGLNLIDIWKSFKPRHKHSHYIWNRTELLTLDPYTVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVEMAIKILSKNPEGFFLLVEGGRIDHGHHEGKAKQALHEVVEMDRAIGQAGDMTSQEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDKKPFTAILYGNGPGYKVVGAHNNYQAQSAVPLRHETHGGEDVAVFAKGPMAHLLHGVHEQNYIPHVMAYAACIGANRDHCASASLAGSPSPGPLLLLLALLPLGILF

Equus caballus (Horse)

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;Reference proteome;Signal;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;

A0A3Q2TTB3

MKRKWEERVKKVEELASYYERNPLPTVYKPRLSKPLQPSRVWKIFCRQADAFRFVKTCKEDVHVFALERNTQNGQRFYLVTTYQELWYYYTKGYKTSLMHCYEVIPEKDACKLYFDLEFYKAANPGADGKDMVAKLIELVSQKLKELYDVNCSARDVLNLDSSTDEKFSRHLIFLPCKTVFKDNIHVGNFVRTILQPAIRLVGSNVAAPIAEGGAGYTSQCSAPTVELDGPLTNLTAVEDASKGWPAIADQRKETETSHHGENSEFSFLIVNNKEGDKQLFVDLGVYTRNRNFRMYKSSKAGKNVILTIAEDNKFVPNCEENVSLEEAYFLSSLVCNVRFEDGTKILSSNFVEEEIKMSAFLRSKTTRSTREPMEGYQESPYPEIDCFVRSLINKDGVQGGIRQWNYFSGEEILVYDISGYRWCENIGRAHRSNNIMILVDLKKEVWYQKCHDPVCREKNFKSQSLPLPSRICLSSLFIEEEDHMVTDERENTEVTSHSNPADLSESSAYLAINTSQDTQWDNASDDAYLVETAEDVELAEAADYSLGYDTEEIPDEVLLEMSWKQDTCSKDDS

Gallus gallus (Chicken)

FUNCTION: DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them (PubMed:26626482, PubMed:30478192). Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions (PubMed:26694751, PubMed:27230014). Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (By similarity). Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as UV lesions, R-loops and G-quadruplexes, to allow DNA replication to continue (PubMed:26694751, PubMed:27230014, PubMed:26626482). Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion. Repriming avoids fork degradation while leading to accumulation of internal ssDNA gaps behind the forks (By similarity). Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase (By similarity). Also required for reinitiating stalled forks after ultraviolet (UV) damage during nuclear DNA replication (By similarity). Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides (By similarity). In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (By similarity). {ECO:0000250|UniProtKB:Q96LW4, ECO:0000269|PubMed:26626482, ECO:0000269|PubMed:26694751, ECO:0000269|PubMed:27230014, ECO:0000269|PubMed:30478192}.

2.7.7.102; 2.7.7.7

CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.102; Evidence={ECO:0000269|PubMed:30478192}; 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:0000250|UniProtKB:Q96LW4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22509; Evidence={ECO:0000250|UniProtKB:Q96LW4};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96LW4}; Note=Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo. {ECO:0000250|UniProtKB:Q96LW4};

Alternative splicing;Chromosome;Coiled coil;DNA damage;DNA repair;DNA-directed DNA polymerase;DNA-directed RNA polymerase;Manganese;Metal-binding;Mitochondrion;Nucleotidyltransferase;Nucleus;Reference proteome;Transcription;Transferase;Zinc

error-prone translesion synthesis [GO:0042276]; mitochondrial DNA repair [GO:0043504]; mitochondrial DNA replication [GO:0006264]; R-loop processing [GO:0062176]; replication fork processing [GO:0031297]; response to UV [GO:0009411]; translesion synthesis [GO:0019985]

DNA-directed RNA polymerase complex [GO:0000428]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]; replication fork [GO:0005657]

chromatin binding [GO:0003682]; DNA primase activity [GO:0003896]; DNA-directed DNA polymerase activity [GO:0003887]; manganese ion binding [GO:0030145]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LW4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q96LW4}. Chromosome {ECO:0000250|UniProtKB:Q96LW4}.

DOMAIN: The zinc knuckle motif binds zinc and is required for the DNA primase activity. It facilitates the binding and selection of the 5'-nucleotide of the newly synthesized primer and the recognition of preferred initiation sites. {ECO:0000250|UniProtKB:Q96LW4}.; DOMAIN: The presence of an Asp-Aaa-Glu (DxE) motif in the metal-binding active site favors the use of Mn(2+) ions to achieve optimal incoming nucleotide stabilization, especially required during primer synthesis. Glu-118 is required to stabilize the incoming nucleotide at the 3'-site. {ECO:0000250|UniProtKB:Q96LW4}.

IPR044917;

A0A3Q2U639

MGCVQCKDKEATKLTDERDGSLTQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHATGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMEKADGLCFNLTVIATNNTPQTVGLAKDAWEVARDSLFLEQKLGQGCFAEVWRGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGDNL

Gallus gallus (Chicken)

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};

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

ATP-binding;Kinase;Lipoprotein;Nucleotide-binding;Palmitate;Reference proteome;SH3 domain;Transferase;Tyrosine-protein kinase

activated T cell proliferation [GO:0050798]; cell differentiation [GO:0030154]; cellular response to amyloid-beta [GO:1904646]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to transforming growth factor beta stimulus [GO:0071560]; dendrite morphogenesis [GO:0048813]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; forebrain development [GO:0030900]; gene expression [GO:0010467]; heart process [GO:0003015]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of dendritic spine maintenance [GO:1902951]; negative regulation of gene expression [GO:0010629]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein ubiquitination [GO:0031397]; neuron migration [GO:0001764]; phosphorylation [GO:0016310]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; protein catabolic process [GO:0030163]; protein ubiquitination [GO:0016567]; regulation of calcium ion import across plasma membrane [GO:1905664]; regulation of cell shape [GO:0008360]; regulation of glutamate receptor signaling pathway [GO:1900449]; response to ethanol [GO:0045471]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

actin filament [GO:0005884]; cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glial cell projection [GO:0097386]; membrane raft [GO:0045121]; postsynaptic density [GO:0014069]; Schaffer collateral - CA1 synapse [GO:0098685]

alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; disordered domain specific binding [GO:0097718]; ephrin receptor binding [GO:0046875]; G protein-coupled receptor binding [GO:0001664]; growth factor receptor binding [GO:0070851]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; scaffold protein binding [GO:0097110]; signaling receptor binding [GO:0005102]; tau protein binding [GO:0048156]; transmembrane transporter binding [GO:0044325]

IPR047924;IPR035750;IPR011009;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;

3.30.505.10;2.30.30.40;1.10.510.10;

A0A3Q2U7N5

MPRAEGGTAAPIGQLLEQLRGDWPAATSVRPLAIASGGGLSPPAMAGGCGRRRVVVCAVALGLSAAVLALTAVVLLRAYVLRSPAIPRLWARRGSTAAFSASERRELKEALRGAVRIPTVSLSSEDFNTTAMAEFGDYIRKAFPAVFSSKFIQHEIIGEYSHLFTVQGSDSEMMPYMLLAHMDVVPAPPEGWDFPPFSAAEHEGFIYGRGTLDNKNSAIGILQALEFLLRRNYRPRRSFYVGIGHDEEVFGQKGALKIAALLESRGVKLSFLLDEGSAILDGIIAGVKKPVALIAVTEKGLMTLNFTVEKEPGHSSFPPKETSIGILATAVSRLEQNPMRSLFGHGPELMTMEHLASEFNFPLNLIMSNLWLFSPIVSRVLAWKPSTNALIRTTTAVTMFNAGIKFNVIPPSARATVNFRIHSGEKAKEVLETVRNTVADDRVKIDVIEALDPLPISPWDDQTFGVHVFQRTILDTFPNVDSVVPGTCIGNTDSRHFTNVTNAIYRFNPVLLKSDDLPRIHGLNERISVESYEKQVEFLFQLIKNCDVDKLPEPHANSHELKAQGTL

Gallus gallus (Chicken)

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;Reference proteome;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;

1.10.150.900;3.30.70.360;3.40.630.10;

A0A3Q2UHM4

MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDGRKTAGDENDPATWKNPRHLSKEIDAEEWGKFLHTKNKIYTDFDEIRQEIENETERISGNNKGISPEPIHLKIFSSNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILQFISNPNSIILAVTAANTDMATSEALKIAREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVADSIRDEYGFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVEDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRRRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSSVPRDKSTKAPGALPPASQETVTAASAEADGKAAAGAGDVTQESGTGNWRGMLKSSKAEEVSAEEKSKPAAALPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSLLLDDLLTESEDMAQRRKEAADMLKALQRASQIIAEIRETHLW

Gallus gallus (Chicken)

3.6.5.5

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=3.6.5.5; Evidence={ECO:0000256|ARBA:ARBA00001837};

Biological rhythms;Coated pit;Cytoplasmic vesicle;Golgi apparatus;GTP-binding;Lipid-binding;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Peroxisome;Proteomics identification;Reference proteome;Synapse

calcium ion transport [GO:0006816]; endocytosis [GO:0006897]; heart contraction [GO:0060047]; intracellular distribution of mitochondria [GO:0048312]; membrane fusion [GO:0061025]; mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial membrane fission [GO:0090149]; mitocytosis [GO:0160040]; necroptotic process [GO:0070266]; peroxisome fission [GO:0016559]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of protein secretion [GO:0050714]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; protein complex oligomerization [GO:0051259]; protein localization to mitochondrion [GO:0070585]; regulation of ATP metabolic process [GO:1903578]; regulation of gene expression [GO:0010468]; regulation of mitophagy [GO:1901524]; regulation of peroxisome organization [GO:1900063]; release of cytochrome c from mitochondria [GO:0001836]; rhythmic process [GO:0048511]

brush border [GO:0005903]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; mitochondrion-derived vesicle [GO:0099073]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]; synaptic vesicle membrane [GO:0030672]

GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267]; ubiquitin protein ligase binding [GO:0031625]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004432}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004450}. Peroxisome {ECO:0000256|ARBA:ARBA00004275}.

IPR022812;IPR001401;IPR019762;IPR045063;IPR000375;IPR030381;IPR003130;IPR020850;IPR027417;

1.20.120.1240;3.40.50.300;

A0A3Q2UKD3

MDPLAPLVLYGFSLIISGKVEAALDLILINSFPLVGNSETSLICITSKWRSRESITIDRDQEDVTNQHREPLEVSEDSKRATAKMVIWKREKASETIGAYYCEGKLKDEVTRIHTMKMPRGASFHPVALTVTANKGEHVNISFIRMAAKEEDAVIYKNGSFIHSVPRHEVPGELEVSYPHVQLQDAGVYSARYIGGNLFTSAYTRLIVRRCEAQKWGPSCSSHCPSCMNNGICHEDTGECICPPGFMGKTCEKACGANTFGKTCEESCKENYGCKNYMFCLPDPYGCSCATGWMGLECDKECKPGYYGSDCKLKCNCHNRGTCDRYKGCVCSYGWHGLQCEKEGSADLSPQIENLLDPVELNSGVEFKPYCIASGMPLPKSEEFKLLKQDGTVLRPSLIVTSNRSEAMFTINRVLPRDTGTWVCSVQTVAGMAEKPFQVTVKVPPVPQYAPRLTNSGHNFLIIDINAELHTGDGPVVSTKLLYKPAKRYQSWMSVEVKGSTKRLDNLEPKTEYQFCVQLSRQGEGGEGHPGPQASFTTAALGLPPPEGLTLLPKSMTSLNLSWHPLTLRTDDDIRVEVERKSVNDNGDESSVITQVPGNMSTLIIKDLEPRQQYMCRVRVNTRSQGEWSNYLYAWTFSDRIPPAPYNIKFFNTTDTSSVISWTTAEGHSISSIIISYKIYGKAEYNHIDIIIKNSTITQYHLKGLEPNTVYQVQINAQNNIGLSNPNTSFELKTLPEMKAPYESKGGKMLLIAILGSAGMTCVTILLAFLIMLQLKRANFQRRMAQAFQNVVREEPAVQFNSGTLTLSRKAKNSPDPTIYPVLEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDCSAEEAA

Gallus gallus (Chicken)

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;EGF-like domain;Glycoprotein;Immunoglobulin domain;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Receptor;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

angiogenesis [GO:0001525]; endothelial cell proliferation [GO:0001935]; negative regulation of angiogenesis [GO:0016525]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Rac protein signal transduction [GO:0035022]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of establishment or maintenance of cell polarity [GO:0032878]; sprouting angiogenesis [GO:0002040]; substrate adhesion-dependent cell spreading [GO:0034446]; Tie signaling pathway [GO:0048014]

actin filament [GO:0005884]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; centriolar satellite [GO:0034451]; membrane raft [GO:0045121]; microvillus [GO:0005902]; receptor complex [GO:0043235]; stress fiber [GO:0001725]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; 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}.

IPR000742;IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR011009;IPR000719;IPR017441;IPR001245;IPR018941;IPR008266;IPR020635;

2.60.40.10;2.170.300.10;1.10.510.10;

A0A3Q7GYG2

MASNNNICAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

FUNCTION: Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects (PubMed:22711283). Catalyzes S-adenosylmethionine-dependent regioselective 7/4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates (PubMed:22711283). {ECO:0000269|PubMed:22711283}.

