UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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Q9TSK0 | MWQLVFLTLSCDLAVATAHSGSRKGMDIAAGKKQYQVQHGACSYTFLLPETDHCRSPSSAYVPNAVQRDAPLDYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEISKLQDKNSFLEKKVLDMEDKHIVQLRSIKEEKDQLQVLVSKQNSIIEELEKQLVTATVNNSVLQKQQHDLMETVNNLLTLMSTSNPSYSLLAKDEQIIFRDCGEAFKSGLTTSGVYTLTFPNSTEEIKAYCDMETGGGGWTVIQRREDGSVDFQRTWKEYKVGFGNPSGEHWLGNEFVSQVTGQKRYVLKIHLRDWEGNEAYSLYDHFYLSNEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDADNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF | Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Involved in the regulation of lymphangiogenesis. Interacts with TEK/TIE2, competing for the same binding site as ANGPT1. Interacts with ITGA5. Found to be expressed throughout the ovarian cycle. Overexpressed during luteolysis, this could reflect the regression of capillaries that had developed pericyte contact in the midstage corpus luteum. The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor. |
A0A8J8 | MWQIVFFTLSCDLVRAAAYNNFRRSMDSIGRRQYQVQHGSCSYTFLLPETDNCRSPGSYVPNAVQRDAPLDYDDSVQRLQVLENIMENNTQWLIKLENYIQDNMKKEMVEMQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLDMEDKHIVQLRSIKEEKDQLQVLVSKQNSIIEELEKQLVTATVNNSVLQKQQHDLMETVHSLLTMISPSKSPKDTFVAKEEQIIYRDCAEVFKSGLTTNGIYTLTFPNSTEEIKAYCDMETSGGGWTVIQRREDGSVDFQRTWKEYKVGFGNPSGEHWLGNEFVFQVTNQQPYVLKIHLKDWEGNEAYSLYEHFYLSGEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDADNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKGTTMMIRPADF | Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Involved in the regulation of lymphangiogenesis. Interacts with TEK/TIE2, competing for the same binding site as ANGPT1. Interacts with ITGA5. The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor. |
Q9P2Y7 | MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF | Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473,PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473,PubMed:9204896). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (PubMed:15284220, PubMed:19116766, PubMed:19223473,PubMed:9204896). Involved in the regulation of lymphangiogenesis (PubMed:32908006). Interacts with TEK/TIE2, competing for the same binding site as ANGPT1 (PubMed:9204896, PubMed:12427764, PubMed:15284220, PubMed:19223473, PubMed:32908006). Interacts with ITGA5 (PubMed:32908006). The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor. The disease is caused by variants affecting the gene represented in this entry. Angiopoietin entry |
Q9D2D2 | MWQIIFLTFGWDLVLASAYSNFRKSVDSTGRRQYQVQNGPCSYTFLLPETDSCRSSSSPYMSNAVQRDAPLDYDDSVQRLQVLENILENNTQWLMKLENYIQDNMKKEMVEIQQNVVQNQTAVMIEIGTSLLNQTAAQTRKLTDVEAQVLNQTTRLELQLLQHSISTNKLEKQILDQTSEINKLQNKNSFLEQKVLDMEGKHSEQLQSMKEQKDELQVLVSKQSSVIDELEKKLVTATVNNSLLQKQQHDLMETVNSLLTMMSSPNSKSSVAIRKEEQTTFRDCAEIFKSGLTTSGIYTLTFPNSTEEIKAYCDMDVGGGGWTVIQHREDGSVDFQRTWKEYKEGFGSPLGEYWLGNEFVSQLTGQHRYVLKIQLKDWEGNEAHSLYDHFYLAGEESNYRIHLTGLTGTAGKISSISQPGSDFSTKDSDNDKCICKCSQMLSGGWWFDACGPSNLNGQYYPQKQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF | Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity). Involved in the regulation of lymphangiogenesis (PubMed:32908006). Interacts with TEK/TIE2, competing for the same binding site as ANGPT1. Interacts with ITGA5. Expressed only at sites of vascular remodeling. The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor. |
Q8I1F2 | MSCFSQAINPITGQNSWQERGDDYDYHLEVANAGFGDMLHDWERNQKYFAALKKTIAGMREAGREVHVLDIGTGTGILSMMAVEAGADSVTACEAFLPMANCAERILAANGAGDKVRLIRKRSTEIQVGEDMPRKANLLVAELLDTELIGEGAIGIYNHAHAELLTEDALCIPARARCYAQVAQSPLAAQWNSLKTIANLDGEPLLHPPEQLKSCQGEAALHDVQLSQLPSSAFRPLTDPVEIFQFDFQRKQEREKQRAQLLKLQSKQPGAAELVFYWWDIQLDDGGEILLSCAPYWAHPQLKELAAEKGNDHPLPNVVPWRDHWMQAIYYIPKPLQLVEAGKSFHLSCHHDEYSLWFDAREEAPTKSVRRHTCTCDLHMTYSRSRIGQINQSPRNKRYLRYLEESIEAEKSNVLVLGNGCLLGLASSALGAASVLLHEPHRFSRRLLESIVKHNQLKNVQFLDKVEELEDSQLAALTHIFAEPYFLNAILPWDNFYFGTLLTKIKDRLPQNVKISPCSARIYALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPCRALSEPQEVLNVEFSNFSQEHSLKGSIELKHSGTCNGVALWVDWQLVEDNSPRSIVSSGPSEPVVPGEFVKWDMFVRQGVHFPRRPKEPITHLEWSTAFKPELGELNFTFGQKKL | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4JWL5 | MASFGQVINPMTGENTWQERDENYDYHQEVANAGFGDMLHDWERNQKYDAALRKTIAAMREAGREVHVLDIGTGTGILAMMALRAGADTVTACEAFMPMANCAQRILNANGYGDRVRLIRKRSTDIEMGVDMPHRANLLVAELLDTELIGEGAIGIYNHAHNELLTADALCIPARATCYAQAAQSALATQWNSLKMLASLDGDILLKPPAQLLQCSGEAALHDVQLSQLPIDSFHVLTAPTPIFQFDFQRKQAREQQRENILRLQIVRPGSVELIFYWWQIELDDRGEQLLSCAPYWAHPELAQLQRSNSSKPLANVVPWRDHWMQAIYYIPKPLQLHTAGEQFYLRCYHDEYSLWFDAHQTEPPSQPARRHCCTCDLHMTYTRNRIGQLNQGTRNKRYLRYLEQAVHAKESAHLLVLGDGCLLGLASSALGAGSVRCLEPHRFSRRLLGAIAKHNQLKNVSFVESVQQLQPIELAAITHIFAEPYFLNSILPWDNFYFGTLLLQLLEQIPALSVQISPCAARIYALPVEFLDLHKIRTPIGSCEGFDLRLFDDMVQRSAEQAVALVEAQPLWEYPCRALAQPQQLLNVNFDNFGEDKHSHGCLQLTASGDCNGVALWVDWQLAADESPRSIVSSGPSETVVPGQLVKWDMFVRQGVHFISQPTKDRRQTDAGKRQLDWSINFKPRLGELNFNFSLRSSSEKSE | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
Q8MYV1 | MSCFSHVMNPITGQNSWQERGDDYDYHLEVANAGFGDMLHDWERNQKYFAALRKTIAGMREAGREVHVLDIGTGTGILSMMALAAGADSVTACEAFLPMANCAEKILAANGAGDKVRLIRKRSTEIQVGEDMPRKANLLVAELLDTELIGEGAIGIYNHAHAELLTEDALCIPARARCYAQVAQSPLAAQWNSLKTIANLDGEPLLHPPEQLKSCQGEAALHDVQLSQLPSSAFRPLTDPVEIFQFDFQRKQEREKQRSQLLKLQSKQPGAAELVFYWWDIQLDDDGEILLSCAPYWAHPQLKELAAEKAKDHPLPNVVPWRDHWMQAIYYIPKPLQLLEAGKSFHLSCHHDEYSLWFDAREEAPTKSVRRHTCTCDLHMTYSRSRIGQLNQSPRNKRYLRYLEESIEAEKSNVLVLGNGCLLGLASSALGAASVLLHEPHRFSRRLIESIVKHNQLKNVQFLDKVEELEDSRLAALTHIFAEPYFLNAILPWDNFYFGTLLTKIKDRLPEGVKISPCSARIYALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPCRALSEPQEVLSVDFSNFGQEHSLKGSIELKHPRICNGVALWVDWQLVEDNSPRSIVSSGPSEPVVPGEFVKWDMFVRQGVHFPRRPKEAITHLEWSTVFKPLLGELTFSFGQKKL | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3. Expressed at low level in ovary. Death at pupal stage. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4KSL6 | MASFAQVINPMTGQNTWQERGDDYDYHQEVANAGFGDMLHDWERNQKYDAAIRKTIAGMRQAGKQVHVLDIGTGTGILAMMALRAGADTVTACEAFVPMANCAARILAANDAAHVRLIRKRSTDIVMGVDMPHRANLLVAELLDTELIGEGAIGIYNHAHEELLTDDALCIPARATCYAQVAQSPLASQWNSLKILPDLDGDILLRPPTQLLQCSGEAALHDVQLSQLPPHSFHVLSEPTQIFHFDFQRKQPLELMRENVVRVQLSRPGSVELVFYWWQIELDDAGEQLLSCAPYWAHPELEQLKATCKDKQRPLANIVPWRDHWMQAIYYIPKALHLHDAGEEFWLRCYHDEYSLWFDAHKEQPEKPARRHSCTCDLHMTYTRNRIGQLNQSIRNKRYLAYLEQAVQSKSAHVLVMGDGCLLGLASAALGAASVYCLEPHRFSRRLLESVVKHNQLKNVKFLDSLKQLEPNELDTITHIFAEPYFLNSILPWDNFYFGTLLLQLEQLHQKLPANVEISPCAARIFALPVEFLDLHKIRAPIVSCEGFDLRLFDDMVQRSAEQALSQVEAQPLWEYPCRALAQPQQLLSVDFANFGVEQSNHGSIKLTAEGNCNGIALWVDWQLSPNENPKSIVSSGPLEPVETGQYVKWDMFVRQGVHFINQTTAEKKYLNWSTQFRPLLGELNFNFSLNANREKSE | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4GA28 | MSCFSHVMNPITGENSWQEREDDYDYHQEVANAGFGDMLHDWERNQKYFAALRKTIKGMRAAGREVHVLDIGTGTGILSMMALKAGADSVTACEAFLPMANCAAKIFTDNGVGDKVQLIRKRSTDIKIGADLDMPQRANLLVAELLDTELIGEGAISIYNHAHAELLTDDALCIPARARCYAQVAQSPLASQWNSLKILPSLDGEALLRPPEQLKSCKGEAALHDVQLSQLPAGTFRLLTEPIEIFQLDFQRKEKREKQREKLVQLQASQPGAAELVFYWWDIQLDDQGEILLSCAPYWAHPELNELSASKEERVPVANVVPWRDHWMQAIYYVPKPPQLATAGQDFYLSCHHDEYSLWFDAMLEAPAKTVRRHTCSCDLHMTYSRSRIGQLNQAIRNKRYLRYLEATIVPKQSNVLVLGNGCMLGLASAALGAASVQLHEPHRFSRRLIDSIVQHNELKNVKYVENVEQLEDTELIALSHVFAEPYFLNAILPWDNFYFGTLLMKLKDKLPEKVEISPCEARIFALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPSRALAEPQQLLSVDFANFNVEHHLQGSIELTQSGVCNGIALWVDWHLDKTNNPKSIVSTGPSEAVVPGEFVKWDMFVRQGVHFPRKPTDLSGRVAWSTDFKPLLGQLNFGFSQEKR | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B5DZN7 | MSCFSHVMNPITGENSWQEREDDYDYHQEVANAGFGDMLHDWERNQKYFAALRKTIKGMRAAGREVHVLDIGTGTGILSMMALKAGADSVTACEAFLPMANCAAKIFTDNGVGDKVQLIRKRSTDIKIGADLDMPQRANLLVAELLDTELIGEGAISIYNHAHAELLTDDALCIPARARCYAQVAQSPLASQWNSLKILPNLDGEALLRPPEQLKSCKGEAALHDVQLSQLPAGTFRLLTEPIEIFQLDFQRKEKREKQREKLVQLQASQPGAAELVFYWWDIQLDDQGEILLSCAPYWAHPELKELSASKEERVPVANVVPWRDHWMQAIYYVPKPPQLATVGQDFYLSCHHDEYSLWFDAMLEAPAKTVRRHTCSCDLHMTYSRSRIGQLNQAIRNKRYLRYLEATIVPKQSNVLVLGNGCMLGLASAALGAASVQLHEPHRFSRRLIDSIVQHNELKNVKYVENVEQLEDTELIALSHVFAEPYFLNAILPWDNFYFGTLLMKLKDKLPEKVEISPCEARIFALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPSRALAEPQQLLSVDFANFNVDHHLQGSIELTQSGVCNGIALWVDWHLDKTNNPKSIVSTGPSEAVVPGEFVKWDMFVRQGVHFPRKPTDLSGRVAWSTDFKPLLGQLKFGFSQEKR | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4I8G2 | MSCFLQVMNPITGQNSWQERGDDYDYHLEVANAGFGDMLHDWERNQKYFGALRKTIAGMREAGREVHVLDIGTGTGILSMMALAAGADSVTACEAFLPMANCAEKILAANGAGDKVRLIRKRSTEIQVGEDMPRKANLLVAELLDTELIGEGAIGIYNHAHAELLTEDALCIPARARCYAQVAQSPLAAQWNSLKTIANLDGEPLLHPPEQLKSCQGEAALHDVQLSQLPISAFRPLTDPVEIFQFDFQRKQEREKQRAQLLKLQSKQPGAAELVFYWWDIQLDDGGEILLSCAPYWAHPQLKELAAEKAKDHPLPNVVPWRDHWMQAIYYIPKPLQLLEAGKSFHLSCHHDEYSLWFDAREEAPTKSVRRHTCTCDLHMTYSRGRIGQLNQSPRNKRYLRYLEESIEAEKSNVLVLGNGCLLGLASSALGAASVLLHEPHRFSRRLLESIVKHNQLKNVQFLDKVEELEDSQLAALTHIFAEPYFLNAILPWDNFYFGSLLTKIKDRLPEGVKISPCSARIYALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPCRALSEPQEVLSVDFSNFGQEHSLKGSIELKHTGICNGVALWVYWQLVEDNSPRSIVSSGPSEPVVPGEFVKWDMFVRQGVHFPRKPKDAVTHLEWSTDFKPLLGELNFSFGQKKL | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4QI55 | MLRNFLKSRFLAPRGMSCFSQVMNPITGQNSWQERGDDYDYHLEVANAGFGDMLHDWERNQKYFAALRKTIAGMREAGREVHVLDIGTGTGILSMMALAAGADSVTACEAFLPMANCAEKILAANGAGDKVRLIRKRSTEIQVGEDMPRKANLLVAELLDTELIGEGAIGIYNHAHAELLTEDALCIPARARCYAQVAQSPLAAQWNSLKTIANLDGEPLLHPPEQLKSCQGEAALHDVQLSQLPSSAFRPLTDPVEIFQFDFQRKQEREKQRAQLLKLQSKQPGAAELVFYWWDIQLDDGGEILLSCAPYWAHPQLKELAAEKAKDHPLPNVVPWRDHWMQAIYYIPKPLQLLEAGKSFHLSCHHDEYSLWFDAREEAPTKSVRRHTCTCDLHMTYSRSRIGQLNQSPRNKRYLRYLEESIEAEKSNVLVLGNGCLLGLASSALGAASVLLHEPHRFSRRLLESIVKHNQLKNVHFLDKVEELEDSQLAALTHIFAEPYFLNAILPWDNFYFGTLLTKIKDKLPEGVKILPCSARIYALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPCRALSEPQEVLSVDFSNFGQEHSLKGSIELKHTGICNGVALWVDWKLVEDNSPRSIVSSGPSEPVVPGEFVKWDMFVRQGVHFPRKPKDAVTHLEWSTDFKPLLGELNFSFGQKKL | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4LPB6 | MASFSQVINPMTGQNTWQERGDDYDYHQEVANAGFGDMLHDWERNQKYYAALRKTIAAMRKAGKEVHALDIGTGTGILAMMALRAGADTVTACEAFMPMANCAARILAANDAAQVRLIRKRSTDIQMGIDMPHRANLLVAELLDTELIGEGAISIYNHAHQELLTDDALCIPARATCYAQVAQSPLATQWNSLKVLPSLDGDILLRPPAQLMECSGEAALHDVQLSQLPPNSFHTLTEPAQIFQFDFQRKQPREQQREHVLRLQLSKPGSVELVFYWWQIELDDAGEQLLSCAPYWAHPELQQLQKSFKDADRPLPNIVPWRDHWMQAIYYIPKPLQLHQAGEQFWLRCYHDEYSLWFDAHKEQPEQPARRHSCSCDLHLTYTRNRIGQLNQGTRNKRYLAYLEQAVQQAKPAHVLVIGDGCLLGLASSALGACSVRCLEPHRFSRRLLESVAKHNKLKNVRFLESLQQLEPEELNTLTHIFAEPYFLNAILPWDNFYFGTLLLQLQQQQKLSESVEISPCAARIYALPVQFLDLHKIRTPIISCEGFDLTLFDEMVQRSAKQALSQVEAQPLWEYPCRALAEPQLLLSVNFANFGVEQHNQGCLELTAKGNCNGVALWVDWQLAANNSSKSIVSTGPLEPIVPGQFVKWDMFVRQGVHFPSQTDDQTHLKWSTTLRPLLGELTFNFSLQASHEETK | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4MNL1 | MSSFSQVRNPITGQATWQENADDYDYHQEVANAGFGDMLHDWERNQKYYAAIKKTIKRMQADGREVHVLDIGTGTGILSMMALKAGADSVTACEAFLPMANCAAKIMTANGADKIQLIRKRSTEIQIGVDMARRANLLVAELLDTELIGEGAIGIYNHAHQELLTKDALCIPARARCYAQVATSSLAKQWNGFKLMANLDGETLLRVPPQLNECKGDAALHDLQLSQLPTESFRLFSKPVEIFEFDFQQHLEPIQKQRNKVVPLQASQPGSADMVFYWWDIDLDHESEIVLSCAPFWAHPDKDKHVAGEDKPLANAIPWRDHWMQAIYYIPKPLHLSNTKETFYLSCHHDEYSLWFDAQLKEPAESIERHHCTCDLHLINPRSRIGQLNQSPRNKRYLNYLEETTTKDSQFLVLGNSCFLGLATCGLGAASVEIYDSNSLSRRLLDSFIKFNKLENVSLLEKLEDVQDHSKLTHIFAEPYFINSILPWDNFYFGTLLLSLKDKLSEGTQISPCAARIFALPMEFLDLHKIRAPVGNCEGFDLSLFDEMVKDSADKAVSSVEAQPLWEYPGRALAQPQEILRVDFANFNQELHQQGSIELIRSKECNGIALWVDWQLYSSESPKAFVTSGPSQPIEIGKFVKWDMFVRQGVHFPQTRTTNATQVEWQIDFKPFLGELNFKFDLKSI | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B4P925 | MSCFSHVMNPITGQNSWQERGDDYDYHLEVANAGFGDMLHDWERNQKYFAALKKTIAGMREAGREVHVLDIGTGTGILSMMAVEAGADSVTACEAFLPMANCAERILAANGAGDKVRLIRKRSTEIQVGEDMPRKANLLVAELLDTELIGEGAIGIYNHAHAELLTEDALCIPARARCYAQVAQSPLAAQWNSLKTIANLDGEPLLHPPEQLKSCQGEAALHDVQLSQLPSSAFRPLTDPVEIFQFDFQRKLEREKQRAQLLTLQSKQPGAAELVFYWWDIQLDDGGEILLSCAPYWAHPQLKELAAEKGKDHPLANVLPWRDHWMQAIYYIPKPLQLVEAGKSFHLSCHHDEYSLWFDAREEAPTKSVRRHTCTCDLHMTYSRSRIGQINQSTRNKRYLRYLEENIEAEKSNVLVLGNGCLLGLASSALGAASVLLHEPHRFSRRLLESIVTHNQLKNVQFLDKVEELEDSQLSALTHVFAEPYFLNAILPWDNFYFGTLLTKIKDRLPESVKISPCSARIYALPVEFLDLHKIRAPVGSCEGFDLRLFDEMVERSAEQAVSLVEAQPLWEYPCRALSEPQEVLNVEFSSFTQEHSLKGSIELKHPGTCNGVALWVDWQLVEENSPRSIVSSGPSEPVVPGEFVKWDMFVRQGVHFPRRPTGGITHLEWSTDFKPVLGELNFSFGQKKL | Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
Q9H9L0 | MKIFCSRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNVKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPEGDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVESGRMWSWNKLFPIHVQTSLGEQVIVPPVDVESCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSIDFSKQVSSSAACHSRRFEPLTSGRAQVVLSWWDIEMDPEGKIKCTMAPFWAHSDPEEMQWRDHWMQCVYFLPQEEPVVQGSALYLVAHHDDYCVWYSLQRTSPEKNERVRQMRPVCDCQAHLLWNRPRFGEINDQDRTDRYVQALRTVLKPDSVCLCVSDGSLLSVLAHHLGVEQVFTVESSAASHKLLRKIFKANHLEDKINIIEKRPELLTNEDLQGRKVSLLLGEPFFTTSLLPWHNLYFWYVRTAVDQHLGPGAMVMPQAASLHAVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPLWEYPCRSLSEPWQILTFDFQQPVPLQPLCAEGTVELRRPGQSHAAVLWMEYHLTPECTLSTGLLEPADPEGGCCWNPHCKQAVYFFSPAPDPRALLGGPRTVSYAVEFHPDTGDIIMEFRHADTPD | Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine Homodimer and heterodimer (By similarity). Interacts with CTCFL (By similarity). Interacts with PRMT5 and SNRPD3. The disease is caused by variants affecting the gene represented in this entry. May be involved in etoposide-induced cytotoxicity, a chemotherapeutic agent frequently used for testicular cancer and small-cell lung cancer that can cause cytotoxicity in the treatment of other cancers. Down-regulation confers increased sensitivity to the Top1 inhibitor camptothecin (CPT). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. Truncated N-terminus. |