2.1.1.-; 2.1.1.155; 2.1.1.82

CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = H(+) + rhamnetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73116; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=kaempferol + S-adenosyl-L-methionine = H(+) + kaempferide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15105, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58573, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789; EC=2.1.1.155; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15106; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = 7-O-methylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74719, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:194065; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74720; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=kaempferide + S-adenosyl-L-methionine = 7,4'-O-dimethylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74775, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789, ChEBI:CHEBI:194067; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74776; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=isorhamnetin + S-adenosyl-L-methionine = 3',4'-O-dimethylquercetin + 2 H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74723, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055, ChEBI:CHEBI:194064; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74724; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16181, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789, ChEBI:CHEBI:77710; EC=2.1.1.82; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16182; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = 7,4'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74731, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706, ChEBI:CHEBI:194068; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74732; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + syringetin = 7,3',5'-O-trimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:194069; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74736; Evidence={ECO:0000250|UniProtKB:F2YTN5}; CATALYTIC ACTIVITY: Reaction=3',4',5'-O-trimethylmyricetin + S-adenosyl-L-methionine = 7,3',4',5'-O-tetramethylmyricetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74739, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194070, ChEBI:CHEBI:194071; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74740; Evidence={ECO:0000250|UniProtKB:F2YTN5};

PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:22711283}.

Methyltransferase;Reference proteome;S-adenosyl-L-methionine;Transferase

aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259]

O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A3Q7HYF0

MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLRAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGNVHTSYNLTPLSQSLILDKDGTSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRFNGVFNKAMQNVTCIDMKRVLECYNGFEGVKEIIDVGGGLGISLASIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDECCVKILKNCWRALPKDGKVVVIEQMQPEYPEINLISKNSFSVDMLMMTMLDGGKERTKQQFEDLAKQAGFTVFKIVARAYYCWVIELYK

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

FUNCTION: Flavonoid 3-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects (PubMed:25128240). Catalyzes S-adenosylmethionine-dependent regioselective 3-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates (PubMed:22711283, PubMed:25128240). Active with myricetin, quercetin, kaempferol, 4'-methyl kaempferol (kaempferide), 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin), 3',4',5'-trimethyl myricetin, 3'-methyl myricetin (laricitrin) and 3',5'-dimethyl myricetin (syringetin), thus producing 3-methyl myricetin, 3-methyl quercetin, 3-methyl kaempferol, 4',3-methyl kaempferol, 3',3-methyl quercetin, 7,3-dimethyl quercetin, 3',4',5',3-tetramethyl myricetin, 3',3-dimethyl myricetin and 3',5',3-dimethyl myricetin, respectively (PubMed:22711283). Inactive with flavonol substrates methylated at the 3-hydroxyl position such as 3-O-methyl quercetin (PubMed:22711283). {ECO:0000269|PubMed:22711283, ECO:0000269|PubMed:25128240}.

2.1.1.-; 2.1.1.76

CATALYTIC ACTIVITY: Reaction=3',4',5'-O-trimethylmyricetin + S-adenosyl-L-methionine = 3,3',4',5'-O-tetramethylmyricetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74771, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194070, ChEBI:CHEBI:194076; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74772; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=kaempferol + S-adenosyl-L-methionine = 3-O-methylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74743, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58573, ChEBI:CHEBI:59789, ChEBI:CHEBI:194073; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74744; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = 3',4',5,7-tetrahydroxy-3-methoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17673, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789; EC=2.1.1.76; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17674; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = 3-O-methylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74747, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:194072; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74748; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=kaempferide + S-adenosyl-L-methionine = 3,4'-O-dimethylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74755, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789, ChEBI:CHEBI:194074; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74756; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=isorhamnetin + S-adenosyl-L-methionine = 3,3'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74759, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055, ChEBI:CHEBI:194063; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74760; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77710, ChEBI:CHEBI:192706; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74764; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=laricitrin + S-adenosyl-L-methionine = 3,3'-O-dimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74779, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:60006, ChEBI:CHEBI:194066; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74780; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + syringetin = 3,3',5'-O-trimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:194075; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74768; Evidence={ECO:0000269|PubMed:22711283};

PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:25128240}.

Methyltransferase;Reference proteome;S-adenosyl-L-methionine;Transferase

aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259]

3',4',5'-trimethylmyricetin 3-O-methyltransferase activity [GO:0102440]; kaempferol 3-O-methyltransferase activity [GO:0102449]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; quercetin 3-O-methyltransferase activity [GO:0030755]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A3S5YBC7

MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLTWSNIDAITERANVPTVITEFGDGDPTVLKNTLARADERFIGWQYWHFGAGNATDPFLGEVGRQLVRTYPQATAGEPGRMIFDADNGDFAYRFTPRAATRPTEIFVSDLHYPDGYAVQVDGGQVTSAPGARIVTVVADGSGPVTVKINRPGSAGAEVPDGPIETSSSGSSGSS

Rhodococcus hoagii (strain 103S) (Rhodococcus equi)

FUNCTION: Hydrolyzes glycosphingolipids; exhibits broad substrate specificity including monosialodihexosylganglioside (GM3), monosialotetrahexosylganglioside (GM1), fucosyl-GM1, lactosylceramide, globotriosylceramide, globotetraosylceramide, ganglioside GD1a, and ganglioside GD1b (PubMed:28179425). No activity towards glucosylceramide and galactosylceramide (PubMed:28179425). {ECO:0000269|PubMed:28179425}.

3.2.1.123

CATALYTIC ACTIVITY: Reaction=an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:22288, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:136875, ChEBI:CHEBI:156536; EC=3.2.1.123; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22289; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 + H2O = an N-acyl-sphingoid base + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:65540, ChEBI:CHEBI:15377, ChEBI:CHEBI:79210, ChEBI:CHEBI:83273, ChEBI:CHEBI:156068; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65541; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + H2O = an N-acyl-sphingoid base + beta-D-Gal-(1->3)-beta-D-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-D-Gal-(1->4)-D-Glc; Xref=Rhea:RHEA:65544, ChEBI:CHEBI:15377, ChEBI:CHEBI:82639, ChEBI:CHEBI:83273, ChEBI:CHEBI:156537; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65545; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a ganglioside Fuc-GM1 + H2O = alpha-Fuc-(1->2)-beta-Gal-(1->3)-beta-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-Gal-(1->4)-Glc + an N-acyl-sphingoid base; Xref=Rhea:RHEA:65548, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:90189, ChEBI:CHEBI:156538; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65549; Evidence={ECO:0000269|PubMed:28179425}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + lactose; Xref=Rhea:RHEA:65552, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:79208, ChEBI:CHEBI:83273; Evidence={ECO:0000269|PubMed:28179425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65553; Evidence={ECO:0000269|PubMed:28179425};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for monosialotetrahexosylganglioside (GM1) {ECO:0000269|PubMed:28179425}; Note=kcat is 10.5 sec(-1) with monosialotetrahexosylganglioside as substrate. {ECO:0000269|PubMed:28179425};

3D-structure;Disulfide bond;Glycosidase;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Palmitate;Secreted;Signal;Sphingolipid metabolism

galactosylceramide catabolic process [GO:0006683]

extracellular region [GO:0005576]; membrane [GO:0016020]

endoglycosylceramidase activity [GO:0047876]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28179425}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.

IPR041036;IPR001547;IPR013780;IPR017853;

3.20.20.80;2.60.40.1180;

A0A3S5ZP79

MDLAVVLVLCLSCLLLLSLWKQSSGKGKLPPGPTPLPILGNIFQLDVKNISKSLTSLSKVYGPVFTVYFGMKPTVVLHGYEAVKEALIDLGEEFSRRGSFPVIERNVKGHGIVFSNGKTWKETRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNGLPCDPTFILGCAPCNVICSIIFQNRFDYKDQTFLNLMKTINENIKILGSPWIQVLNIFPVLLDFFPWSYSYKKLYTNTAYVKNYVLEKTREHQASLDINNPRDFIDCFLIKMEQEKHNHQSEYTFENLTITVSDLFGAGTETTSTTLRYGLLLLLKHPEVTAKIQEEIDRVIGRHRSPCMQDRTHMPYMDAVLHEIQRYIDLAPMSVPHAVNCDVKFRNYLIPKGTDILTSLTSVLHDDKEFPNPEVFDPGHFLDENGNFRKSDYFMAFSAGKRVCVGEGLARMELFLFLTTILQTFTLKSVVDPKDLDTTPAVTGIANVPPPYQLCFIPV

Bos taurus (Bovine)

FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics. {ECO:0000256|RuleBase:RU368050}.

1.14.13.n7; 1.14.14.1

CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50088, 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:77016, ChEBI:CHEBI:132025; Evidence={ECO:0000256|ARBA:ARBA00000615, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089; Evidence={ECO:0000256|ARBA:ARBA00000615, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50076, 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:78043, ChEBI:CHEBI:132024; Evidence={ECO:0000256|ARBA:ARBA00001354, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077; Evidence={ECO:0000256|ARBA:ARBA00001354, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, 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:58562, ChEBI:CHEBI:76636; Evidence={ECO:0000256|ARBA:ARBA00000326, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence={ECO:0000256|ARBA:ARBA00000326, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 13-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50096, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132031; Evidence={ECO:0000256|ARBA:ARBA00000338, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50097; Evidence={ECO:0000256|ARBA:ARBA00000338, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000256|ARBA:ARBA00000089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000256|ARBA:ARBA00000089}; CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; Evidence={ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76628; Evidence={ECO:0000256|ARBA:ARBA00001427, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752; Evidence={ECO:0000256|ARBA:ARBA00001427, ECO:0000256|RuleBase:RU368050};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU368050};

PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000256|ARBA:ARBA00004872, ECO:0000256|RuleBase:RU368050}.

Endoplasmic reticulum;Fatty acid metabolism;Heme;Iron;Lipid metabolism;Membrane;Metal-binding;Microsome;Mitochondrion;Mitochondrion inner membrane;Monooxygenase;NADP;Oxidoreductase;Reference proteome;Signal

epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805]

cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]

arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368050}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368050}. Microsome membrane {ECO:0000256|RuleBase:RU368050}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368050}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368050}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368050}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.

IPR001128;IPR017972;IPR002401;IPR008070;IPR036396;

1.10.630.10;

A0A3S5ZPK0

MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNVDSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA

Bos taurus (Bovine)

2.4.1.255

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

Glycosyltransferase;Phosphoprotein;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;

A0A3S5ZPN3

MPGYSSDRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLTKKKWNLDELPKFEKNFYQEHPDVVRRTAQEVEQYRSSKEVTVRGHNCPKPIINFYEANFPANVMEVIQRQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYSRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKEYVHINIGALELSANHNILQIVDVCHDVEKDDKLIRLMEEIMSEKENKTIVFVETKRRCDDLTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVNDLISVLREANQAINPKLLQLIEDRGSGRSRGDRRDRYSAGKRGGFSSFRERENFERTYGALGKRDFGAKAQNGAYSTQSFSNGTPFGNGFAAAGMQAGFRAGNPAGAYQNGYDQQYGSNIANMHNGMNQQQYAYPATGAAPMIGYPMPASYSQ

Gallus gallus (Chicken)

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;

A0A3S7WQS5

MDDRSLKLAEDFVSARYIEAGRESLRATARIMRSILAQRCCPDEGLTDAAIELILRQLSLMDTNNLAHHVGGGEREGRVVSALVRMRHFHLTHGIGRSGDLFSEQPKAAGSSLLYKITNVLMLDLIRQAGAPSTAAAVVVPMATGMTLALVLRCVAKTHMKELMKEAEAVQLQRTVTKDSTSATSAAPVQEPPMSEADRDRHDRTSLPVPATPRYVIWPRIDQKTALKCIDAAGLVPVPVQLRPAVPLARSAAPCVSTNRDSLDRGQDSIGSPSTPTSSSSLFLECHVDDVAAAVNAVGGPSQVVCVLSTTSCFAPRLPDNTVAIAQYCKKAGIPYVVNNAYGVQSRRIMTRLDAAQRLGRVDFVVQSGDKNFLVPVGGSIICSGDKERCKAVAALYAGRASMSPIVDLFITALSLGRRGMQTLWSDRYKCRARLIRQLRVFARERREVLLVDDSDDDKADEDTVGGSQRTSNAVVPRNDISVAVTMRAYGLPAAEASSSGAQLGSEQAGRVTNWAAARALGAQLFRSAVTGPRVITPAPSTPTTIAGCTFRNYGMHQDREPPCPLLVIACGIGMSESEVDALMARLRDLWPVPA

Leishmania donovani

FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.

2.9.1.2

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041, Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377, ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551, ChEBI:CHEBI:78573; EC=2.9.1.2; Evidence={ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914};

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|PIRNR:PIRNR017689, ECO:0000255|PIRSR:PIRSR017689-50};

PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2. {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.

Cytoplasm;Protein biosynthesis;Pyridoxal phosphate;RNA-binding;Selenium;Transferase;tRNA-binding

conversion of seryl-tRNAsec to selenocys-tRNAsec [GO:0001717]; selenocysteine incorporation [GO:0001514]

cytoplasm [GO:0005737]

O-phosphoseryl-tRNA(Sec) selenium transferase activity [GO:0098621]; selenotransferase activity [GO:0016785]; tRNA binding [GO:0000049]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.