Q6PG80 | MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAEAAVKIVERNGFSDKIKVINKHSTEVTVGPDGDLPCRANILITELFDTELIGEGALPSYEHAHKHLVQEDCEAVPHRATVYAQLVESRRMWSWNKLFPVRVRTSLGEQVIVPPSELERCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSVDFSKQVSSSAACHSRQFVPLASGQAQVVLSWWDIEMDPEGKIKCTMAPFWAQTDPQELQWRDHWMQCVYFLPQEEPVVQGSPRCLVAHHDDYCVWYSLQRTSPDENDSAYQVRPVCDCQAHLLWNRPRFGEINDQDRTDHYAQALRTVLLPGSVCLCVSDGSLLSMLAHHLGAEQVFTVESSVASYRLMKRIFKVNHLEDKISVINKRPELLTAADLEGKKVSLLLGEPFFTTSLLPWHNLYFWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPHPLWEYPCRSLSKPQEILTFDFQQPIPQQPMQSKGTMELTRPGKSHGAVLWMEYQLTPDSTISTGLINPAEDKGDCCWNPHCKQAVYFLSTTLDLRVPLNGPRSVSYVVEFHPLTGDITMEFRLADTLS | Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity). L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine Homodimer and heterodimer. Interacts with PRMT5 and SNRPD3 (By similarity). Interacts with CTCFL. Present in undifferentiated embryonic stem and germ cells; expression is lost when cells differentiate. In the developing testis, it is expressed at all stages. Present in all cells within the developing tubule, including gonocytes and spermatogonia (at protein level). It the developing kidney, it is confined to the nephrogenic zone in the cortical region, where the tips of the ureteric bud induce de novo formation of epithelia in the metanephric mesenchyme and early glomeruli. Expression is around 8-fold lower in adult kidneys. Mutants, shortly after birth, display significant reduced body size, reduced weight and shortened fifth metatarsals. They are subviable with about 45% of the expected number of mutant pups at P14. Surviving adult mice exhibit increased fat mass, reduced length and limb abnormalities. They also have reduced bone mineral content and density. Knockout mice show sexually dimorphic phenotypes, including changes in bone mineral content, bone mineral density and fifth metacarpal length that are only significant in females. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. Truncated N-terminus. |
B8B1M3 | MPSCCCLLGLGFPSPPSALRILRRRMASRAFQLRLNPLTGDSEWLVVEEEEEEDHHPTPPPKQLLATTSYLDMLNDSARNRAYRRAIEAAVTDPSSRVLDIGAGTGLLSMMAARALAAVGGETRGGSVSACESYLPMGKLMRRVLRANGMENRVKVFHKRSDELKVGDDLDSPADILVSEILDSELLGEGLIPTLQQAYDMLLAKNPKIVPYRATTYGQLVESTFLWKLHDLHNNEANAADGVWLTPGEMERIVSVKPQQHAMQCDALEDEIRLLSEPFKVFEFDFWKRPDSHREANIKIQTTRDGYVHAIISWWVLQLDSAGSIFYSTAPRWARQSSSEGPQRDMKDWCDHWKQCVWFMQGKGIPATEDQVLSLRARHNQTSISYQLNINDEACDRSSKGDHLTLLPERIALYGDKDWRSALINTIKNALTVKSSPTCVVADDSMFLALLISSMSPTSKVIAMYPGLRDKGAAYLRSVADANNFSIDQIQVIGKRASSITADDLKHKKVNLLVGEPFYLGSEGMLPWQNLRFWSVRTLLDSMLSEDAFIMPCKGILKLCAMSLPDLWRSRSSLKDVEGFDHSVVNETLGACGYLPGDQQGPCLPYYVWQCGYTKKLSKVYSLMDFNFSEPIHSCFGKTKIEFSHDGTCHGFAVWIDWVLDERKSVVLTTGPDNRYWKQGVQLFGKPVEVNPGKSVMHVEASFDPSTGEITFSSSSTTCS | Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
B9FR35 | MPSCCCLLGLGFPSPPSALRILRRRMASRAFQLRLNPLTGDSEWLVVEEEEEEDHHPTPPPKQLLATTSYLDMLNDSARNRAYRRAIEAAVTDPSSRVLDIGAGTGLLSMMAARALAAVGGETRGGSVSACESYLPMGKLMRRVLRANGMENRVKVFHKRSDELKVRDDLDSPADILVSEILDSELLGEGLIPTLQQAYDMLLAKNPKIVPYRATTYGQLVESTFLWKLHDLHNNEANAADGVWLTPGEMERIVSVKPQQHAMQCDALEDEIRLLSEPFKVFEFDFWKRPDSHREANIKIRTTRDGYVHAIISWWVLQLDSAGSIFYSTAPRWARQSSSEGPQRDMKDWCDHWKQCVWFMQGKGIPATEDQVLSLRARHNQTSISYQLNINDEACDRSSKGDHLTLLPERIALYGDKDWRSALINTIKNALTVKSSPTCVVADDSMFLALLISSMSPTSKVIAMYPGLRDKGAAYLRSVADANNFSIDQIQVIGKRASSITADDLKHKKVNLLVGEPFYLGSEGMLPWQNLRFWSVRTLLDSMLSEDAFIMPCKGILKLCAMSLPDLWRSRSSLKDVEGFDHSVVNETLGACGCLPGDQQGPCLPYYVWQCGYTKKLSKVYSLMDFNFSEPIHSCFGKTKIEFSHDGTCHGFAVWIDWVLDERKSVVLTTGPDNRYWKQGVQLFSKPVEVNPGKSVMHVEASFDPSTGEITFSSSSTTCS | Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
Q5U4E8 | MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDKGQKALVLDIGTGTGLLSMMAVTAGADFCYAVEVFKPMAEAAVKIVEKNGFSDKIKVINKHSTEVTVGPDGDLPCRANILVTELFDTELIGEGALPSYEHAHKHLVQEDCEAVPHRATVYAQLVESKRMWSWNKLFPVRVQTGLGEQLIIPPSELERCPGAPSVYDIQLNQVSPADFTVLSDVLPMFSVDFSKQVSSSAACHSKQFVPLASGQAQVVLSWWDIEMDPEGKIKCTMAPFWAQTDPQELQWRDHWMQCVYFLPQEEPIMQGSPRCLAAHHDDYCVWYSLQRTSPDENNSAYQVRPVCDCQAHLLWNRPRFGEINDQDRTDHYARALRTMLMPGSICLCVSDGSLLSVLAHHLGAEQVFTVESSVASYRLMKRIFKVNHLEDKITVINKRPELLTSADLEGKKVSLLLGEPFFTTSLLPWHNLYFWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPQPLWEYPCRSLSEPRQILTFDFQQPIPQQPMQSRGVMELRRPGKSHGAVLWMEYQLTPDSTVSTGLMNPAEDKGDCCWNPHCKQAVYFLSATLDPSAPLDGPQSVSYAVEFHPLTGDITMEFRLADDTLN | Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine Homodimer and heterodimer. Interacts with CTCFL, PRMT5 and SNRPD3 (By similarity). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
Q582G4 | MPPKQHRHQKKDKNDNALQNTIGFVPPGATLASVSGYRPPDAFVNRIDRNIPVPARLRHTPVSLIEAVNDFHYAMMNDEERNNFYYEVLKKHVTPETGVLEIGAGSGLLSLMAAKLGAKWVVAVEGSEELAKLARENIRANNMEHQVKVLHMMSTELKSKHLPEPPDVLLSEIFGTMMLGESALDYVVDVRNRLLKPTTKIIPQFGTQYAVPIECDALHRISSVSGWRDLDLKHMMTLQDTVSIVFAKHYGIRMNSVNFRRLSDPIELFRVDFSSSNRNDIPRRKHFDVVAKESGTAHAMLFYWKVTDDEFVMSTDPEDTVNNFPRDMQWGQALQLLDASNGPLPTPVVFTEGKNYNFECNFSGDRVILHMQLCPESGNGEMTECEGKTT | Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. Present in large multiprotein complexes. Expressed during both bloodstream (BF) and procyclic insect (PF) life cycle stages. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. Compared to PRMT7 orthologs in other metazoans, it is shorter and lacks the C-terminal part. |
Q6PCI6 | MKVFCGRVNPTTGAMDWVEEDEHYDYHQEIARSSYADMLHDKDRNEKYYQGICAAVRRVKQRGQEAVVLDIGTGTGLLSMMAVTAGADCCYAIEVFKPMSDAAVQIVKANGFSDKIKVINKHSTEVTVGPDGDMKTKANILITELFDTELIGEGALPSYEHAQHNLMQETWEAVPHRATVFAQLVESTRLWSWNKLFPLNLETGDIKPHPELETCPGAPSVCDIQLSQLNPRDFKILSEVLCVFRVDFSCQVSSAPTSHPVHFTSLASGAAQVVLSWWEIDMDPDGSITCTMQPSWMYETQQSVPWRDHWMQCVYFLPKECSVTQGEVCCLTAHQDDYCVWYSLNKSSAENDPVCRERPTCHCGAHITWNRARFGELNDRHRTQQYFEALKKVVTPSSTCLCVSDGSLLPVLAHSLGAKQIYTLESSSIAQHLMKKLFQVNHLGEKIQVLHKSADSLITADFEDRKISTLIGEPFFTTNLLPWHNLYFWYSRTALSTNLAKDCTVLPLSASLHVVAVEFKDLWRIRSPCGMCEGFDVSIMDKMIKNSLNFRESQEAEPHPLWEYPCRALSEPIQVMTFNFTEPVPTEEIRASGSLNLVRSGQCHGAVLWMVYELTKEITVSTGLIGISEEMGECQWYPHRKQGVYFFSSILNPQTIPAQSPSSVSYSVTFIPKEGDIRMCFEPDF | Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily. |
Q5RGQ2 | MGLRHSSRCLLLRRKMAEAESTEQQQQKHKQPQHQQQQSISSIPSSQSLQPSPLPKPVTSVHHVPPHPPHTPHVSALSACPGRGKMAKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHIFKDKIVLDVGSGTGILSMFAAKAGAKHVYGIECSSISEYSEKIIKSNHLDSVITILKGKVEETELPVDQVDIIISEWMGYCLFYESMLNTVIYARDKWLKPGGFMFPDRATLYVVAIEDRQYKDFKIHWWENVYGFDMTCIRNVAMMEPLVDIVDPKQVVTNSCLVKEVDIYTVKTEDLSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKTGFSTAPDAPSTHWKQTVFYLEDYLTVRRGEEILGSITVRPNENNERDLDFTFELDFKGQLCDAAISHDYKMR | S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Homodimer. Tetramer; individual homodimers associates to form a homotetramer. Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane. The N-terminal region (1-60) inhibits the arginine N-methyltransferase activity. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily. |
Q8TBJ8 | MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGKMSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR | S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer (PubMed:16051612, PubMed:17925405, PubMed:26876602, PubMed:26529540). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (PubMed:18320585). L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Homodimer (PubMed:16051612, PubMed:26876602, PubMed:26529540). Tetramer; individual homodimers associates to form a homotetramer (PubMed:26529540). Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane (PubMed:26876602). Heterodimer with PRMT1; heterodimerization may recruit PRMT1 activity to the plasma membrane (PubMed:16051612). Interacts with PRMT2 (via the SH3 domain) (PubMed:17925405). Interacts with FYN (via the SH3 domain) (PubMed:17925405). Interacts with EWS; independently of EWS methylation status (PubMed:18320585). Brain-specific. The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein. The N-terminal region (1-60) inhibits the arginine N-methyltransferase activity. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily. |
Q2W2T7 | MLALGLMSGTSLDGVDVALLETDGETVARFGPATTVPYGDEQRIALMGVLGGKGPVEQVERDFTLFHAQVVRDFLAAQGIDAATVGVAGFHGHTILHAPAERRTWQIGDGALLASEIGIPVVNDFRSADVAAGGQGAPLVPVYHRALAAGLEAPLAILNLGGVGNVTWISDDGSLLAFDTGPGNALLDDWALAHTGRPVDVDGRLAAAGKVRRDAVEAFLHHTYFDCQPPKSVDRDEFHALAWELVKGCSAEDGAATLTAFTAAAVALAAYSFPRPVKRWLVTGGGRRNPEMMTALSRGLSAPVEPVEAVGWNGDALEAQAFAFLAVRSLAGKMLTYPETTGAPAPQTGGRHHVP | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q65R57 | MMKQYYIGVMSGTSLDGVDLALMDFTLNPPKLMATDFTPMPEKIREKLTALLRSGETSLRNLGEIDHQLGLLYAESINRFLQKVRLKSEDICAVGCHGQTVWHSPNCEFPFTMQIGDMNLVAAKTGITTVGDFRRKDMALGGQGAPLVPAFHQDLFFAAERLTVVLNIGGISNISVLEENCPTVGYDVSVGNALLDSWIELHQGKRYDKDALWAKNGKISTALLTDLLAEPFFQQAPPKSTGRELFNLAWLNKKLEKFTALSQPMPSPQDVQRTLVEFTALSIANELKKLQKSDRTNLLLVCGGGARNPLIMQRLTALLAEWQVSTTSEFGLDIDYVEAAAFAWLAYRRIHNLPSNLPSVTGAKSEVSLGVIFPK | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
B7KT22 | MAMKRAIGLMSGTSLDGIDVALIESDGERIRLVKSANGLVAPLGPTGYRGYAEAERALLREATRDAEGLRARTDRPGRLAEAEDFVARAHAEAIEAFLAQNDLRPEDIDVVGFHGQTVIHRPKLGLTVQLGDGAALAKRLGIRVVSDMRANDVAQGGQGAPLVPVFHKALAEAAGFTGPLGILNIGGLANATLIDSGGNMLAFDTGPGNGPINDWMKERTGQDFDEGGATAARGTVDEDLLENLLGHPLILRAPPKSLDRNWFSHRLAGYLTVEDGAVTLTAFTAHAVARSLAFASERPARWIVGGGGAKNRTLMVMLERLLAAEVLNADAIGWSSDFLEAQAFAYLALRSLEGLPLTYPTTTGVAAPVTGGIVSEP | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
B8IS49 | MRAIGLMSGTSLDGIDVALIESDGETVRVRRGHNGRIGPLGPTGYRAYSDEDRALLRRALAEAEAIAVRTDRPGCLREAEERVTRLHAEAVENFLTENGLTPADIDLIGFHGQTVIHRPGQGLTVQIGDGARLSRHLGIPVVSDFRQADVAAGGQGAPLVPIFHRALARASGFEGSLAILNIGGVANVTLIAGNGDLLAFDTGPGNALIDDWMSERASRPFDARGSTAAAGRPDEALLAWLLVHPYFTRRPPKSLDRNSFSHRLVGPLSTEDGAATLTAFTVRAVARALDFASEPPRRWIVAGGGARNDEMLRLLRHHLRAEVTPADEIGWSSAFLEAQAFAHLAVRAWNGLPITFPSTTGVSAPMTGGVTARP | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
B1ZHK6 | MTMKRAIGLMSGTSLDGIDVALIESDGESIRIVKSANGFIAPLGPTGYRGYREDEKTLLREATRDAEGIRARADRPGRLPQAEDFVTHAHAEAIEAFLAENGLSPADIDVVGFHGQTVIHRPKLGLTVQIGDGAALARRLGIRVVSDMRADDVAQGGQGAPLVPVFHKALAEAAGFAGPLGILNIGGLANATLIDSSGNMLAFDTGPGNGPINDWMKERTGRDLDEDGATAARGTVDKDLLENLLGHPLILRQPPKSLDRNWFSHRLAGYLTIEDGAATLTAFTAHAVARSLAFASERPTRWIVGGGGAKNRTLMTMLERLLKAEVLNADAIGWSSDFLEAQAFAYLALRALEGLPLTYPTTTGVSEPVTGGLVSEP | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
B0JSC7 | MLVIGLMSGTSVDGIDTALVEISGTVESPQVQLLAGETYPYSPRLRETILQVCGGEKLSIEALASLDDNIAAEFAQAALNIQKEAPKAQLIGSHGQTVFHRPPANDRLGYTVQLGRGAAIAKITRIPTISNFRAADIAQAGHGAPLVPKIDAYLLSHPTKTRCVQNIGGIGNLTYLPPRQRENWQQKIFGWDTGPGNVLIDLAVQFLSQGQQTYDHNGQWSAQGQPCSELVHKWLQEPYFQQYPPKSTGRELFSPAYLAQLREDAQAYCLSDADWLASLTDLTAISIAHSYQTFLPEMPAEVLLCGGGARNAYLRQRLLAHLGSNVKLLTTDEVGLNSDFKEAIAFALLAYWRWHNFPGNLPQVTGAKAAVLLGEIYR | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q5F6H5 | MMETQLYIGIMSGTSMDGADAVLVRMDGGKWLGAEGHAFTPYPDRLRRKLLDLQDTGTDELHRSRMLSQELSRLYAQTAAELLCSQNLAPCDITALGCHGQTVRHAPEHGYSIQLADLPLLAELTRIFTVGDFRSRDLAAGGQGAPLVPAFHEALFRDDRETRVVLNIGGIANISVLPPGAPAFGFDTGPGNMLMDAWTQAHWQLPYDKNGAKAAQGNILPQLLGRLLAHPYFSQPHPKSTGRELFALNWLETYLDGGENRYDVLRTLSRFTAQTVCDAVSHAAADARQMYICGGGIRNPVLMADLAECFGTRVSLHSTAELNLDPQWVEAAAFAWLAACWINRIPGSPHKATGASKPCILGAGYYY | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
B4RQI7 | MAFCTSLGVMMETQLYIGIMSGTSMDGADAVLVRMDGGKWLGAEGHAFTPYPDRLRRKLLDLQDTGTDELHRSRMLSQELSRLYAQTAAELLCSQNLAPCDITALGCHGQTVRHAPEHGYSIQLADLPLLAELTRIFTVGDFRSRDLAAGGQGAPLVPAFHEALFRDDRETRVVLNIGGIANISVLPPGAPAFGFDTGPGNMLMDAWTQAHWQLPYDKNGAKAAQGNILPQLLGRLLAHPYFSQPHPKSTGRELFALNWLETYLDGGENRYDVLRTLSRFTAQTVCDAVSHAAADARQMYICGGGIRNPVLMADLAECFGTRVSLHSTAELNLDPQWVEAAAFAWLAACWINRIPGSPHKATGASKPCILGAGYYY | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
A9M2L4 | METQLYIGIMSGTSMDGADAVLIRMDGGKWLGAEGHAFTPYPDRLRRKLLDLQDTGTDELHRSRMLSQELSRLYAQTVGELLNKQNLAPSDITALGCHGQTVRHAPEHGYSVQLADLPLLAELTQIFTVGDFRSRDLAAGGQGAPLVPAFHEALFRDDRETRAVLNIGGIANISVLPPDAPAFGFDTGPGNMLMDAWMQAHWQLPYDKNGAKAAQGNILPQLLDRLLAHPYFAQPHPKSTGRELFALNWLETYLDGGENRYDVLRTLSRFTAQTVFDAVSHAAADARQMYICGGGIRNPVLMADLAECFGTRVSLHSTAELNLDPQWVEAAAFAWMAACWVNRIPGSPHKATGASKPCILGAGYYY | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
A1ITU1 | MMETQLYIGIMSGTSMDGADAVLIRMDGGKWLGAEGHAFTPYPGRLRRKLLDLQDTGADELHRSRMLSQELSRLYAQTAAELLCSQNLAPSDITALGCHGQTVRHAPEHSYSVQLADLPLLAERTQIFTVGDFRSRDLAAGGQGAPLVPAFHEALFRDDRETRAVLNIGGIANISVLPPDAPAFGFDTGPGNMLMDAWMQAHWQLPYDKNGAKAAQGNILPQLLDRLLAHPYFAQPHPKSTGRELFALNWLETYLDGGENRYDVLRTLSRFTAQTVFDAVSHAAADARQMYICGGGIRNPVLMADLAECFGTRVSLHSTAELNLDPQWVEAAAFAWMAACWVNRIPGSPHKATGASKPCILGAGYYY | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q9K118 | MMETQLYIGIMSGTSMDGADAVLIRMDGGKWLGAEGHAFTPYPGRLRRQLLDLQDTGADELHRSRILSQELSRLYAQTAAELLCSQNLAPSDITALGCHGQTVRHAPEHGYSIQLADLPLLAERTRIFTVGDFRSRDLAAGGQGAPLVPAFHEALFRDNRETRAVLNIGGIANISVLPPDAPAFGFDTGPGNMLMDAWTQAHWQLPYDKNGAKAAQGNILPQLLDRLLAHPYFAQPHPKSTGRELFALNWLETYLDGGENRYDVLRTLSRFTAQTVCDAVSHAAADARQMYICGGGIRNPVLMADLAECFGTRVSLHSTADLNLDPQWVEAAAFAWLAACWINRIPGSPHKATGASKPCILGAGYYY | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