IPR015424;IPR015421;IPR019872;IPR008829;

3.40.640.10;

A0A452DHX3

MRGARGAWDFLFVLLLLLLVQTGSSQPSVSPGELSLPSIHPAKSELIVSVGDEIRLLCTDPGFVKWTFEILGQLSEKTNPEWITEKAEATNTGNYTCTNKGGLSSSIYVFVRDPEKLFLIDLPLYGKEENDTLVRCPLTDPEVTNYSLTGCEGKPLPKDLTFVADPKAGITIRNVKREYHRLCLHCSANQRGKSMLSKKFTLKVRAAIKAVPVVSVSKTSYLLREGEEFAVTCLIKDVSSSVDSMWIKENSQQTKAQMKKNSWHQGDFSYLRQERLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMMNTTVFVNDGENVDLVVEYEAYPKPVHRQWIYMNRTSTDKWDDYPKSENESNIRYVNELHLTRLKGTEGGTYTFHVSNSDVNSSVTFNVYVNTKPEILTHDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSVPVGPVDVQIQNSSVSPFGKLVVYSTIDDSTFKHNGTVECRAYNDVGKSSASFNFAFKGNSKEQIHAHTLFTPLLIGFVIAAGLMCIFVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEVALYKNLLHSKESSCNDSTNEYMDMKPGVSYVVPTKADKRRSARIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPHRENPAVDHSVRINSVGSSASSTQPLLVHEDV

Bos taurus (Bovine)

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|PIRNR:PIRNR500951};

ATP-binding;Cell membrane;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;Ubl conjugation

actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; digestive tract development [GO:0048565]; ectopic germ cell programmed cell death [GO:0035234]; embryonic hemopoiesis [GO:0035162]; erythrocyte differentiation [GO:0030218]; erythropoietin-mediated signaling pathway [GO:0038162]; Fc receptor signaling pathway [GO:0038093]; glycosphingolipid metabolic process [GO:0006687]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell migration [GO:0035701]; immature B cell differentiation [GO:0002327]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; Kit signaling pathway [GO:0038109]; lamellipodium assembly [GO:0030032]; lymphoid progenitor cell differentiation [GO:0002320]; male gonad development [GO:0008584]; mast cell chemotaxis [GO:0002551]; mast cell degranulation [GO:0043303]; mast cell differentiation [GO:0060374]; mast cell proliferation [GO:0070662]; megakaryocyte development [GO:0035855]; melanocyte adhesion [GO:0097326]; melanocyte differentiation [GO:0030318]; melanocyte migration [GO:0097324]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of developmental process [GO:0051093]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reproductive process [GO:2000242]; ovarian follicle development [GO:0001541]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of dendritic cell cytokine production [GO:0002732]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular associated smooth muscle cell differentiation [GO:1905065]; regulation of cell shape [GO:0008360]; response to radiation [GO:0009314]; spermatid development [GO:0007286]; stem cell differentiation [GO:0048863]; T cell differentiation [GO:0030217]

cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrillar center [GO:0001650]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [GO:0005020]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. 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;IPR003599;IPR003598;IPR013151;IPR011009;IPR000719;IPR017441;IPR027263;IPR001245;IPR008266;IPR020635;IPR001824;

2.60.40.10;1.10.510.10;

A0A452DI66

MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTRGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRCGGAPRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS

Bos taurus (Bovine)

FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. {ECO:0000256|ARBA:ARBA00025390, ECO:0000256|PIRNR:PIRNR001149}.

3.4.21.5

CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5; Evidence={ECO:0000256|ARBA:ARBA00001621, ECO:0000256|PIRNR:PIRNR001149};

Acute phase;Blood coagulation;Disulfide bond;Gamma-carboxyglutamic acid;Hemostasis;Hydrolase;Kringle;Protease;Reference proteome;Serine protease;Signal

acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell surface receptor signaling pathway [GO:0007166]; cytolysis by host of symbiont cells [GO:0051838]; fibrinolysis [GO:0042730]; G protein-coupled receptor signaling pathway [GO:0007186]; ligand-gated ion channel signaling pathway [GO:1990806]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of proteolysis [GO:0045861]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; platelet activation [GO:0030168]; positive regulation of blood coagulation [GO:0030194]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of insulin secretion [GO:0032024]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway [GO:1900738]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; regulation of cytosolic calcium ion concentration [GO:0051480]

collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]

calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; lipopolysaccharide binding [GO:0001530]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]; thrombospondin receptor activity [GO:0070053]

IPR035972;IPR000294;IPR000001;IPR013806;IPR018056;IPR038178;IPR009003;IPR043504;IPR001314;IPR003966;IPR018992;IPR037111;IPR001254;IPR018114;IPR033116;

2.40.20.10;4.10.140.10;2.40.10.10;

A0A452DI94

MGREGAGPRGRSSRAVRDALQGPESVSSTQRPPCTMSRQGISLRFPLLLLLLSPSPVLPADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYYGPNCTIPEIWTWLRTTLRPSPSFVHFLLTHGRWLWDFVNATFIRDKLMRLVLTVRSNLIPSPPTYNVAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMVYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRELRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGDVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPHREDRPGVERPPTEL

Bos taurus (Bovine)

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;Reference proteome

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

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

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;

A0A452DIU3

QPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE

Bos taurus (Bovine)

FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation. {ECO:0000256|RuleBase:RU369032}.

5.3.99.3

CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000256|ARBA:ARBA00000609, ECO:0000256|RuleBase:RU369032};

PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702, ECO:0000256|RuleBase:RU369032}.

Chaperone;Cytoplasm;Fatty acid biosynthesis;Fatty acid metabolism;Isomerase;Lipid biosynthesis;Lipid metabolism;Prostaglandin biosynthesis;Prostaglandin metabolism;Reference proteome

chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated protein complex assembly [GO:0051131]; fibroblast proliferation [GO:0048144]; glucocorticoid receptor signaling pathway [GO:0042921]; glycogen biosynthetic process [GO:0005978]; lung saccule development [GO:0060430]; positive regulation of phosphorylation [GO:0042327]; prostaglandin biosynthetic process [GO:0001516]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; skin development [GO:0043588]; telomerase holoenzyme complex assembly [GO:1905323]; telomere maintenance via telomerase [GO:0007004]

cytosol [GO:0005829]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; telomerase holoenzyme complex [GO:0005697]

DNA polymerase binding [GO:0070182]; Hsp90 protein binding [GO:0051879]; prostaglandin-E synthase activity [GO:0050220]; protein-folding chaperone binding [GO:0051087]; telomerase activity [GO:0003720]; unfolded protein binding [GO:0051082]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369032}.

IPR007052;IPR008978;IPR045250;

2.60.40.790;

A0A452E9Y6

MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLLAKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKLLDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHVTKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN

Capra hircus (Goat)

FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism (PubMed:10894086). Shows antibacterial properties against several Gram-positive bacteria including some Staphylococcus species and Gram-negative bacteria including E.coli, P.aeruginosa and some Salmonella species (PubMed:10894086). Inhibits the growth of several fungi including A.niger, Trichoderma species, C.cassicola, P.meadii and C.salmonicolor (PubMed:10894086). Does not have anti-fungal activity towards C.albicans and Pythium species (PubMed:10894086). May protect the udder from infection and may promote growth in newborns (PubMed:10894086). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity). {ECO:0000250|UniProtKB:P22079, ECO:0000250|UniProtKB:P80025, ECO:0000250|UniProtKB:Q5SW46, ECO:0000269|PubMed:10894086}.

1.11.1.7

CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137; Evidence={ECO:0000250|UniProtKB:P80025}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + thiocyanate = H2O + hypothiocyanous acid; Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417; Evidence={ECO:0000250|UniProtKB:P80025}; CATALYTIC ACTIVITY: Reaction=H2O2 + iodide = H2O + hypoiodite; Xref=Rhea:RHEA:69420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:29232; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421; Evidence={ECO:0000250|UniProtKB:P80025};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304};

3D-structure;Antibiotic;Antimicrobial;Calcium;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Nitration;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Secreted;Signal

antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]; thiocyanate catabolic process [GO:0046265]

basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]

calcium ion binding [GO:0005509]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; peroxidase activity [GO:0004601]; thiocyanate peroxidase activity [GO:0036393]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}.

IPR019791;IPR010255;IPR037120;

1.10.640.10;

A0A453Z0R4

MSGETHHSAAAEENKVRYRRTQSVTRAEEITKKESEQRKSQPDKPCHRPRDSLFSWSSGFDNFTGLVNWGFLLLTMGGIRLVLENFIKYGIRVDPVQWFTVLTGKGEGEGYPSVLLISYSLVPVMICLMMERALASDIIPESAGMAVHIVNIIVLVLIPMVVIHVKGHIFSLVGAMTVCFIYCILFLKLWSYVQVNLWCRAEKKQHRHSRSGRRQSITIAQLQNGREQEAERTANGSATGYCNDKDKVPALVHYPDNLHPVDLFYFLLAPTLCYELNFPKTNRIRKRFLIKRMLEVVIGVHIVMGLFQQWMIPSVRNSLVPFSNMDLTKTAERLLKLAIPNHLMWLCFFYLTFHSFLNLMGELLHFADRNFYSDWWNANNIDTFWRTWNMPVHKWCVRHLYIPVVELGYSKVAASVIVFFFSAFFHEYLVSVPLKTFKVWAFTGMMAQIPLSFVAKYMETNYGPRWGNMLVWASIILGQPLAIMMYYHDFVITNYNDVLV

Anopheles gambiae (African malaria mosquito)

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:ARBA00000645}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38380; Evidence={ECO:0000256|ARBA:ARBA00000645}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000256|ARBA:ARBA00000389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; Evidence={ECO:0000256|ARBA:ARBA00000389}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75735; Evidence={ECO:0000256|ARBA:ARBA00000883}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436; Evidence={ECO:0000256|ARBA:ARBA00000883}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75342; Evidence={ECO:0000256|ARBA:ARBA00001009}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916; Evidence={ECO:0000256|ARBA:ARBA00001009}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:197429; Evidence={ECO:0000256|ARBA:ARBA00043738}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; Evidence={ECO:0000256|ARBA:ARBA00043738}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:138735, ChEBI:CHEBI:197429; Evidence={ECO:0000256|ARBA:ARBA00043821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345; Evidence={ECO:0000256|ARBA:ARBA00043821}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38307, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75728, ChEBI:CHEBI:75729; Evidence={ECO:0000256|ARBA:ARBA00001100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38308; Evidence={ECO:0000256|ARBA:ARBA00001100}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75824; Evidence={ECO:0000256|ARBA:ARBA00001338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440; Evidence={ECO:0000256|ARBA:ARBA00001338}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence={ECO:0000256|ARBA:ARBA00001793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912; Evidence={ECO:0000256|ARBA:ARBA00001793}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75583; Evidence={ECO:0000256|ARBA:ARBA00001349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164; Evidence={ECO:0000256|ARBA:ARBA00001349}; CATALYTIC ACTIVITY: Reaction=13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:55296, ChEBI:CHEBI:45479, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:138722; Evidence={ECO:0000256|ARBA:ARBA00000895}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55297; Evidence={ECO:0000256|ARBA:ARBA00000895}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:73990, ChEBI:CHEBI:75466; Evidence={ECO:0000256|ARBA:ARBA00001313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072; Evidence={ECO:0000256|ARBA:ARBA00001313}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000256|ARBA:ARBA00001150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; Evidence={ECO:0000256|ARBA:ARBA00001150}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76; Evidence={ECO:0000256|ARBA:ARBA00000633}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489; Evidence={ECO:0000256|ARBA:ARBA00000633}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000256|ARBA:ARBA00001764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176; Evidence={ECO:0000256|ARBA:ARBA00001764}; CATALYTIC ACTIVITY: Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584; Evidence={ECO:0000256|ARBA:ARBA00001796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168; Evidence={ECO:0000256|ARBA:ARBA00001796}; CATALYTIC ACTIVITY: Reaction=hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-dihexadecanoyl-1,2-hexadecanediol + 2 CoA; Xref=Rhea:RHEA:38211, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75608; Evidence={ECO:0000256|ARBA:ARBA00001118}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38212; Evidence={ECO:0000256|ARBA:ARBA00001118}; CATALYTIC ACTIVITY: Reaction=hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoA; Xref=Rhea:RHEA:38171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75587; Evidence={ECO:0000256|ARBA:ARBA00000174}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172; Evidence={ECO:0000256|ARBA:ARBA00000174};

PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000256|ARBA:ARBA00005175}.