A1KVQ5 | MMETQLYIGIMSGTSMDGADAVLIRMDGGKWLGAEGHAFTPYPDRLRRQLLDLQDTGADELHRSRILSQELSRLYAQTAAELLCSQNLAPSDITALGCHGQTVRHAPEHGYSIQLADLPLLAERTRIFTVGDFRSRDLAAGGQGAPLVPAFHEALFRDNRETRAVLNIGGIANISVLPPDAPAFGFDTGPGNMLMDAWTQAHWQLPYDKNGAKAAQGNILPQLLDRLLAHPYFARPHPKSTGRELFALNWLETYLDGGENRYDVLRTLSRFTAQTVFDAVSHAAADTRQMYICGGGIRNPVLMADLAECFGTRVSLHSTAELNLDPQWVEAAAFAWLAACWINRIPGSPHKATGASKPCILGAGYYY | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q82UQ3 | MYYVGIMSGTSLDGIDAVLVDFSGPSFSLLHTCYIPYDQSLRAALLGLNQAGENELHRAAILSNQLSGWYAQAVGRLLEKSGIDPGEIIAVGCHGQTIRHCPQPENGYSIQLVNGALLAELTGMTVVTDFRSRDIAAGGQGAPLVPAFHHEMFAHRDIHRLIINIGGITNITSLPVSGGVNGFDCGPGNMLMDAWCLKHTGMTYDHNGSWAESGRVINPLLENLLNFPYFSLPPPKSTGREMFSLDWLQPCLRGDEATQDVQSTLLQLTVRTITDSVETYYPAVRELYLCGGGAHNGTLVTRLQQQLPGRRINLTDALGIEADWVEACAFAWLARQSIERAPGNLPAVTGATGSRTLGAIYPA | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q2YBK8 | MKAAYYIGIMSGTSLDGIDAVLADFEAPRPVLLDNFYLPYPEKLREQLKALHFPAHGELHRAATLGNQLARHYAEAVGGLLRKSGVAPPEVAAIGCHGQTIRHCPQAEAGYTIQLCNSPLLVELTGIRVVSDFRSRDIAAGGQGAPLVPAFHQALFADPHVHRVIVNIGGISNLTDLPRNGSVTGFDCGPGNAMMDEWCARHTGQAYDEEGRWAATGKTLSVLLEKLLALPFFSLPPPKSVSRELFSTTWLEGYLKGDESPADVQATLLELTVAGIARCILGYCGDATEIYVCGGGARNSYLIASLQEALSGRKVGLTDSLGVDADWLEAFAFAWLARQLIQGIPGNIPSVTGAKGPRLLGAIYPA | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q3JCM5 | MAQRYIGLLSGTSMDAVDAALVELEPLRILATHSIPISLALRQQLFAVIERSTTSLGELGALDIRLGRLFAETALELLAKAKCSVTEVQAIGSHGQTIYHWARGPDPFTLQLADPNTIAEITGITTIADFRRRDLAAGGQGAPLAPAFHAAFLRSPHYHRAVLNIGGIANISFLPADHRTPIWGFDTGPGNTLMDGWISRHLNQSIDREGRWAASGRVNKTLLRYLLTDPYFSLPPPKSTGREYFNLVWLDHILSKTGIKLSPPDVQATLCALTIASVKLAIQSSSPHTEELLICGGGANNETLMEGLRKQLAFCRVTTTTAYGIPPQWVEACTFAWLAKQTLEGHPGNLPEVTGARHPVILGAIYPANAAVSSRT | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q3SS13 | MMTAIGMMSGTSLDGVDVALIETDGERVTAFGPTGYRPYTNDERGLLREALAEAVNLTRRDARPGVIGMAEHAVTMAHSDAVTSFLARNGIRREDIDIVGFHGQTVLHRPGERLTVQIGDADALAKAIRVPVMHDFRAADVAAGGQGAPFVPAYHRALAQSLGRDGPICVVNIGGVSNVTYIDGADTLIACDTGPGNALLDDFMLRTTGEPFDRDGRLAQQGRPDADWIASALNHPFFALPPPKSLDRNDFASLALPDRPPADGAATLTAFTAAAIARIVPLLPKAPERWIVAGGGARNPIMLEMLREKVAPAPVERADALGWSIDAMEAQAFGYLAARGLKGLPLSYPATTGVPVPMTGGVVTRP | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q8YNP4 | MYSSQASAVPNRVVGLISGTSVDGIDAALVEITGTELDLKVELLAGKTYPYPADLRERILAVCAGEAISMLELAHMDDAIALAFAQAAQNIQIGYQPANLIGSHGQTVYHRPPKEAGVGKKNLGYTLQLGRGEMIAYLTGITTVSNFRVADIAVGGHGAPLVPRVDAFLLSHPHESRCIQNLGGIGNLAYIPARTDDWLSQICGWDTGPSNSLLDLAVERLTAGAKTYDEDGQWAASGTPCYPLVEKWLTHEYFHLSPPKSTGRELFGVAYLNQCFQDAEPYQLSPADMLATLTELTVASIVHSYRTFLPQMPQRVFLCGGGSRNLYLKQRLQLALETVPVLTTDEAGVSADFKEAIAFAVLAHWRQLAIPGNLPTATGAPHEVLLGEIHQG | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q7U4A1 | MLCLGLMSGTSADGVDAVLARFQGAPDRPEWQLLSHHHSPYPAALRDELVRIGQGEARPAAALLDLAEAVTEHQALAARGADPDQRASLIGCHGQTLWHRPPSSDKRGASWQLLLAPLLAQLLARPVVHDFRATDLALGGQGAPLVPRADAALIGPGDGWRGVLNLGGIANLTLIPPRWGPQKQESVLGWDCGPANSLIDLAMEQFSDGQQLFDRDGAMAAAGRCDDGMIQRWLREPYFQLSPPKSTGRECFGQEDLRRRLQELESVERADAVATLTGFTAAVVAQDLDRLRADRSIHLLELLVAGGGCRNPVLMSELQRRCRGLAVRASDQIGLAAEAREALVFALLAWWHHRGHPGNAPAITGATREACLGVRVAPA | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q13UB5 | MAQDPADGVYFGLMSGTSMDGVDGVAVRFAQGKPSVVLAEAFVGFAAGLRDALFALQQPGDNEIEREALAANALATRYAVCCHDLLHNSRVPAAEVRAIGVHGQTVRHRPEKGYTRQINNPALLAEMMHIDVIADFRSRDVAAGGQGAPLVPAFHATVFGAKNETRVVCNLGGISNITILNATGSVRGFDCGPANALLDEWAQRHLGKPFDENGHFAAGGQVDRTLLNALLDEPFFGQQPPKSTGRDLFNADWLDAKLPPFAALDHADVQATLVALTAVTVAREIERHASDAKAVYVCGGGARNPEILKALQQALEDSGVSGVPVMTTDALGVPPSQVEPLAFAWLAMRCVARLPGNLPAVTGASAERVLGAIYPR | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q9CK07 | MKEATMYYIGVMSGTSLDGVDLALMDFSCAQPQLIHADFYPMPPAIRQQISTLCNSGTTTLQALGELDHQLGLLYTDCIQQFLQKHRLSPEQITAIGCHGQTVWHSPNSHYPFTMQIGDANLIAAKTGITTVADFRRKDMAFGGQGAPLVPAFHQALFRKPNQATVVLNVGGISNISRLLPNEEVIGYDTGPGNTLLDAWIEKHQGKAYDKNAEWAKSGKVNTDLLADLLDEPFFALPAPKSTGRELFNLAWLNKKLQKHTALLPQDVQATLVELTAQSIVDQLNQIETELDRHLLVCGGGVKNCLLMARLTALLPQWQVQTTNDYGLDADYVEAAAFAWLAYQRLNDLPGNLPSVTGAKSAVSLGAIYPKEKDVAA | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. Cell wall biogenesis; peptidoglycan recycling. Belongs to the anhydro-N-acetylmuramic acid kinase family. |
Q5EA33 | MEKEKVNDEKPDPENSLDFSEHFNQLELLETHGHLIPTGTQSLWIGNSDDDEEQDEKTEEWYQLQEKKMEKDPSKLLLWAAEKNRLTTVQRLLSERATHVNTRDEDKYTPLHRAAYNGHLDVVRELIAHGADVHAVTVDGWTPLHSACKWNNARVASFLLQHDADVNAQTKGLLTPLHLAAGNRDSKDTLELLLMNRYIKPGLKNSLEETAFDIARRTGIYHYLFEIVEGCTNCSPQS | May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF-kappaB pathway. |
Q9NXK7 | MEKEKGNDDGIPDQENSLDFSEHFNQLELLETHGHLIPTGTQSLWVGNSDEDEEQDDKNEEWYRLQEKKMEKDPSRLLLWAAEKNRLTTVRRLLSEKATHVNTRDEDEYTPLHRAAYSGHLDIVQELIAQGADVHAVTVDGWTPLHSACKWNNTRVASFLLQHDADINAQTKGLLTPLHLAAGNRDSKDTLELLLMNRYVKPGLKNNLEETAFDIARRTSIYHYLFEIVEGCTNSSPQS | Induces HBG1 expression (PubMed:16131492, PubMed:11162141). May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF-kappaB pathway (By similarity). Widely expressed in fetus, at a high level in fetal liver, brain and lung. |
Q9Z2S1 | MEKEKKDDEKPDLENSVDFSEQFNQLELLKTHGHLIPTGTQSLWVGNSDEDEEQEEKNEEWYQLQEKKMEKDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMNRYIKPELKNNSQETASDIARRTSIYHYLFEIAEGCTNSSPPS | May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF-kappaB pathway. Expressed in spermatogonia, spermatocytes and round spermatids. Expressed in liver at embryonic stage 13 dpc, and in liver, brain and lung at 16 dpc (PubMed:11162141). In testis, expression levels steadily increase from 1 week after birth and plateau by 8 weeks after birth (PubMed:26043108). |
Q6ZSE6 | MTNPWEEKVCKMAQTSLLQGKQFYCREWVFHKLQHCLQEKSNCCNSAVNAPSLVMNSGNNASGVSGKGAAWGVLLVGGPGSGKTALCTELLWPSSPASLQRGLHRQALAFHFCKAQDSDTLCVGGFIRGLVAQICRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVLLPLLGMKPPQQSLYLLVDSVDEGCNITEGEQTSTSLSGTVAALLAGHHEFFPPWLLLLCSARKQSKAVTKMFTGFRKISLDDLRKAYIVKDVQQYILHRLDQEEALRQHLTKETAEMLNQLHIKSSGCFLYLERVLDGVVENFIMLREIRDIPGTLNGLYLWLCQRLFVRKQFAKVQPILNVILAACRPLTITELYHAVWTKNMSLTLEDFQRKLDILSKLLVDGLGNTKILFHYSFAEWLLDVKHCTQKYLCNAAEGHRMLAMSYTCQAKNLTPLEAQEFALHLINSNLQLETAELALWMIWNGTPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNGCSPSPVHTMEQKPLQSLSSKVQSLTIKSNSSGSTGGGDMQPSLRGLPNGPTHAFSSPSESPDSTVDRQKSSLSNNSLKSSKNSSLRTTSSTATAQTVPIDSFHNLSFTEQIQQHSLPRSRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKSTKASKGGKSENSAKSGSAGKKAKQSNSSQPKVLEYEMTQFDRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNGIMTNPNYHLQSNQVFLGRVSVPRTMQDRGHQEVLEGYPSSETELSLKQALKLQIEGSDPSFNYKKETPL | Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552). Interacts with VPS35 (PubMed:25278552). |