Acyltransferase;Endoplasmic reticulum;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix

triglyceride biosynthetic process [GO:0019432]

endoplasmic reticulum membrane [GO:0005789]

diacylglycerol O-acyltransferase activity [GO:0004144]; retinol O-fatty-acyltransferase activity [GO:0050252]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR027251;IPR004299;IPR014371;

A0A481NV25

MKDMDIKAVFIGDKAENGPVYKMLLNKMVDEHLGWRENYIPSDMPAISEGDKLTPDYLATRDHMIEVLDEVSQRLRAGSIPWHSAGRYWGQMNAETLMPALLAYNYAMLWNPNNVALESSMATSQMEAEVGQDFASLFNMADGWGHIAADGSIANLEGLWYARCIKSIPLAVKEVLPEKVKNMSEWALLNLSVEEILEMTESFTDEEMDEVKAASSRSGKNIQKLGKWLVPQTKHYSWMKALDICGVGLDQMVAIPVQEDYRMDINALEKTIRELADQKIPILGVVAVVGTTEEGQVDSVDKIIQLREKLKDEGIYFYLHVDAAYGGYARSLFLNEAGEFVPYASLAEFFEEHHVFHHYVTIDKEVYEGFRAISEADSVTIDPHKMGYVPYAAGGIVIKHKNMRNIISYFAPYVFEKSVKAPDMLGAYILEGSKAGATAAAVWTAHRVLPLNVTGYGQLIGASIEAAQRFREFLEQLHFTVKGKTIEVYPLNHPDFNMVNWVFKVQDCTDLNAINELNEKMFDRSSYMDGDVYGERFITSHTTFTQEDYGDSPIRFIERMGLSKEEWQKEQQITLLRAAIMTPYLNDDRIFNFYTKEIAKAMEKKLNEIIK

Enterococcus faecium (Streptococcus faecium)

FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:30659181). Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecium (By similarity). {ECO:0000250|UniProtKB:Q838D6, ECO:0000269|PubMed:30659181}.; FUNCTION: Also involved in drug metabolism, being able to catalyze decarboxylation of levodopa (L-dopa) to dopamine. In gut microbiota this enzyme is in fact exclusively responsible for the decarboxylation of levodopa, and thus reduces in situ levels of levodopa in the treatment of Parkinson's disease. It was shown that abundance of bacterial tyrosine decarboxylase in the proximal small intestine - the primary site of levodopa absorption - contributes to interindividual variation in drug efficacy and can explain the requirement for an increased dosage regimen of levodopa treatment in Parkinson's disease patients. {ECO:0000269|PubMed:30659181}.

4.1.1.-; 4.1.1.25

CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:30659181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:0000305|PubMed:30659181}; CATALYTIC ACTIVITY: Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:30659181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12273; Evidence={ECO:0000305|PubMed:30659181};

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:30659181};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for L-tyrosine (at pH 5.0) {ECO:0000269|PubMed:30659181}; KM=0.4 mM for L-dopa (at pH 5.0) {ECO:0000269|PubMed:30659181}; Vmax=4.4 umol/min/mg enzyme for the decarboxylation of L-tyrosine (at pH 5.0) {ECO:0000269|PubMed:30659181}; Vmax=3.4 umol/min/mg enzyme for the decarboxylation of L-dopa (at pH 5.0) {ECO:0000269|PubMed:30659181}; Note=kcat is 435.6 min(-1) for the decarboxylation of L-tyrosine. kcat is 342.4 min(-1) for the decarboxylation of L-dopa (at pH 5.0). {ECO:0000269|PubMed:30659181};

PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:30659181}.

Coiled coil;Decarboxylase;Lyase;Pyridoxal phosphate

L-dopa metabolic process [GO:1903184]

L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837]

IPR002129;IPR015424;IPR015421;IPR021115;IPR049373;IPR022397;

3.40.640.10;

A0A482N9V7

MAANDSNNQTKPQLPEEPVAIVGSSCRFPGSSNSPSKLWDLLRQPRDVLKEFDPDRLNLKRFYHPDGDTHGSTDVTNKSYLLEEDSRLFDASFFTINPAEAAGMDPQQRILLETVYEAFESAGMTLEQLRGSLTAVHVGTMTNDYAGIQLRDLETIAKYNATGTANSIVSNRISYVFDLKGPSETIDTACSSSLVALHHAARGLLNGDCETAVVAGVNLIYDAASYIAESKLHMLSPDSQSRMWDKSANGYARGEGAAALLLKPLSRALRDGDHIEGVIRATGVNSDGQSPGITMPFAPTQAALIRQTYRRAGLDPVKDRPQYFECHGTGTPAGDPVEARAISEAFEPSADNPIYVGSIKTIIGHLEGCAGLAGVMKVILALKNRTIPPNMLFNELNPAIAPFYGPLQIPKKAMPWPELPENTPIRASVNSFGFGGTNAHVIIESFESSTPSSDSEKCEEGALGPLLFSAGSGASLLHTVQAYVQYLDQNPSVDLRDLSWLLQTRRSTHRVRTHFSGTSSDAILESMIKFVNNNEKTPSTEVGHQPKLINPKEVPGILGVFTGQGAQWPQMGKELIGKSPIFRRTLEDCDATLQALPSSDIPKWSLVKELMANASSSRVAEAAISQPLCTAVQLGLVNMLKASGLNFDAVVGHSSGEIAATYASGIINLQAAIQIAYYRGFHAKLAKGEKGQQGGMLAAGLTLDKAKQLCLREEFVGRLQVAASNAPQTVTLSGDLDAIEEVKKYLDEENVFARQLKVDTAYHSHHMKPCAEPYLKSLLACDIEVRKPTPGQCIWNSSVRGDTGLLKGDLSSLKGPYWVANMVQTVLFSQAVESSIWHGGPWDLAIEVGPHPALKGPTEQTLKAVYGVVPLYTGVLKRGASDVEAFSTAIGVTWSQLGPSFVDFAGYRKTFYESEPPTPKVIKDLPGYSWDHDKVYWRESRISKRYRTGRDQTHELLGRRTPDDNEFELRWRNVLKLSEMPWLRGHEVLEEVLLPGAAYVSIAVEASKHIATSKGKSIELLEVEDVDIQRPVVVPDNKEGVETLFTARLLPGSSSDKVLKALFSYYICNDQSTGTMVHTCSGRLSVHLGEAKEDVLPQRDPVPQNLVNINTDRAYGMFKDIGLNYTGVFRSIKESSRTLQYSAATGIWPEGSLSDKYLVHPAMLDVAFQTLFIARAHPASRLITSALLPSHIERIQVSPSVPILHARENSDEIKADFDCWVVHQTASSLTGDLNIYDKVSGKTFLQVEGLTTKMVGEQDASGDRPVFTKTVWGSDGSLGLDEPERDPVGDAEGLSLAEAAERMALFYMKRVVKEISPEERTKFQWYHQRMFEAFEQHLVNVGSGSHPMLKSEWLSDDSSIMDGLDRIHPTSIDLKLLRACGENMPDVVREKTQLLEVMSKDDMLNRFYMDNCAARINNDIAKVVKQISFKFPRANILEIGAGTGGTTWSILKDINDAYDSYTFTDISSGFFPKAAEKFSDFAHKMIFKTLDVEKQPSEQGFAENSYDVIVAANVLHATRSLETTLRNARSLLRPGGYLILMEITNPESLRTTFIFGGFSGWWLSEEPHRKLGPVVTAMDWDTVLNDTGYSGADMVVHDLAEESKHLTSLIVSQAVDDDFLRLREPLSNLADMSAPTESILVIGGKKLLTSKMVNEINKLLPKSWKRHISSAGSIDDIDINELKPGTEVISLQELDDPLFSTPMTAERMSTIQNLMMSAKTLLWVTTAGKSHAPRASMFHGIARIVPSELQHLQIQVLGLEAGSTPAIATRHCVEAFLRLRGTSDTTREMLWAIEPEVEIMADGQVLIPRVVPDETLNQTYNASRRVVTKTVDATDLAVEAVAGPTKMMLQTAELQAGERKTRIQVKYALHLPAMDGKGIYVVYGQRQDDTSSFVLAVSKSNSSIVDVDSKHAVSVSDNCEPATLNVLATYLIARAIATLSKQAGSVLLSEPEESLAAIVATETAKQGTQAYFLSSKKVSPVEWIKVHANASKRAIQKAVPHDVQLLIDCSGIEASGNAVMASMPLHCVERQLDAHLLFDALESTESKPESLLEEAYQYATQLITQEQVQSECEVFPASDLPLTNMLSLVHKKYVTDWQQRDSLVVSVPPLDLEGIFKADKTYLMVGAAGGLGLSICEWMIRNGAKNLIITSRKPQVDQNMIEEASRVGATVKVMAMDVSSKESVAEVVQQAQEIMPPIAGVCNAAMVLSDKMFLDMDVDQLNGTLAAKVYGTEHLDAVFADAPLDFFIVLSSTATTIGNIGQANYHVANLFMTSLVAQRRARGLAGSVIHIGYVADVGYVTRQDRERQLEQHFRNVRLMALSETDVHHAFAEAVRGGRPGNTVGSPDIIMGLEPASVPLEPERQTLWLSNPCFGHLVPSTLQNDSSQTGGTGNGSSVRRQVEEAQTEDEAVDAVLDGFCAKLEAILQLREGSVKENVQRAVIDLGIDSLVAVEIRTWFLKELGAEVPVVKILGGDTVLQICTTAAKKVMANAMKKKEEDAVAEEGGREAASKKEPAPAASAPTPAPVAPSLLDVPARAFEPDSATISEVGDDSAFSNKGSSSSATGASSPKELSDSESVPDTSKDQSHVRPETVRDERMSPAQARIWFLTKHLDDPSAYNMVFHYRVKGPLKTVRLRHALQVATGHHESLRTLFYSRLEDGQPMQGVMPASAYELKHVPGADEADLKKELALLKAREWDLENGRTFSVSVLSRAADEHDVVFGYHHIIMDVVGWYFFVRDLDRAYRMQPFDKKISGSYVDYSVMQLSQKNTAAASDDLAFWQKEFSTVPDPIPLLPIAAVSARPTDSGRKVSHHEYLELDPAQNLAVKETCEKLRISPFHFHVAVLRALIGGYTNIDDMCIGVVDANRGDERFAQTVGCFVNMLPVRVEAPSDATFADIARSASRKALMAFAHSSAPLDMILDAVKAPRSSETTPLFQVAVNYRTGGVWDLPMGDCQMKLSLTDGKDAENPFDISLGIAETGKGCVIEMHCQKTLYSSDATRTLLNTYLRLVDTFCKNTHVKLKDCVIHDQAKVSEALQIGKGPTTDFGWPSTLSHRVLETCLKSPKNAAIQFKGELLSYEQLASRIHLVAAAIVRAGASKGSRVAVLCEPSADAIISMLATLHIGGVYIPMDVSLPTARHAAMMNGGQPTLLLSHAATKHRVEDLVNETGSTISVLQVDTISSVEEKETVSCAAEPHNNAVLLFTSGSTGTPKGIMLSQANFVNHLALKTDRLQLGQENVLQQSSMGFDMSLIQMFCALANGGCLVIAPSEMRRDPVELTNLVHNSQISLTIATPSEYLAWLRYGTASLKDHTIWRHACMGGEPVSRQLKTEFWRLDLANLQLTNCYGPTEITAAATFETIRLDDQDDDNDRAQHAVGKALPNYSVRILDTAGRPQPVDHIGEICIGGASVALGYLGLPEQTKAKFTVDPVSGERLYLTGDKGKLLSDGTLLCLGRLDGDTQIKHRGLRIELQEVESALIQTANGLFSSAVVSARGSILVAHATISQSQAEPSESDLAKILSRLKLPQYFIPATIGILPTMPTTANGKLDRKAIASLPLPQKVTGEEGPQEKMNIREGELRLLWERVLPDTATTTPLGPSSDFFLCGGNSMLLMKLQAAIKESIGIEISTRVLYQASTLREMALCVDEQREEQADALEQHFDWQAETSLPKWLLDQIEDLPKTTKQPPKPNGIDILMTGATSFIGGRLLRSLVRSPSVRKVHCVAVLADEQDQLYQDEKVKCYTGSLLSSTLGLNNGERDQLARNVDVVIHAGSSGHCLNTYGSLRTPNLVSLQFLASLALPRSIPLLLLSSNRVPLLSGNTALPPTSVAAFPPATDGREGYTATKWASEVFLEKLVGAVQKKAPRPWVASVHRPCVVVSEHAPNSDALNAILRYSASMKCVPHLESATGYLDFASVESIVDSMAESAIEMATGNVTDQPSIRFQHHSGGVKVPIGDFKVHMENVYGGNFEEVHLEEWMHRAAAAGLDPLITAYMEGIIEAGAPIVFPYLGETV

Talaromyces variabilis (Penicillium variabile)

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:30905148). IccA assembles the backbone of ilicicolin H (PubMed:30905148). The PKS portion and trans-acting enoyl reductase iccB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly (PubMed:30905148). The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate (PubMed:30905148). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (Probable) (PubMed:30905148). {ECO:0000269|PubMed:30905148, ECO:0000305|PubMed:30905148}.

2.3.1.-; 6.3.2.-

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 8 AH2 + ATP + 4 H(+) + holo-[ACP] + L-tyrosine + 7 malonyl-CoA + 2 S-adenosyl-L-methionine = 8 A + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-tetraenoyl]-L-tyrosyl-[ACP] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64544, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16623, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:58315, ChEBI:CHEBI:59789, ChEBI:CHEBI:64479, ChEBI:CHEBI:155893, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:30905148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64545; Evidence={ECO:0000269|PubMed:30905148};

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30905148}.

Ligase;Methyltransferase;Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Repeat;Transferase

fatty acid biosynthetic process [GO:0006633]; ilicicolin H biosynthetic process [GO:0140781]; methylation [GO:0032259]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; non-ribosomal peptide synthetase activity [GO:1904091]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218]

DOMAIN: IccA has the following domain architecture: KS-MAT-DH-MT-KR-ACP-C-A-T-R. The PKS module (domains KS to ACP) is responsible for the biosynthesis of the polyketide chain and catalyzes three Claisen condensations, as well as beta-keto processing and methylation. The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide. The bimodular assembly line is terminated with a putative reductase (R) domain that facilitates formation and release of the tetramic acid product. {ECO:0000250|UniProtKB:Q5ATG8}.

IPR010071;IPR001227;IPR036736;IPR014043;IPR016035;IPR045851;IPR020845;IPR000873;IPR042099;IPR023213;IPR001242;IPR013120;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR013968;IPR049900;IPR020806;IPR009081;IPR006162;IPR029063;IPR016039;

3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;

A0A482PDI9

MLSPLNVLQFNFRGETALSDSAPLQTVSFAGKDYSMEPIDEKTPILFQWFEARPERYGKGEVPILNTKEHPYLSNIINAAKIENERVIGVLVDGDFTYEQRKEFLSLEDEHQNIKIIYRENVDFSMYDKKLSDIYLENIHEQESYPASERDNYLLGLLREELKNIPYGKDSLIESYAEKRGHTWFDFFRNLAVLKGGGLFTETGKTGCHNISPCGGCIYLDADMIITDKLGVLYAPDGIAVYVDCNDNRKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGVGKGLKRHFNYSSLQDYNVFCNFIEFKHKNIIPNTSMYTNSSW

Citrobacter rodentium

FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:16552063, PubMed:23955153, PubMed:24025841, PubMed:28522607). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TNFRSF1A and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:23955153, PubMed:28522607, PubMed:28860194). Has preference for host FADD as substrate compared to TNFRSF1A and RIPK1 (PubMed:28860194). Also acts on host proteins without a death domain: catalyzes GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2 and TRAF3, leading to inhibit NF-kappa-B signaling and type I interferon production, respectively (PubMed:23332158, PubMed:27387501, PubMed:28522607). Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB (PubMed:31974499). Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (By similarity). {ECO:0000250|UniProtKB:B7UI21, ECO:0000269|PubMed:16552063, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:28522607, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:31974499}.

2.4.1.-

CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:31974499}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:31974499};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B7UI21};

Glycoprotein;Glycosyltransferase;Manganese;Metal-binding;Secreted;Toxin;Transferase;Virulence

symbiont-mediated perturbation of host defense response [GO:0052031]; symbiont-mediated perturbation of host defense-related programmed cell death [GO:0034053]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034]

extracellular region [GO:0005576]; host cell [GO:0043657]

glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16552063}. Host cell {ECO:0000269|PubMed:16552063}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:16552063}.

PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000250|UniProtKB:B7UI21}.

DOMAIN: Adopts a GT-A fold and acts as an inverting enzyme that converts the alpha-configuration in the UDP-N-acetyl-alpha-D-glucosamine donor to the beta configuration in the N-linked (GlcNAc) arginine product. {ECO:0000250|UniProtKB:B7UI21}.

3.90.550.20;

A0A494BAW1

MLPTSPKTLVLLGALLTGPLGPAGGQDAPSLPWEVQRYDGWFNNLKYHQRGAAGSRLRRLIPANYADGVYQALEEPLLPNPRRLSDAVAKGKAGLPSVHNRTVLGVFFGYHVLSDLVSVETPGCPAEFLNIYIPRGDPVFDPDKRGNVVLPFQRSRWDHNTGQSPSNPRDQSNQVTGWLDGSAIYGSSHSWSDTLRSFSGGQLASGPDPAFPRNSQSSLLMWMAPDPSTGRGGPQGVYAFGAQRGNREPFLQALGLLWFRYHNLCARKLAQEHPHWGDEELFQHARKRVIATYQNIALYQWLPSFLQKTPPEYSGYRPFMDPSISPEFVVASEQFLSTMVPPGVYMRNSSCHFRKFPKEGSDSSPALRVCNSYWIRENPNLKTAQDVDQLLLGMASQISELEDRIVIEDLRDYWPGPERFSRTDYVASSIQRGRDMGLPSYSQALLALGLEPPKNWSALNPQVEPQVLEATAALYNQDLSQLELLLGGLLESHGDPGPLFSNIILDQFVRLRDGDRYWFENTRNGLFSKEEIAEIRNTTLRDVLVAVSNVDPSALQPNVFFWQEGAPCPQPRQLTTDGLPQCAPVTVIDYFEGSGAGYGVTLVAVCCFPLVSLIVAGVVAHFRNREHKMLLKKGKESLKKQPASDGVPAMEWPGPKEKSYPVTLQLLPDRSLQVLDKRFTVLRTIQLQSPQQVNLILSSNSGRRTLLLKIPKEYDLVLMFNSEEDRGAFVRLLQDLCICCTPGLHIAEVDEKELLRKAVTKQQRAGILEIFFRQLFAQVLDINQADAGTLPLDSSQQVREALTCELSRAEFADSLGLKPQDMFVESMFSLADKDGNGYISFREFLDILVVFMKGSSEDKSRLMFTMYDLDGNGFLSKDEFFTMMRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSDLRFTQLCVKGGAGGTKDIFKQSSACRVSFINRTPGNSSCPPETALSDMETPELGSTGLKKRFGKKVMGPSPRLYTEALQEKKQSGFLAQKFKQYKRFVENYRRHIVCVTIFSAICIGLFADRAYYYGFASPPTDIEETTYVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYIPFDAAVDFHRWIAMAAVVLAVLHSAGHAVNVYIFSVSPLSLMACVFPNVFVNDGSKFPPKYYWWFFETVPGMTGVLLLLVLAIMYVFASHHFRRHSFRGFWLTHHLYVVLYVLIIIHGSYALIQLPSFHIYFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTYLQFQRPKTFEYKSGQWVRIACLDLGTNEYHPFTLTSAPHEDTLSLHIRAVGPWTTRLREIYSPPVGGTCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSMGSQMLCKKIYFIWVTRTQRQFEWLADIIREVEENDCQDLVSVHIYITQLAEKFDLRTTMLYICERHFQKALNRSLFTGLRSITHFGRPPFELFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINRQDRAHFVHHYENF

Mus musculus (Mouse)

FUNCTION: Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain. {ECO:0000256|ARBA:ARBA00003796}.

1.6.3.1

CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1; Evidence={ECO:0000256|ARBA:ARBA00000518}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; Evidence={ECO:0000256|ARBA:ARBA00000547};

PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. {ECO:0000256|ARBA:ARBA00005197}.

Calcium;Cell membrane;FAD;Flavoprotein;Glycoprotein;Membrane;Metal-binding;NADP;Oxidoreductase;Proteomics identification;Reference proteome;Repeat;Signal;Thyroid hormones biosynthesis;Transmembrane;Transmembrane helix

adenohypophysis morphogenesis [GO:0048855]; bone mineralization [GO:0030282]; defense response [GO:0006952]; fertilization [GO:0009566]; hormone biosynthetic process [GO:0042446]; hormone metabolic process [GO:0042445]; inner ear development [GO:0048839]; multicellular organism growth [GO:0035264]; response to oxidative stress [GO:0006979]; superoxide anion generation [GO:0042554]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]; thyroid hormone metabolic process [GO:0042403]

apical plasma membrane [GO:0016324]; NADPH oxidase complex [GO:0043020]; plasma membrane [GO:0005886]

calcium ion binding [GO:0005509]; heme binding [GO:0020037]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; peroxidase activity [GO:0004601]; superoxide-generating NAD(P)H oxidase activity [GO:0016175]

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR034821;IPR011992;IPR018247;IPR002048;IPR013112;IPR017927;IPR013130;IPR013121;IPR039261;IPR019791;IPR010255;IPR037120;IPR017938;

1.10.238.10;1.10.640.10;3.40.50.80;2.40.30.10;

A0A499UB99

MATNNIVVLGAGVSGLTTAWLLSKDPSNKITVAAKHMPGDYDIEYCSPWAGANYLPVGAENSRVGQWERATWPHLRDIAQNHPEAGIHFQDTVVYNRTKDQGSTTGQWFSELVKPNPWYGKVLPNFRELSKDELPPGIDNANRFTSVCINTAVYLPWLVGQCRKNGVVFKRAVFKHVAEAANAHHSGQKADLVVNCTGLSSRKLGGVQDNTLLPARGQIVVVRNDPGLMCSISGTDDGDDEVTYMMTRAAGGGTILGGTYQKHNWDSLPDPNLAVRIMKRCIELCPSLVAPGQGIEGLDIIRHGVGLRPVREDGPRIEKELIDGVWVVHNYGHGGYGYQTSFGCATTAVEVVREALQQQKQRRDKARL

Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii)

FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:31420577). Enables the organism to utilize D-amino acids as a source of nutrients (By similarity). Unusually, has high activity on D-glutamate (PubMed:31420577). {ECO:0000250|UniProtKB:Q9HGY3, ECO:0000269|PubMed:31420577}.

1.4.3.3

CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29986; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-serine + H2O + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-phenylalanine + H2O + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:57981; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70964; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78220; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-methionine + H2O + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:37583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32557, ChEBI:CHEBI:58183; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37584; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-valine + H2O + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78203, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:74338; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78204; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-histidine + H2O + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:78227, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58133, ChEBI:CHEBI:142967; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78228; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-glutamine + H2O + O2 = 2-oxoglutaramate + H2O2 + NH4(+); Xref=Rhea:RHEA:78215, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16769, ChEBI:CHEBI:28938, ChEBI:CHEBI:58000; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78216; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-isoleucine + H2O + O2 = (R)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:193151, ChEBI:CHEBI:228255; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78236; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-allo-isoleucine + H2O + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:85306; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78224; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-threonine + H2O + O2 = (S)-3-hydroxy-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78251, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57757, ChEBI:CHEBI:228256; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78252; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-asparagine + H2O + O2 = 2-oxosuccinamate + H2O2 + NH4(+); Xref=Rhea:RHEA:78243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735, ChEBI:CHEBI:74337; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78244; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-tryptophan + H2O + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:78247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57719; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78248; Evidence={ECO:0000269|PubMed:31420577}; CATALYTIC ACTIVITY: Reaction=D-tyrosine + H2O + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70959, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58570; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70960; Evidence={ECO:0000269|PubMed:31420577};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:31420577, ECO:0000269|PubMed:33135670};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.213 mM for D-methionine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=0.628 mM for D-valine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=2.7 mM for D-alanine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=12.1 mM for D-glutamate (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=19.2 mM for D-arginine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; Note=kcat is 120 sec(-1) with D-methionine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 225 sec(-1) with D-valine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 189 sec(-1) with D-alanine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 90.7 sec(-1) with D-lutamic acid as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 45.6 sec(-1) with D-arginine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). {ECO:0000269|PubMed:31420577};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:31420577};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:31420577};

3D-structure;Disulfide bond;FAD;Flavoprotein;Oxidoreductase;Peroxisome

D-amino acid catabolic process [GO:0019478]; D-amino acid metabolic process [GO:0046416]; nitrogen utilization [GO:0019740]

peroxisomal matrix [GO:0005782]

D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949]

SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q9HGY3}.

PTM: The disulfide bond might contribute to the high thermal stability of the protein. {ECO:0000269|PubMed:33135670}.

IPR006181;IPR023209;IPR006076;

3.30.9.10;3.40.50.720;

A0A4D6K823

MSVSMSLVQGGAAGGAPQGASAILAAAAPYYQPPAVPQDVQPDRPIGYGAFGVVWAVTDPRDGRRVALKKLPNVFQSLVSSKRVFRELKMLCFFKHENVLSALDILQPPHLDFFQEIYVITELLQSDLHKIIVSPQHLSADHIKVFLYQILRGLKYLHSARILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDQAKHMTQEVVTQYYRAPEILMGARHYSSAVDVWSVGCIFGELLGRRILFQAQNPVQQLELITELLGTPTMEDMRHACEGARTHMLRRAPKPPSFSVLYTLSSHATHEAVHLLCQMLVFDPDKRISVTDALAHPYLDEGRLRYHSCMCKCCFTTSAGMRQYTADFEPSAGQPFDDLWERKLTSVQQVKEEMHKFIAEQLQTGRVPLCINPQSAAFKSFASSTVAHPSELPPSPHQWEXRQNEAIAA

Drosophila melanogaster (Fruit fly)

2.7.11.24

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=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000494}; 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=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000088, ECO:0000256|RuleBase:RU361165};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|RuleBase:RU361165};

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

cellular response to stress [GO:0033554]; intracellular signal transduction [GO:0035556]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; phosphorylation [GO:0016310]; regulation of establishment of planar polarity [GO:0090175]; response to external stimulus [GO:0009605]; wing disc dorsal/ventral pattern formation [GO:0048190]

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

ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR003527;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A4P8DY91

MTTTELIPPTIQVDEEEEEACMFAMQLASASVLPMVLKSAIELDLLESIAKAGPGAYVSPSELAAKLPSSQPDTPVMLDRILRLLASYSVLKCKVQDLPQGGVERLYALAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNLGMSNHSTITMKKILQTYNGFAGLKTVVDVGGGTGATLNMIISKYPNIKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPEGDAIFMKWICHDWSDAHCLSFLKNCYKALPQNGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKEFEALGKMAGFKSFNKVCCAHNTWIMEFLK

Kitagawia praeruptora (Peucedanum praeruptorum)

FUNCTION: O-methyltransferase involved in the biosynthesis of methoxylated coumarins natural products such as isoscopoletin, scopoletin, xanthotoxin and bergapten, photosensitizers used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubMed:30934718). Catalyzes the methylation of esculetin, bergaptol and xanthotoxol, but seems inactive on scopoletin and isoscopoletin (PubMed:30934718). {ECO:0000269|PubMed:30934718}.