Q5ZLC8 | MGILSITDQPPLVQAIFNRDVEEVRSLLNQKENINVLDQERRTPLHTAAYIGDVAILELLILSGANVNAKDTVWLTPLHRAAASRNEKALHLLLKHSADVNARDKYWQTPLHVAAANRATKCVEAIIPLLSTVNVADRTGRTALHHAVHSGHLEMVNLLLNKGASLSTCDKKDRQPIHWAAFLGHLEVLKLLVARGADVMCKDKKGYTLLHTAAASGQIEVVRHLLRLGVEIDEPNSFGNTALHIACYMGQDAVANELVNYGANVNQPNEKGFTPLHFAAVSTNGALCLELLVNNGADVNFQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKYGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCTVTLVTAGASINEADCKGCTPLHYAAASDTYRRAETHSGNSHDTDEEPLKESRMKEAFFCLEFLLDNGADPSLRDKQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTIPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALYLATERGSTECVEVLTSHGASALVKERKRKWTPLHAAAANGNTDSLHLLIDSGERADITDVMDIHGQTPLMLAIMNGHVDCVHLLLEKGSTADAADKRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHFASACGHLEILRTLLQAALSTDPLDSVVDYSGYSPMHWASYSGHEDCLELLLEHNPFAYLEGNPFTPLHCAVINNQDSTAEMLVEALGAKIVNSRDAKGRTPLHAAAFADNIHGLQLLLRHQAEVDTTDKLGRTPLMMASENGHTAAVEFLLYQAKANITVLDVNKNTALHLACSKGHEKCALLILGETQDLGLINASNSALQMPLHIAARNGLATVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALILSTMKPFPPKDAISSFSFNLLKNCGIAAKTAACGALPNGSTCPYSKDRHNAIGLDGCYSE | Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). |
Q502K3 | MGVLNISDQPPLVQAIFNRNADEVKLFLHKKDEVNALDQERRTPLHAAAWLGDVHIMDLLISAGANVNAKDHVWLTPLHRAAASRNERAVGLLLRKGADVTARDKYWQTPLHIAAANRATRCVETLLPHVSSLNMADRTGRAPLHHAAQSGYQEMVKLLLNKGANLSASDKKDRQPIHWAAYLGHLEVVKLLVSQGSDKSCKDKRGYTPLHAAAASGHVDVVKYLLRNGAEIDEPNAFGNTALHVACYTGQEAVANELVNRGANVNQPNHRGYTPLHLAAVSTNGALCLELLVNNGADVNMQSKEGKSPLHMAAIHGRFTRSQILIQNGGEIDCVDRYGNTPLHVAAKYGHELLISTLMTNGADTARQGIHGMFPLHLAVLYGSSDCCRKLLSSGQLYSIVLSMSKEHVLSAGFDINTPDNFGRTCLHAAASGGNIECLNLLLSSGADMNKKDKFGRTPLHYAAANGRYQCVVVLVGAGAEVNERDRSGCTPLHYSAASTAFCRTDRPHASTHQNQEDGEKESFLCVEHLLDNGADPCLCNTKGYSAVHYAAAHGNKQNLELLLEMCFNTLGDKESNGSISPLHLAVESGHWECVTVLIESGVCVDVCDPVGRSVLYLASQRGHSRCVELLLSQSASCLLAEHRSKWGPLHVAAANGHSECLRMLLCSEGGADLVNVTDAEGQTPLMLAVLGGHTDCVHLLLERGACPDMKDRRGRTALHRGAVMGREDCLTALLSHNVSVLSRDFQGRSALHLAASCGHADILSNLLSAADHSQPQDPLTDRHGYTPAHWAAYHGHEDCLEVLLELKPCSIQEGNPFTPLHCALINGHSGSAELLLESSVCNSLVNIRDAKGRTPLHAAAVAEDVAGLQLVLRQGADIDAVDHSGRSALMVAADYGQSGAVALLLHRAKADLSLLDVNKNTALHLACSKAHEMCAMLILKEIHNPILINATNSMLQMPLHIAARNGLATVVQALLNRGATVLAVDEEGHTPALACASNKAVADCLALILSTMKPSSSTASSSSPSSPSLNLLKHCGITAACPPLPNGGLRHGYGKDRHGATIGLDGCLTE | Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). |
B1Q2K2 | MGILSITDQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEPHTPSSHDAEEDEPLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTIPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINATNSALQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLALILSTMKPFPPKDAVSPFSFSLLKNCSIAAAKTVGGCGALPHGASCPYSQERPGAIGLDGCYSE | Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6R1. |
Q148Z3 | MGILSITDQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKHLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEPHTASSHDAEEDELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTVPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAESGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALILSTMKPFPPKDAVSPFSFSLLKNCGIAAAKTVGGCGALPHGASCPYSQERHGAIGLDGCYSE | Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6R1 (By similarity). |
Q8IYP8 | MASAGSTARRAGSGSWHSERGEGRGARPQPTPSGSMQQANKVSLKATWTDAESKQPSQPLPDLADHLSAQATALARPRRPASLTPPRADPSPSKESDQTAIDQTAIGSYYQLFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIEYQKEHKILREAAIRKWLHGKLHPGHSLVSNTKQARATALSKTPEQRESQRSRSFHPSVDARLQCIPQPTEMPKPIYRKPTVKRPTMWNVSNNPARPPTTQISHSQGIRLGVHPDPTPEHDFSSFLEVRPDGHGGARLHTVDGHWVAPVPRLPFEVLLRMLYPRVWPYRMKVPQGFYPISMREVPRKRHLGDNTFWTDTLAMNLRDTFDEAFLAAVRSHQGLPTLPSPQTNP | Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization. Interacts with PSRC1; recruited by PSRC1 to the spindle during mitosis (PubMed:26820536). Localizes at the spindle around the centrosome at prophase and prometaphase and at the spindle poles at metaphase and anaphase (PubMed:26820536). Phosphorylated during mitosis (PubMed:26820536). |
Q4R739 | MASAGSTARRAGSGSWHSERGEGRGARPQPTPHGSMQRANKVSLKATWTDAESKQPRPSEESDQTTIDQTAIRSYYQLFAAAVGNVEWLRFCLNQSLREIPTDYKGFTAIHFAAQRGKLACLQVLVEEYKFPVNLLTNNSQTPLHLVIHKDNTTVALPCIYYLLEKGAALNAQTCNGCTPLHLAVREGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDAMWKKDKKDFACEMRKMKTLKSQLALMEYNYLIEYQKEHKILREAAIRKWLHGKLHPGHSLVSNTKQARATALSKTPEQRGSQCSSSFHPSVEARLQCIPQPTEMPKPIYRKSTIKRPTMWNVSNNPARPPTTKISHSQGIRLGVHPDPSPEHDFSSFLEVRPDRHGGAWLHTVDGHWVAPVPRLPFEVLLRMLYPHVRPYRMKVPQGFYPISMREVPRKRHLGDDTFWTDTLAMNLRDTFDEAFLAAVRSHQGLPALPSPQINP | Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization. Interacts with PSRC1; recruited by PSRC1 to the spindle during mitosis. Localizes at the spindle around the centrosome at prophase and prometaphase and at the spindle poles at metaphase and anaphase. Phosphorylated during mitosis. |
E9QN79 | MRRPSRRRSKASTPPRSHTTPRRTGPSDSRRRPGTKEQPRPSVQGGTRQAEHDLKVSSPNSESSQYSTSELWSHKVIANYSELFAASVGNVDWLRFCVNPERKEIIVDDKGFTAIHFAAQKCQLSCLKVLIEEYKYPVDLPTNKGQTPLHLVIHKNNKSDILPCIDYLLKKGAAINSQTYNGSTPLHLASCNGLLGCIKLLVQSGANVHARDATGFKPIDYCRLWNHRTCARFLKDVMWKHDKKVLAQEMEKLRTLKEKLTILEYHYLVEYQKEHQILREAHFRKWLQNKVLAQTLGSADSKQKAGVQPWSLASNTLRCPITESLHYPSVEAQLKNLPSPVVPPKPIYKQTTISRPKLWNYSANPARSPITNIGHPQNIRLGVHPEPYKEHDFRRFLEVTRNKHGGACLRTVDRQLVTPVPQLPFEMMVRVLYPGTQPYRMKVPQGLYPRDILKVPEKRHVGDTCSNTMAMTLRETFDKPFLDSLEVCRTRVAPPSK | Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization. Interacts with PSRC1; recruited by PSRC1 to the spindle during mitosis. Localizes at the spindle around the centrosome at prophase and prometaphase and at the spindle poles at metaphase and anaphase. Phosphorylated during mitosis. |
Q1LZC5 | MAAAAGGADDESRSGRSSSDGECAVAPEPLTGPEGLFSFADFGSALGGGAGLPGRASGGAQSPLRYLHVLWQQDAEPRDELRCKIPAGRLRRAARPHRRLGPTGKEVHALKRLRDSANANDVETVQQLLEEGTDPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHAPVITTLLRGGARVDALDRAGRTPLHLAKSKLNILQEGHSQCLEAVRLEVKQIIQMLREYLERLGRHEQRERLDDLCTRLQKTSTREQVDEVTDLLASFTSLSLQMQNMEKR | Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. Interacts (via ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN. Forms a multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1, DBNL AND LASP1. Shuttles between nucleus and cytoplasm during the cell cycle. |
Q6DGX3 | MDGSSPLLAAAGSDGDRSSSEGEYTLAGGPSAGDTEKREGESPMEAAGAGTVGFSISRLDTLSALRLNRTRPAADTELRYLHLLWKPGELLQAGRSTPGKITSSRVRRLARARRNMGPIGKDLHAVKRLREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLARSKLNILQEGDSRSLETLRGEVTQIIQMLREYLNIMGQSEEREKLEHISTQLQNTRTREQVDEVTDLLASFTSLSIQMQNMGDR | Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. Shuttles between nucleus and cytoplasm during the cell cycle. |