2.1.1.-; 2.1.1.69; 2.1.1.70

CATALYTIC ACTIVITY: Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809; Evidence={ECO:0000269|PubMed:30934718}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + xanthotoxol = H(+) + S-adenosyl-L-homocysteine + xanthotoxin; Xref=Rhea:RHEA:17901, ChEBI:CHEBI:15378, ChEBI:CHEBI:15709, ChEBI:CHEBI:18358, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.70; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17902; Evidence={ECO:0000269|PubMed:30934718}; CATALYTIC ACTIVITY: Reaction=esculetin + S-adenosyl-L-methionine = H(+) + isoscopoletin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68944, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81484, ChEBI:CHEBI:490095; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68945; Evidence={ECO:0000269|PubMed:30934718}; CATALYTIC ACTIVITY: Reaction=esculetin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + scopoletin; Xref=Rhea:RHEA:68948, ChEBI:CHEBI:15378, ChEBI:CHEBI:17488, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:490095; Evidence={ECO:0000269|PubMed:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68949; Evidence={ECO:0000269|PubMed:30934718};

PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:30934718}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30934718}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:30934718};

3D-structure;Methyltransferase;S-adenosyl-L-methionine;Transferase

aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to hydrogen peroxide [GO:0042542]; response to UV [GO:0009411]

catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; O-methyltransferase activity [GO:0008171]; orcinol O-methyltransferase activity [GO:0102938]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;

3.40.50.150;1.10.10.10;

A0A4X1UM84

MPPQLSNGLNHSAKVVRGTLDSLPQAVRDFVESSAKLCQPDQIHICDGSEEENQQLLSHMEEEGVIKRLKKYDNCWLALTDPRDVARIESKTVIITQEQRDAVPIPRSGLSQLGRWMSPEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGSAVLDALGAGEFIKGLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGVTNPEGQKKYFAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDQQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQSNTIFTNVAETSDGGVYWEGIDQPLAPGIKLTSWKGTEWDPKDGEPCAHPNSRFCTPASQCPIIDPAWEAPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKDGRFLWPGFGENCRVLAWMFDRVQGKGGARLTPIGYVPEEAALDLRGLEAIRVSELFQVSKEFWEEEADEIHKYLEEQVNADLPYEIQSEVLALKQRISQM

Sus scrofa (Pig)

FUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:26792594). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (By similarity). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (By similarity). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (By similarity). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (By similarity). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000250|UniProtKB:Q9Z2V4, ECO:0000269|PubMed:26792594}.

2.7.11.-; 4.1.1.32

CATALYTIC ACTIVITY: Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence={ECO:0000269|PubMed:26792594}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; Evidence={ECO:0000250|UniProtKB:Q9Z2V4}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390; Evidence={ECO:0000250|UniProtKB:Q9Z2V4}; CATALYTIC ACTIVITY: Reaction=GTP + L-seryl-[protein] = GDP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:64020, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P35558}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64021; Evidence={ECO:0000250|UniProtKB:P35558};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P35558}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P35558};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 uM for phosphoenolpyruvate {ECO:0000269|PubMed:26792594}; KM=27.4 uM for GDP {ECO:0000269|PubMed:26792594}; KM=13.1 uM for oxaloacetate {ECO:0000269|PubMed:26792594}; KM=45.9 uM for GTP {ECO:0000269|PubMed:26792594}; Note=kcat is 6.8 sec(-1) with phosphoenolpyruvate as substrate (PubMed:26792594). kcat is 7.6 sec(-1) with GDP as substrate (PubMed:26792594). kcat is 46 sec(-1) with oxaloacetate as substrate. kcat is 39 sec(-1) with GTP as substrate (PubMed:26792594). {ECO:0000269|PubMed:26792594};

PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000250|UniProtKB:Q9Z2V4}.

Acetylation;Cytoplasm;Decarboxylase;Endoplasmic reticulum;Gluconeogenesis;GTP-binding;Kinase;Lyase;Manganese;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase;Ubl conjugation

cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; cellular response to potassium ion starvation [GO:0051365]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol biosynthetic process from pyruvate [GO:0046327]; hepatocyte differentiation [GO:0070365]; oxaloacetate metabolic process [GO:0006107]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of memory T cell differentiation [GO:0043382]; positive regulation of transcription by RNA polymerase II [GO:0045944]; propionate catabolic process [GO:0019543]; regulation of lipid biosynthetic process [GO:0046890]; response to bacterium [GO:0009617]; response to starvation [GO:0042594]; tricarboxylic acid metabolic process [GO:0072350]

cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]

carboxylic acid binding [GO:0031406]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; protein serine kinase activity (using GTP as donor) [GO:0106264]

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35558}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}.

PTM: Acetylated (By similarity). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2 (By similarity). Deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000250|UniProtKB:Q9Z2V4}.; PTM: Ubiquitination by UBR5 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P35558}.; PTM: Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation. Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2. {ECO:0000250|UniProtKB:P35558}.

DOMAIN: Binds oxysterols in a pocket within their transmembrane domains and interacts with SCAP via transmembrane domains 3 and 4. {ECO:0000250|UniProtKB:Q9Y5U4}.; DOMAIN: The KxHxx motif mediates association with the coatomer complex. {ECO:0000250|UniProtKB:Q9Y5U4}.

IPR018091;IPR013035;IPR008209;IPR035077;IPR035078;IPR008210;

3.90.228.20;3.40.449.10;2.170.8.10;

A0A4Y6HUD7

MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQSEEKTLLDKFVEAYYEFESYKSGQTVKVDGKTLSLAGVVAAARHHAKISLDDSASIKDKVVKSRKVIADKVASGASVYGLSTGFGGSADTRTDQPLSLGHALLQHQHVGVLPSSSQPLDVLPLSDPMSATSMPEAWVRAAMLIRMNSLIRGHSGVRWELIEKIAEIFDANITPVVPLRSSISASGDLSPLSYIAGTVVGNPSIRVFDGPAAFGAREMVPSAKALASHGIDPLPLASKEPLGILNGTAFSAAVGALALNEAVHFAMLAQVCTAMGTEALVGTRLSFEPFIHATCRPHPGQIEAARNIYNLLEGTTFASVHHEEVHIAEDQGTLRQDRYPLRTSPQFLGPQLEDILHAYVSVTQECNSTTDNPLIDGETGEIHHGGNFQAMAVTNAMEKTRLALHHIGKLLFAQCTELVNPAMNNGLPPSLAATDPSLNYHTKGIDIATAAYVSELGYLANPVSTHIQSAEMHNQAVNSLALISARATVNSLDVLSLLISSYLYILCQALDLRALQMEFVKGVEEIIREELSLLFASVVSPAELEALTSKVLSAAQTSLDTSGSMDAPARMKKMASTTTIPLFDFLTELTLPDAISSGIAMVSIPSFRSHLASRATALLDQLRRDYLSGQRGAAPASPYLNKTRMVYEFVRLTLGVKMHGSENYARFAKGLGVEDETIGQNISRIHEAIRDGKMQAITVAMFA

Pleurotus ostreatus (Oyster mushroom) (White-rot fungus)

FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion (PubMed:31655558). Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity). {ECO:0000250|UniProtKB:P11544, ECO:0000269|PubMed:31655558}.

4.3.1.24

CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; EC=4.3.1.24; Evidence={ECO:0000269|PubMed:31655558};

PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.

Cytoplasm;Lyase;Phenylalanine catabolism;Phenylpropanoid metabolism

cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559]

cytoplasm [GO:0005737]

phenylalanine ammonia-lyase activity [GO:0045548]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.

PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.

IPR001106;IPR024083;IPR008948;IPR022313;IPR005922;IPR023144;

1.20.200.10;1.10.275.10;

A0A4Z3

MALEGLRAKKRLLWRLFLSAFGLLGLYHYWFKIFRLFEVFIPMGICPMAIMPLLKDNFTGVLRHWARPEVLTCTSWGAPIIWDETFDPHVAEREARRQNLTIGLTVFAVGRYLEKYLEHFLVSAEQYFMVGQNVVYYVFTDRPEAVPHVALGQGRLLRVKPVRREKRWQDVSMARMLTLHEALGGQLGREADYVFCLDVDQYFSGNFGPEVLADLVAQLHAWHFRWPRWMLPYERDKRSAAALSLSEGDFYYHAAVFGGSVAALLKLTAHCATGQQLDREHGIEARWHDESHLNKFFWLSKPTKLLSPEFCWAEEIGWRPEIHHPRLIWAPKEYALVRT

Rattus norvegicus (Rat)

FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form polygalactose structures. Synthesis of iGb3 is the initial step in the formation of the isoglobo-series glycolipid pathway and is the precursor to isogloboside 4 (iGb4) and isoForssman glycolipids. Can glycosylate only lipids and not proteins and is solely responsible for initiating the synthesis of isoglobo-series glycosphingolipids. {ECO:0000269|PubMed:10854427, ECO:0000269|PubMed:12626403, ECO:0000269|PubMed:17206613}.

2.4.1.87

CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507, ChEBI:CHEBI:138024; EC=2.4.1.87; Evidence={ECO:0000269|PubMed:10854427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13014; Evidence={ECO:0000305|PubMed:10854427}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = an isogloboside iGb3Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:42000, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:52570, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; Evidence={ECO:0000269|PubMed:10854427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42001; Evidence={ECO:0000305|PubMed:10854427}; CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer + UDP-alpha-D-galactose = a globoside GalGb3Cer + H(+) + UDP; Xref=Rhea:RHEA:56740, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:88154, ChEBI:CHEBI:140743; Evidence={ECO:0000269|PubMed:10854427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56741; Evidence={ECO:0000305|PubMed:10854427};

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P14769}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};

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

carbohydrate metabolic process [GO:0005975]; cellular response to manganese ion [GO:0071287]; glycosphingolipid biosynthetic process [GO:0006688]; lipid glycosylation [GO:0030259]

Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; vesicle [GO:0031982]

alpha-1,3-galactosyltransferase activity [GO:0001962]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; N-acetyllactosaminide 3-alpha-galactosyltransferase activity [GO:0047276]

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}; Single-pass type II membrane protein {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}. Note=Also found in numerous large vesicles throughout the cytoplasm of the soma.

DOMAIN: The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.

IPR005076;IPR029044;

A0A509AFG4

MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVKKGKYNFKGKEWNNISEEAKDLIKRCLTIDSGKRINASEALKHPWFKKKKGSFNLDVKMDIHVLENFKNYALLLKLQKLAMTIIAQQSNDYDLQQLKTVFLYLDEDGKGNITKNQLKKGLENSGLKLPQNFDVLLDQIDSDGSGRIDYTEFLAAALDRKHLSKKLIYCAFRVFDVDNDGEITTAELAHILYNGNKKGSITQKDVNQVKKMIQEVDKNNDGKIDFYEFCEMMKLKY

Plasmodium berghei (strain Anka)

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 (By similarity). In the mosquito midgut, regulates the gliding motility of the ookinete which is essential for the ookinete to invade the midgut epithelium (PubMed:16796674). However, another study showed that while required for ookinete invasion of the midgut epithelium, is not required for ookinete gliding motility (PubMed:16430692). {ECO:0000250|UniProtKB:Q8IBS5, ECO:0000269|PubMed:16430692, ECO:0000269|PubMed:16796674}.

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:0000250|UniProtKB:Q8IBS5}; 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:0000250|UniProtKB:Q8IBS5};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IBS5};

ATP-binding;Calcium;Cytoplasm;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of cell motility [GO:2000147]

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

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]; mitogen-activated protein kinase binding [GO:0051019]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16430692}.

DOMAIN: The EF-hand domain 1 cannot bind calcium due to the presence of a Lys instead of an Asp at position 427 and a Gln instead of a Glu at position 434 preventing calcium binding (By similarity). The EF-hand domains 3 and 4 probably bind calcium constitutively when calcium levels are low, while the EF-hand domain 2 binds calcium following an increase in calcium levels (By similarity). {ECO:0000250|UniProtKB:Q9NJU9}.; 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:Q8IBS5}.

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

1.10.238.10;1.10.510.10;

A0A509AH51

MLNMVDQKKGINNGSSTGVINNINGKIKNEFIFMYLIAAGGFSCVYKIKKKKSNKFYALKKIKFSANESNYEKKVLLNLREIECLRKLKNHPNIVSMNDFWLEVVQTLSKSKRERRGRRKEQQREQMGDKRREKRQQQRREKRKEQNTNTKKRVLITLSDHKKKKLKHLSCPENALNISNITNNERNVLKKDNWKNLILLKNFKKEKHNYNFNHQIELNKYNIMCLWKILNQMCVCKNEKKNIESLLPEQLIKNFKNFLFEKYILAIYDDCSYLNNKNNKTFIFFNNNLGNILHYLWWSYLGKNGKEKKNDIFKLLKYVSDNIIKDNTNLYNIILEFRHSLIELSRFPSNELGNVILNMRIPPNGSCELSEYISNMAKINKLEIYRNKNTLEKFIFKINCNNFDVYKMWINFKNDIIYEGKDVYKEHRKINLKRKIIKKKDIWIKGKKEKHLKNTIGNKCIKKINIYYEKPIHVFVYKSLTYKRQKHHKLWRKHYNNKKNWKYCLNKHENSKKYILFSKICRLMKTQMNKFKREEKFEKKKKIAITNIKVNYNDFEQDISSFNIQIYNKKNKNQLINRIKEQYEQLSISLNPYKLTYENENILRYNEHNYLFGLKNDNEKENIYNAIYFLNFYIWIRREINEYAIISKKRQICQNSRNYQSKKKFYIKRHNQKTYFFENIIFYHYIIMLFLDIEKYKNKFVSLFQYNLYRKLLKISKRIVLMLHRIETNVICIFLLKHFEDYFIRKGIHIVQDKSDRSNKGDEIGIHKMVKIWKSMIAISLIFGKKMYKKKKNIFNFFIELFLNNIQINIFKKFEILYLIIYFYNYFEKSKQFDIEGIGDIIYVWLSLINLFYDDKGKCIKILSKIFAKLNKKLYYVYWGKLYIIMNWTTIVDTIFIRNVLSINREGNYYWVIIVLKMINYFVNVAYTLTRMDIFFIKVMIKFYTRIGSAAATNSVSKNSYNEIFNNIFTLNFMNYIIYNSYFENEKKNYDIYTKYAILFIYCFIIQAYYFDTLFNIRSLESNEIANNLFPGYNYSYKNILLFYERLGRVIKNSNNTKICKYMWRKFINMWSNSIVIKENIISCLTTSRHIYFNILMNFMKIYCLDNILHIKKKKKKMNTPIVLTSKNDLKKWKDCELTKNPKSVKKGILIKKKNRNNNKKYKKKLKETHFIYNIKKVLFKKLVNINIETILYEQNGQCYILVFGSVIKKKNGQIKVKDTKIVRDINIIRDYRIYFYNYLEYFYKNNAHISDNINLIYARKWPYNNKNAVKQFCPYFDKIKDGNRKDIVSLYGNKILVKQNFSKIGNKIKNKKNNLCKKKMRTQKSIYNSNYWREKKENKLLNGNVNIIKKYKSEKIKKKELENFFDNIVYSSENDDFKIIFENATNSNACSTVDLASPNELNTKRNNINKKLKFFKHKKNSKKQKNYKNHKSHKKIFFKSVNNANRFFVTNVEPNPIMSNNHQIADSNDIYNNFSIQKKYEYNHKNCGNIYNTKDCDENDSSYICFLINEHEGQVLSHRHKELYKNMLGMERGNILYRDNACKLKDDFSCLHDQCDNSMIKACGTNELIKESTKIKRENMDKINKMNEVNQHISLETLKYKCSFKKIDKNLIQNKKKIIIRKICQINKTFYFKYNKINDKKRIYFDSVLCKSERHKTYKKRNENIKVILLKTLKGESNEYVLTTYLTEIYSDNINDPFENSRKKINSNEIFYQKTFDMYCIEDEGEVYEEQKRVNKNNKKKKYINEMIKMDTIRTDFEDNFTNSYNKKCNILKMASNINNKNNSGKKERDIKRQFLITNKKKHENNIKIFYNLFKLEESNVNSNPQTNPYYETVIHDNEDNIFYCLYKYIQQQVYRYCNCDIDEYTSNCIDKNVNKWEWYGFIKENENYDKIKTEINSNSFYNCREKHNICNSYNSVYQLEFRKLGNASKEKNFEEKKKIIKIEFRKSFNNFKLPSLLCILKWDNFFKPHFIIRCDNFLHTYNIYFDFFILLMNLFHKGEGSNLYRFNSNKSIIYNPYLSHQIYMVTKYFISNVHKINNKLPIHLENDILEIYSYNRFLTIPNKCSFKNCGNDNNNYDQRSKKHYFTKCGILNTEKVKPSKKRRIGWDGQRQRKRKDIINTLNEENQNMFCKNKEKKEENYKKIDTNISQFSEKNPVSNIDNEKNKQNFIKNKKYKFNLYIRMEYCKDTIENYINRRTRINIKRNIEIINMIIMGLNYIHNNNIMHRDLKPSNIFISNNDIVKIGDFGLASYDYLDDHKINTTKEEEIQKDLIINKNCDKIFFCNKKKLFSNYNSVFPLENGQISDVHNTKGDYNESSISKSKKFAIQNKNRNLRSCKRIFQWWSTIGELNILSKNRRRLTKFKSGSNTIHIRKSTLDENIIVRHANKCHNLSFSQNREHIDRNRMKKCNIIKNHIIKSNKSEKMNISMNVFLRCTKTRRYFTDEDKSVETRKKCSKTSEEENGNICDTKKKKNDIGEKMDKNKIAAQKKKKKKENKHPIGRRSTNSSISSAIVVKRNAYCRLEIEKYFLSKSFQNCRSNKKKKYINIKTIKNKFCSASNKNFGAKWMRIYRKGLHHDDIQEKSADQTTEQMGGCNKTVASDFSSNLKNKKESINHTLGIGTKLYSAPEQLEGNKYTKSVDIFSLGLIIIDLFIKTETNMERTQILCNARERILPDLLIKKHPNVASLCKKMLSLDYKSRPTSAQLYNKIISAGDIFLPDKCP

Plasmodium berghei (strain Anka)

FUNCTION: Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules. {ECO:0000269|PubMed:20584882}.

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:0000305|PubMed:20584882}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:20584882}; 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:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305};

ATP-binding;Coiled coil;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Protein synthesis inhibitor;Reference proteome;Serine/threonine-protein kinase;Transferase;Transmembrane;Transmembrane helix

chromosome segregation [GO:0007059]; dormancy maintenance of symbiont in host [GO:0085015]; microtubule-based process [GO:0007017]; negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]

centrosome [GO:0005813]; cortical microtubule [GO:0055028]; membrane [GO:0016020]; nucleus [GO:0005634]

ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

PTM: Auto-phosphorylated. {ECO:0000250|UniProtKB:Q8I265}.

IPR011009;IPR000719;IPR008271;

1.10.510.10;

A0A509AHB6

MGCNQSKSANDVRGNKVNHVNSKKKNNKREDTNDGEEIAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCKEKNGHSEKAIKVIKKSQFDKGRYSDDNKNIEKFHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLNIKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEKCDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISDEAKELIKLMLTYDYNKRCTAEEALNSRWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNVLRNFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRRAFNLFDTDKSGKITKEELANLFGLTSISEKTWNDVLGEADQNKDNMIDFDEFVSMMHKICDHKTF

Plasmodium berghei (strain Anka)

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 (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK4 and CDPK5 (PubMed:32866196). In the mosquito midgut and during the last stage of male gamete exflagellation, may play a role in the rupture of the host erythrocyte membrane (PubMed:22817984). In the mosquito midgut, required for the differentiation of the zygote into the ookinete by promoting the translational activation of a subset of repressed mRNAs; these mRNAs are kept repressed in the zygote by the DOZI- or CITH-containing mRNP complexes (PubMed:22817984, PubMed:24265753). Dispensable during the asexual blood stage (PubMed:24265753). {ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:22817984, ECO:0000269|PubMed:24265753, ECO:0000269|PubMed:32866196}.

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:0000250|UniProtKB:P62344}; 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:0000250|UniProtKB:P62344};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P62344};

3D-structure;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;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell motility [GO:2000147]; positive regulation of translation [GO:0045727]

cytoplasm [GO:0005737]; host cell plasma membrane [GO:0020002]; motile cilium [GO:0031514]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; 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:22817984}; 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:0000250|UniProtKB:A0A2I0BVG8}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A0A2I0BVG8}. Host cell membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Note=Calcium and/or autophosphorylation does not affect membrane localization. {ECO:0000250|UniProtKB:P62344}.

PTM: Myristoylated. Myristoylation and palmitoylation 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 and palmitoylation are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Phosphorylation at Thr-230 may regulate CDPK1 kinase activity. Phosphorylation increases in response to an increase in intracellular Ca(2+) levels. Autophosphorylated in vitro. Autophosphorylation does not affect membrane localization in vitro. {ECO:0000250|UniProtKB:P62344}.

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;

A0A509ALD0

MEIPNEEIKFLKKEDIKNINLNGMNKKERYEIWKKIPKVELHCHLDLTFSGKFFLKWVRKYNLQPNMTDDQVLDHYLFTKEGKSLAEFIRKAISVSDIYRDYDILEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSHGLDIELIHKAFVKGIKNATEMLNNKIYVALICISDTGHSAASIKHSGDFAIKHKHDFVGFDHGGREIDLKDHKDVYHSVRNHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRVSESEELIELVKKNNILLEVCPISNLLLNNVKSMDTHPIRKLFDAGVKVSVNSDDPGMFLTDINDNYEKLYIHLNFTLEEFMTMNNWALEKSFVNDDIKSKLKTMYF

Plasmodium berghei (strain Anka)

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=57 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=4.4 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 4.7 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.35 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;Reference proteome;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;

A0A509AMC3

MYNKGINICLNEDNKCIILLHIIFNKCIVSFVASHILVEGKICFLNRIKNSKIFRRFGNINNHRRNNVKEYYKFVGRINKGKEKRNKCRIKLHRFYEYAKSYILKQIKWVLNKSKYIYFNIIYHLKTICYLKNAFFLQYTQRKYFSQNIENYIINSLPKHIQSFNPIKWSYYNNNEYASNYIIINNLNFIKYKNKYEKQYDIEMEEDINCKGANDIFYNSYNYCNNNNSNSKCDEKIEKNIVDKNIENKYNIKEYDKTNKSILFPIEEEFKKIIQIENNIERNYMVPNESNKNILYNIKNILEKIRNIEAISNINNYIDMKNTIESYKLNPDKCKEILHKDKDFRNKSKLCLSCFHNIIHKIIYYSKMENISFSDMYKQLLTNYNNTSCEYCNLINNSINSNNDFLSLYNDKNMYNWKNCEKNKFETLENEISCWNFNSSYGNHFQHIQKNSKIYRRILNEENEKAFNNIVGRNEMENDELYKRIHTENNYANQFTENNVDFGVYSDLREYNNGNEKYMLDENEMDQIIDEEVKKQEKNQNLNNMDFNNVNKKYNQLKDDNIIIFNKNNMHNNLYSNGLNDSNLEKNNILFPYEKYNNLDKNEMNLTKYSQNKQFYGQYKYDEAIYKYDLIVLDTSGYIYKVSTDGTYHWKYRIVKNIQYYINYEEENKIENYYNAFKKNNGKINMTHKDILRKNDYEQYHKLKLRAMKKLQYNNFIDVFNSNYKKNYPTYLNEQITEKDDIYKKKNYNYEKSKKKSKNKNAMKKLLSDYSGDLFYVDENNEAIPININIKDVVNNSPFKSTLFPNILFIGSRQSSIVNLDFDTGYVIKKYEENYDDLVKEKQKALPNKYEKFINKNSNVLHDKLEKYLDHSIDINDKNYYVNEEKDDLDKDYTIIDGKVAENNQQLDNIDLYNNEIETENNNGINHLLLIDGKGQIEEQSPNNGNKIIKGDVSNMTDECGTENCLSKHSKEEIEIANNKFNKNNKDKLLIQRTKIKNKKHFLMGKWYMNISNNNLLNINSSVLGINKKKRNSKKGENRNKKRKTQKRQLQISLVKWVIKAVDETSLKQKWITSWVDVGSIFITDSHKQDLSFINSLIDIDGNKLILRTLENNKVNKPYNNTISKNIEDAERNELEFASENYKNDIPNEIDEHNNKMGRNMNKLNSNIKSKIFIFSKEISSVFALQYKSKTNIFTLDTILKQNEKLFPEYDNIKPYSYNLLNLKNNSNALLLPFSSSNDYLKNNDKKNLPWNFNYDENGTNANNSIAFQNYNNFIVQRLNNISINITSIEKDLRYLLLSIIFVFDKHKKIPMNYIFQMKTLLHEYQKTKQKFMICLRGLNHNKNINIFSNHNDIRDTDIKHYGYNDYDYINKEMDAIDEPIHICEYTNKFIDLSFEGKEKCIDYCSMLNIWDKIFNNYTNHDDCLLLSNLYRILNSTYPLTNKDFNRIIDGIFLKNNESMLIKRRRKPNEGSRNHDLTEFSSQKHKKSWYWNIFYAITLVIVIPFIFIYRLFKKQTNNKNNNKIIMRKKKITDYDEDSNDTYDDELLNIDKVLLKRNKRKLANILKENGISSLNKTELEKYMKKSLKKAQDIEQLTLVDILARHARDSDSDSNFYDIHDGKYNLYPYYYSGQESKYSLPNMHYIDLSKSNSGETNKYDLNGNNLFYMHRRRAASQDVTYKQSFIVKKRVRSNYKLGNKYNKRNYTDYEKDKKNSSIKERNINEKAFDKSDFINFLKNFNKKFMKKNPFVDHLMKNNKTDSNNEFNNDNKEKSKYLYNEKYNLNSADEENKSPYAKKYSDEKKNRSKSSKYIENTQSNNNDNTNGNMNVGNHINNDKMNNKGSSARNLSIIQTSHIPYDAPLADFLENGRFTRTFQNISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVNSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMDIIPKEIQNTLKKNKDPFKKVCNKNKKDNDYSSDCTVSSGENNKFDLKNYKKVITKKNSPKLKFYSDNDTPYNKRKNINQKNSFLNDKNLSDNIYIIENNKKKKKKKKKKKKIIYKEKKKGNIGINEDNKYSTFYEQNNPNNFSSTLQEYDPFGYGYLSENERDLIVFADNDESNGSGHSKKNDNDERKSLNNQNGIYNTGGDISKNGNVIHDDSNMLACQQSDKNSMTIKNTQGTSINGTINRNTISDETGTQGTNNNPKYSIDYHIDAIVKPKGESFTWVEKSPSNKYKKDSLDIINRNRKLIEEKNKKEKGQEKEKYKLKMNGELEKKENANKIKYYKKKNVGPEFSIVLLLQMEFCKGFTLRRWLDRSSRSDKPLYFTYGDKNTNHPLEFDLFKQLIKGLKDIHSTCFIHRDLKPENIFVDLDTYILKIGDLGLVRFIEEKKRENDLNNIDNFKDNIYTEINHNTITSQISLKGQMIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFNTIMERYKTLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADLYNKIKVLLDPHLTDFTFSFNDINNDDLEYTGNRNVINSTNPNGDIKENVNQNNLVDDKGNNNIINGNEVDH

Plasmodium berghei (strain Anka)

FUNCTION: During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition (PubMed:29241041). Plays a role in trophozoite differentiation into schizonts (PubMed:29241041). {ECO:0000269|PubMed:29241041}.