Q9UGV1 | MAAAAGDADDEPRSGHSSSEGECAVAPEPLTDAEGLFSFADFGSALGGGGAGLSGRASGGAQSPLRYLHVLWQQDAEPRDELRCKIPAGRLRRAARPHRRLGPTGKEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNILQEGHAQCLEAVRLEVKQIIHMLREYLERLGQHEQRERLDDLCTRLQMTSTKEQVDEVTDLLASFTSLSLQMQSMEKR | Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. Interacts (via ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN. Forms a multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1, DBNL AND LASP1. Shuttles between nucleus and cytoplasm during the cell cycle. EPO stimulation induces nuclear accumulation (By similarity). |
Q3UZL7 | MAATGGGADDESRSGRSSSDGECAVAPEPLAEAGGLVSFADFGVSLGSGAGLPGRSVGRAQSSLRYLQVLWQQDVEPRDELRCKIPAGRLRRAARPHRRLGPTGKEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNILQEGHSQCLEAVRLEVKQIIHMLREYLERLGRHEQRERLDDLCTRLQMTSTKEQVDEVTDLLASFTSLSLQMQSMEKR | Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. Interacts (via ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN. Forms a multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1, DBNL AND LASP1. Shuttles between nucleus and cytoplasm during the cell cycle. EPO stimulation induces nuclear accumulation. Expressed in a variety of hemopoietic cell lines and tissue with high levels in testis. Highly expressed in ciliated cells. Expressed in brachial arches, maxillary process, fore and hind limb buds and in the developing gastrointestinal tract of day 10 embryos. |
Q92125 | MSYQYPSGFPGYPGYPGGDPSYPPAAQQAFPGGQFPPAAGGGAFPPASGGGNAPPPGGGYPHAGGYPAPGGYPGGMPSYPGAPGFGAPAGGQGYGAPPGAPAYGVPGYGGPGFNAPAGGYGAPNAGGFGVPPAGGYGSPGGAPGYGGFSQPSSQSYGAGGPGQMPGQMPGQMPGQAPSGYPSGPAPAQPTPYAAAMTATQGTIKAAPNFDALSDAEKLRKAMKGFGTDEKPIDVVANRSNDQRQKIQAAFKTAYGKDLIKDLKSELSGNVEELIIALFMPSTYYDAWSLYNAMKGAGTQERVLIEILCTRTNSEIRNIVACYKQEFGREIEKDIRSDTSGHFERLLISIMARGIVDESQNVNMQQAEQDAQRLYQAGEGKLGTDESSFNLVLASRSFPQLKAVAEAYARISKRDLLSVIGREFSGYIEDGLKAVLQCAINRPLFFRDRLCRSMKGAGTDDSTLIRIIVTRSEIDLVQIKQAYVQMYQKSLSAAISSDTSGAYKRMLLAISGH | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
Q95L54 | MAWWKAWVEQEGVSVKGSPHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNAQRQQIAKSFKAQFGKDLIETLKSELSGKFERLIIALMYPPYRYEAKELYDAMKGIGTKEGVIIEILASRTKNQLQEIMKAYEEDYGSNLEEDIKADTSGYLERILVCLLQGSRDDLSGYVDPGLALQDAQDLYAAGEKICGTDEMKFITILCTRSATHLMRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTRNLHGYFAERLYFAMKGAGTLDGTLIRNIVSRSEIDLNLIKNQFKKMYGKTLSSMIMEDTSGDYKNALLNLVGSDL | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
Q9BT34 | MAWWKSWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
Q8K2N9 | MAWWKAWVEQEGVSVKGSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNVQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYSYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSTLEEDIQGDTSGYLERILVCLLQGSRDDVSGFVDPGLVLQDAQALHEAGEKIMGTDEMKFITILCTRSATHLMRVFEEYEKIANKCIEDSIKSETHGSLEEAMLTVVKCTRNVHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKGQFKKMYGKTLSSMIMADTSGYYKTALLNLVGTDL | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
A5A6L7 | MAWWKAWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKSLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAHDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
O97529 | MAWWKAWVEQEGVTVKGSPHFNPVPDAETLYKAMKGIGTNEQAIIDVLTRRSSAQRQQIAKSFKAQFGSDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLQEIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVTGFVDPGLALQDAQDLYAAGEKICGTDEMKFITILCTRSARHLMRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTIVKCTRNLHCYFAERLHYAMKGAGTLDGTLIRNIVSRSEIDLNLIKGHYKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
Q4FZU6 | MAWWKAWVEQEGVSVKGSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNVQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSTLEEDIQGDTSGYLERILVCLLQGCRDDVSGFVDPGLALQDAQDLHAAGEKILGTDEMKFITILCTRSATHLMRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTRNVHSYFAERLYYAMKGAGTLDGTLIRNIVSRSEIDLNLIKSQFQKMYGKTLSSMIMGDTSGYYKTALLNLVGTDL | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
Q3ZC08 | MSVTHGKMGLSLTQEILSHLGLANKTAAWGTLGTLRTFLSFSADKDVQRLLKAIAGQGVDRIAILDVLTNRSREQRQLISRAFHERTQQDLLKSLQAALSGNLERIVVALLQPAAHLDARELRTALKGSGSAEDVALEILATRTPPQLQECLAVYKHNFQVDAAEDIKSETRGILRDLLLALAKGGREAYTGIIDYNLAAQDVQALKQAEGPSTERTWVLVFTQRNPEHLVRVLNQYQWYTGHGLEKTVRARFHGAACVALLNLASVIRNTPLYFADKLHQALQETEPNYQALMRILISRSETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCRSALLALCRAEDL | May act as a low affinity receptor for acetylcholine. Homodimer. Belongs to the annexin family. |
Q9HBJ6 | MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVDRSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLLALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRSTGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISRCETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCQSALLALCRAEDM | Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes. Homodimer. Expressed in the stratified squamous skin epithelium, but not in epithelia of other types (at protein level). Belongs to the annexin family. |
Q9CQS1 | MSASCGPLGTSLTQEILSSLGLADKTAAWGTLGTLRTFLSFSVDKDVQRLLKAIAGQGVDYDTIVDVLTNRSREQRQLISRAFQERTKQDLLKSLQAALSGNLEKIVVALLQPAAQFDAQELRTALKTSGSAEDVALEILATRAAPGLQACLAVYKHDFQVEAEEDIRTETNGILQDLLLALSKGDRESYSGIIDYNLEEQDVRALQQAGESSTAGQWVLLLTQRSPEHLIRVFDQYRRCTGQELEDAIRNCFHGDAQLALISLASMLRNTALYFANKLHQALQETEPNFQVLTRVLISRSESDLLSIRAEFKKKFGKSLYSSLQDVVRGDCRSALLALCRAEDI | May act as a low affinity receptor for acetylcholine. Homodimer. Belongs to the annexin family. |
Q9VDF3 | MSSAEYYPFKCTPTVYPADPFDPVEDAAILRKAMKGFGTDEKAIIEILARRGIVQRLEIAEAFKTSYGKDLISDLKSELGGKFEDVILALMTPLPQFYAQELHDAISGLGTDEEAIIEILCTLSNYGIKTIAQFYEQSFGKSLESDLKGDTSGHFKRLCVSLVQGNRDENQGVDEAAAIADAQALHDAGEGQWGTDESTFNSILITRSYQQLRQIFLEYENLSGNDIEKAIKREFSGSVEKGFLAIVKCCKSKIDYFSERLHDSMAGMGTKDKTLIRIIVSRSEIDLGDIKEAFQNKYGKSLESWIKEDAETDIGYVLVTLTAW | Expressed throughout development with highest expression seen in adults. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin family. |