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:29241041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:29241041}; 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:29241041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:29241041};

ATP-binding;Endoplasmic reticulum;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Protein synthesis inhibitor;Reference proteome;Serine/threonine-protein kinase;Transferase;Transmembrane;Transmembrane helix

negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]

cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]

ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29241041}; Multi-pass membrane protein {ECO:0000255}.

IPR011009;IPR000719;IPR008271;

1.10.510.10;

A0A509APX1

MKETDKIKSEVLNLMQLDGKREHINKNNKLYRKVIINPTSEDDLQKFCKNYFRIYQFSLYNFIRRLISLDAVIVYTLFMTVYIFSEISQGITKKYLFVDTAISLFLNIGILVVIESLFELKLLKDIKNANSQHYLRIVPKMSYFEKVMTKDIKVGNIIRVFQGEEFPADVVILYSKKNTNAVVDSFKIDGLYNKSIKYPVEKYKIDRDYLKMLSEINGVIKCELPNKNVFCFQGTYKLDKHPRSLHLSYENFALQSSILKGAEYIDGVVVYTGADTKKNLNIPRKIEENMTFCIKMNNVVYYLIFMYILFVLLSIIIKAIFYRKGKLLENSNDTFFTVLEDFIGLYILVLPVMLYSEKSLIYIIQSLKIERDTRMNKDENSNNTKVFNKNKNDALGTVDIIATARNGVLVNKKEILVSCTINNVLYSKKKFIISDEFLKLPSLNILDAERTNVSELLNLDERIFKDPENIFFPSRDFNNFLKILGNNTNPIYDPINGDFSKILKEIYRNYLNEEFLYKKIKLSSSVKSLLDNGYNQFLEDCESSYDCKEIIEDGLKNNEQSEKIEEFILGICACNRIIIYNEKFGDIEMKDNINEKSTSEHMNYDKDREVENIESENKYAVDSDGEENMNTIEHEDICLFNTSKNIGFHIYCYKKCLFFYNLKNICKEYYIICFHDFLRSNNYTMCILKNKKELDKGILYIRGYDFNILPYLCKNKNDINKIKKTIKIHTANYLKVILICKKNITNEDIAKYIYLKSVRSKFSFKFFDIIKTFFLYDLECIGIIGLKNDLNDGVVETFNDINNFDIRSWIFTNDSSKNTYLTALQCNLITPNSNLFIINFLNPDHSDEETVANYLFNNFLFSMENMKSRSYAIAINEMSLKNIMRSRYALKVFLCIIMRATVVLFCKLNNETKGKIISKFLSYTTPKLTVLGVGSTLNDAYLLKNTTISVCLTLNKQVNALYSISDYAMEEFKYVGELLILGRLNRFSLCRAFLWIIYLKVMIGSFYFFHNFDNFFSGSSISSILYSQTAFAIFHYSLIVAFASYEIDIPYKFIRNFPYIYQLARRKYFLNNTIIFLNIVESIFSSFISYYILRGNLFNLITHRKFTFHIFVLNFFLISEKILLFSKTWHIFFFIMTIIIVSILFIYINIYTLVDCLITGKCEFSLFDPEDSYFWISLLPILYINFIIDKFMKFVKNKIYPDITYHLSNTLKIETQEKFATNNKREEVITDKNIEKLAPVPKSYIIKEDNAYYGKSKKNKYIFDTLRKIIDIKIKYRNQQLNLEYKTYEKRNKLKLRIIILLLFIIFLITFTIQIIISKFIEKKLHSLSYLTVIYYIVAVLYLIKILIRNKTNYTYFYIIGKLLLVIGYLLEISENSVNNIINMLVTYSFTVCYIFFISFKILEGLVMCIIILSIAIWVYYHKNNNLNAMCTDFCDNPYTSLDNLEYINISCICKQQIFTFLICTLSFTLICLFMKYYEIYYLKKKFLTRYKQKVNLGKQIEILHTMLPSFLVEYLLVSDPKADGIMVGKNISGEDRGIISVIFCDIDDFQTMVSTLEPHTLVQTLDNLYLYFDKCIKYFNCIKIETVFESYLAASGLSEKKNNCVHKIKYDTKCAIKMAIAQLSAKYYISYKVLDTLSNNKDSNSIFPIESKYIYKNISLRIGIHTGKAISGVIGSVKPQYSLFGDTVNTASRMKSTSLKDHIHVSYDTYKYLKDDKTLVWKERSIFIKGKGEMKTYLLVDILDNSKKDHTKALEESTSSIFRSNDEIVNKSELITKEKEFDKIEMPDKSEIIDETKKIFKKSEKPSTKKKKIKKENAKEKNINIKMKEMGEILNNYDKEKVYNCNKSDDGSNSIGQNDFLYSTKNYNYKKSKYLDLERLSTNKSFRRNVLAYNFESPINLPPKIGDNTKRNYDSDNFFTSPYIIDKNEKDEIRDTTNKALYIKKSKNIINRMREDSIDFKDEFSKENDKIKEYIKERITYRQKVTPNYFNFNNMSKYSNAFKKKKKKKKDIQKKYTYRQKTSFYNFLNKNDIINYNYSSEFEYFIDPKMKNKKPINFNNLFAKIYKKKLSLLNIKNEPINIKKKNIKNKSRDRIIFSSRRDEEHDDNQKMNKKLFSRTYAQKAEQTSHENIFTEMINDNFLKKEDKEQCEIRNENRCPTVFLIKRNKTTININKNRVLKRIFKDIITRKKIKRNRILKNKKLNYVNKNDNLGKKYEILNNICLVHKRAMTFVQYNTEDEEKKRTKRFHKNDEIFGSDMNISRNLNGSNSNIQNINRRSKNKAEDDLFIRNKVNLNNIKNNINLRKNIYKTDERGMQYNDLKGYDKKKNTEENNEDKEKKIEYDSNENIKNGFPKNEDKMIMKKRMISKRISFYSLKEYEKGDSFKSYDNSSCGIKSKKTNSIISDEEMNEYFNYNTEFNSNRNKNKQNKEFSLASKVNNIFKNIFKKNYISDKLKSGKYNTMSNSKSGQTNITTDNKKSQIKKNGDVNKANTNVSNKNSDFVTNFDNYNKNILKKLTSTLQINRKTSYFNRFYYKFKDEELEEEYTREYYQEIINIDLTKKLIIIFVISELILSLCNVIELSYYENKETPNDFIVIIWLIRSIYLFTITFIWLLLKTKLKEYKDNSSKMMWTTFILNIFLSSWGIIMIDLACIHYSNLVGNSRERSIFFMKDATELIISMQLIFVKNMLFKHKFFFFVFFFVFLMYSFFKLFVIHVCELRICCSILLILSINILYFWYSEYLDRTQYIIKRKRNRMERTSHDFLTRILPRQVLEEYQNDNLQLTYKHEKIAFLFADIVGFTKWSKTAAPKNVLKLLQKLISKIDKDTIKLGLYKLFTIGDAYVATSQPNASITDQTEAADGIISIFKLAKLILHNINTIKIQFNKHDFNMRIGLHYGSCVGGIIGSVRIRYDMWGLDVLIANHIESNGIPGEIVCSEQFKNFFLENEPHAKLNFWHYKTISINDKDIKIYVVEDKNYEEDYDPKIINYETLLKLREQNKVKG

Plasmodium berghei (strain Anka)

FUNCTION: Catalyzes the synthesis of the second messenger cGMP from GTP (By similarity). Probably by regulating cGMP production, required for ookinete gliding motility, which is necessary for the ookinete to traverse the midgut epithelium of the mosquito (PubMed:17030505, PubMed:19779564). {ECO:0000250|UniProtKB:Q8IDA0, ECO:0000269|PubMed:17030505, ECO:0000269|PubMed:19779564}.

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:0000250|UniProtKB:Q8IDA0};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IDA0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8IDA0}; Note=Binds 2 magnesium ions per subunit (By similarity). Is also active with manganese (in vitro) (By similarity). {ECO:0000250|UniProtKB:P30803, ECO:0000250|UniProtKB:Q8IDA0};

cGMP biosynthesis;Glycoprotein;Lyase;Magnesium;Membrane;Metal-binding;Reference proteome;Transmembrane;Transmembrane helix

intracellular signal transduction [GO:0035556]; phospholipid translocation [GO:0045332]; positive regulation of cell motility [GO:2000147]

plasma membrane [GO:0005886]

ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; guanylate cyclase activity [GO:0004383]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

DOMAIN: The N-terminus contains a P-type ATPase-like domain which is required for guanylate cyclase activity. {ECO:0000250|UniProtKB:Q8IDA0}.

IPR001054;IPR023298;IPR008250;IPR036412;IPR023214;IPR029787;IPR032630;

2.70.150.10;3.40.50.1000;3.30.70.1230;

A0A509AQE6

MCEHKANNKNDGEFVNLKEKNENNHCGNTKSTIADCDDDYSIITLCTKCLSTKTEVNKNKIILDSKALKDSRTKRRSSVNINIDILNNNLNLSPYFDRSQIVQETILMNNDDLEKLYELDKYKLGKGSYGNVVKAINKKTGQAKAIKIIDKKRINNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCTGGELFDKIVKHGSFSEYETYKIMKQIFSALAYCHSKNIIHRDLKPENILYVDSSDDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILKGKYDKKCDIWSSGVIMYILLCGYPPFNGKNNDDILKKVKKGEFVFDSNYWSKISLDAKELICECLNYNYKERIDVHKIVNHKWFIKFKNYNHITINKHLSKELIEKFKKFHKLCKIKKLAITCIAYQLNKKKFGKMKKTFEAFDHNGDGVLTISEIFQCLKVGDNEIDRDLYYLLKQLDTDGNGLIDYTEFLAACLDHSILEQDAVCRNAFKIFDANGDGIITKDELLNVLSFSNDQMPFSKEIIENVIKEVDANNDGYIDYDEFYKMMSGRQS

Plasmodium berghei (strain Anka)

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 (By similarity). Plays a central role in host erythrocytes and hepatocytes infection cycles (PubMed:32866196). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK4 (PubMed:32866196). Involved in merosome egress from host hepatocytes, probably together with CDPK4 (PubMed:32866196). Required for the release of hepatic merozoites from merosomes in the host blood stream (PubMed:32866196). During the asexual blood stage, required for merozoite egress from host erythrocytes by triggering microneme secretion (By similarity). Phosphorylates transporter NPT1 at late schizont stage (By similarity). {ECO:0000250|UniProtKB:A0A5K1K8H0, ECO:0000269|PubMed:32866196}.

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:0000250|UniProtKB:A0A5K1K8H0}; 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:0000250|UniProtKB:A0A5K1K8H0};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A5K1K8H0};

ATP-binding;Calcium;Cell membrane;Cytoplasm;Cytoplasmic vesicle;Kinase;Lipoprotein;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell motility [GO:2000147]

cytoplasmic vesicle [GO:0031410]; microneme membrane [GO:0033163]; nucleus [GO:0005634]; plasma membrane [GO:0005886]

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]; mitogen-activated protein kinase binding [GO:0051019]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cell membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Note=During the late stages of schizogony, localizes to the cytoplasm in immature daughter merozoites, co-localizes with AMA1 to a subset of micronemes and to the apical region in maturing daughter merozoites, and near the plasma membrane in mature daughter and free merozoites. {ECO:0000250|UniProtKB:A0A5K1K8H0}.

PTM: May be palmitoylated. {ECO:0000250|UniProtKB:A0A5K1K8H0}.; PTM: Autophosphorylated in vitro. {ECO:0000250|UniProtKB:A0A5K1K8H0}.

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:Q8IBS5}.

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

1.10.238.10;1.10.510.10;

A0A517FNB9

MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGKEGECGLSWDQYKQMEFTHCVINESLRLGNVVRFVHRKAIQDVQYKGYDIPCGWKVLPVFAAVHLDSTLYSDPHRFNPWRWQSSSSKTTAANFMPYGGGLRLCTGSELAKLEMAVFLHHLVLNYQWKLAEPEQAFAYPFLDFPKGLQIKVRAIT

Paris polyphylla (Daiswa polyphylla)

FUNCTION: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation. {ECO:0000269|PubMed:31324795}.

1.14.14.-

CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:31324795}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69840; Evidence={ECO:0000269|PubMed:31324795};

PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}.

Brassinosteroid biosynthesis;Cholesterol metabolism;Iron;Lipid biosynthesis;Lipid metabolism;Membrane;Metal-binding;Oxidoreductase;Steroid biosynthesis;Steroid metabolism;Sterol metabolism;Transmembrane;Transmembrane helix

brassinosteroid biosynthetic process [GO:0016132]; cholesterol metabolic process [GO:0008203]; steroid biosynthetic process [GO:0006694]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]

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

IPR001128;IPR002401;IPR036396;

1.10.630.10;