J9VS56 | MYGQQNNYGAPPPQQWGQAPPQGYQPGYQNGPPAVNYGAHPSQQQQWGAPPGPPQHQPYGAPPVNQYGAPPQHQQGYGGHSPQPPFGAPSPAPAGYGAPPTAPQGQYGAPSPYPQQPPQQGFGGPQQGYGSQPQGQSPMMYLGVPIPAPPPAVPVSTLAGYDARFDAERIRKATKGFGTDERTIIDTLSPLDAFQMDVLSRTYEQTVGRSLKSTLEKELSSWLEYTLVLLSLGPLGGDVYLLHRACNGMGTHEDLLNEVLLGRTNQEIFLLKEAYRRTYNQDLVQIVQGELSMKTERMFNMALSGQRDESPYLNHQLVQQDVETLYRAGPGKIGTDEIAICGILISRSKEHLKAIAQAFPARHRVSLSQMIHSEFSGHMRDALFFIARGVEADGDGVVRDCELLHAAMAGMGTKDERMIYRLVRNHWNRPRFNAIKNQYQVLYRNSLRRAVEGETTGKYEKALVGIIEQN | Does not appear to play a major role in virulence (PubMed:31140968). May play a role in titan cell formation (PubMed:31140968). A pair of annexin repeats may form one binding site for calcium and phospholipid. Increases titan cell formation (low penetrance) (PubMed:31140968). Low or no sensitivity to high temperature or tacrolimus (calcineurin inhibitor); sensitivity may be background dependent (PubMed:31140968). No cell population growth phenotype in a variety of conditions including high pH, low calcium, in presence of the antifungals amphotericin B or fluconazole, heavy metals (nickel or zinc), osmotic stress (NaCl), cell wall integrity stressors (Calcofluor White, caffeine, or Congo Red), oxidative stress (H2O2), or nitro-oxidative stress (NaNO2 or H2O2), or following ultraviolet light radiation (PubMed:31140968). Normal mating (PubMed:31140968). Normal virulence factor secretion; assayed using melanin and urease (PubMed:31140968). Normal virulence in mouse intranasal, intravenous, and intratracheal infection models or in an invertebrate infection model (PubMed:31140968). Normal survival rate following amoebal ingestion (PubMed:31140968). Belongs to the annexin family. |
Q96527 | MATLKVSDSVPAPSDDAEQLRTAFEGWGTNEDLIISILAHRSAEQRKVIRQAYHETYGEDLLKTLDKELSNDFERAILLWTLEPGERDALLANEATKRWTSSNQVLMEVACTRTSTQLLHARQAYHARYKKSLEEDVAHHTTGDFRKLLVSLVTSYRYEGDEVNMTLAKQEAKLVHEKIKDKHYNDEDVIRILSTRSKAQINATFNRYQDDHGEEILKSLEEGDDDDKFLALLRSTIQCLTRPELYFVDVLRSAINKTGTDEGALTRIVTTRAEIDLKVIGEEYQRRNSIPLEKAITKDTRGDYEKMLVALLGEDDA | Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development. Active at pH 7.0 and 9.0, but not at pH 5.5. Monomer and homodimer. translocate from cytosol to membrane upon salt treatment; this translocation is calcium dependent. Ubiquitous. Most abundant in stems. Expressed in the elongation zone of the root and in the root cap in germinating seedlings. Expressed later in the internal cells of the root and in the epidermal cells and the vascular tissue of the hypocotyl. By day 7, expressed in the initiating trichomes on leaf primordia and in the vasculature of hypocotyl and cotyledon. At the transition to reproductive growth (day 14), expressed in the vasculature, epidermis, basal mesophyll cells and pith meristem of leaves. Up-regulated by cold, dehydration, salt, osmotic and oxidative stresses. Up-regulated by abscisic acid (ABA) and salicylic acid (SA). A pair of annexin repeats may form one binding site for calcium and phospholipid. Phosphorylated. Plants are hypersensitive to osmotic stress and abscisic acid (ABA) during germination and early seedling growth. Binds lipids at millimolar calcium concentration. Belongs to the annexin (TC 1.A.31.1) family. |
Q42063 | MASLKVPSNVPLPEDDAEQLHKAFSGWGTNEKLIISILAHRNAAQRSLIRSVYAATYNEDLLKALDKELSSDFERAVMLWTLDPPERDAYLAKESTKMFTKNNWVLVEIACTRPALELIKVKQAYQARYKKSIEEDVAQHTSGDLRKLLLPLVSTFRYEGDDVNMMLARSEAKILHEKVSEKSYSDDDFIRILTTRSKAQLGATLNHYNNEYGNAINKNLKEESDDNDYMKLLRAVITCLTYPEKHFEKVLRLSINKMGTDEWGLTRVVTTRTEVDMERIKEEYQRRNSIPLDRAIAKDTSGDYEDMLVALLGHGDA | May mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development. translocate from cytosol to membrane in a calcium-dependent manner. A number of isoforms are produced. According to EST sequences. Expressed mainly in roots and flowers. Low in stems and bearly detectable in leaves. In germinating seedlings, expressed in root, hypocotyl and cotyledon epidermal cells. By day 4, expression expands in the root endodermis and throughout initiating lateral roots. As the seedling matures, expression in the hypocotyl and cotyledons decreases and by day 14, expression is restricted to creases between the shoot meristem and its lateral primordia. Up-regulated by heat shock stress. Down-regulated by cold, dehydration, and salt stresses. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin (TC 1.A.31.1) family. |
Q9ZVJ7 | MATIRVPNEVPSPAQDSETLKQAIRGWGTDEKAIIRVLGQRDQSQRRKIRESFREIYGKDLIDVLSSELSGDFMKAVVSWTYDPAERDARLVNKILNKEKKKKSLENLKVIVEISCTTSPNHLIAVRKAYCSLFDSSLEEHIASSLPFPLAKLLVTLASTFRYDKDRTDAEVATIEAAMLREAIEKKQLDHDHVLYILGTRSIYQLRETFVAYKKNYGVTIDKDVDGCPGDADLRSLLKVAIFCIDTPEKHFAKVVRDSIEGFGTDEDSLTRAIVTRAEIDLMKVRGEYFNMYNTSMDNAITGDISGDYKDFIITLLGSKI | Expressed mainly in roots and flowers. Lower in stems and leaves. Up-regulated by cold and dehydration stresses. Down-regulated by heat shock stress. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin (TC 1.A.31.1) family. |
Q9ZVJ6 | MALPLELESLTEAISAGMGMGVDENALISTLGKSQKEHRKLFRKASKSFFVEDEERAFEKCHDHFVRHLKLEFSRFNTAVVMWAMHPWERDARLVKKALKKGEEAYNLIVEVSCTRSAEDLLGARKAYHSLFDQSMEEDIASHVHGPQRKLLVGLVSAYRYEGNKVKDDSAKSDAKILAEAVASSGEEAVEKDEVVRILTTRSKLHLQHLYKHFNEIKGSDLLGGVSKSSLLNEALICLLKPALYFSKILDASLNKDADKTTKKWLTRVFVTRADHSDEMNEIKEEYNNLYGETLAQRIQEKIKGNYRDFLLTLLSKSD | May be involved in osmotic stress and abscisic acid signaling in a calcium-dependent manner. Expressed mainly in roots and flowers. Lower in stems and leaves. Up-regulated by salt, osmotic and oxidative stresses. Up-regulated by abscisic acid (ABA) and salicylic acid (SA). Down-regulated by heat shock and dehydration stresses. A pair of annexin repeats may form one binding site for calcium and phospholipid. Plants are hypersensitive to osmotic stress and abscisic acid (ABA) during germination and early seedling growth. Belongs to the annexin (TC 1.A.31.1) family. |
Q9C5V4 | MATMKIPMTVPSPRVDADQLFKAFKGRGCDTSVIINILAHRNATQRALIEQEYETKFSDDLRKRLHSELHGHLKKAVLLWMPEAVERDASILKRSLRGAVTDHKAIAEIICTRSGSQLRQIKQVYSNTFGVKLEEDIESEASGNHKRVLLAYLNTTRYEGPEIDNASVENDARTLKSAVARKHKSDDQTLIQIFTDRSRTHLVAVRSTYRSMYGKELGKAIRDETRGNFEHVLLTILQCAENSCFYFAKALRKSMKGLGTDDTALIRIVVTRAEVDMQFIITEYRKRYKKTLYNAVHSDTTSHYRTFLLSLLGPNV | Expressed mainly in roots and flowers. Lower in stems and leaves. Up-regulated by cold, heat shock, dehydration and salt stresses. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin (TC 1.A.31.1) family. Extended C-terminus. |
Q9C5V3 | MASLKIPANIPLPEEDSEQLHKAFKGWGTNEGMIISILAHRNATQRSFIRAVYAANYNKDLLKELDGELSGDFERVVMLWTLDPTERDAYLANESTKLFTKNIWVLVEIACTRPSLEFFKTKQAYHVRYKTSLEEDVAYHTSGNIRKLLVPLVSTFRYDGNADEVNVKLARSEAKTLHKKITEKAYTDEDLIRILTTRSKAQINATLNHFKDKFGSSINKFLKEDSNDDYVQLLKTAIKCLTYPEKYFEKVLRRAINRMGTDEWALTRVVTTRAEVDLERIKEEYLRRNSVPLDRAIANDTSGDYKDMLLALLGHDHA | Expressed in flowers. Up-regulated by heat shock, dehydration and salt stresses. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin (TC 1.A.31.1) family. Extended C-terminus. |
Q9C5V2 | MASLKVPATVPLPEEDAEQLYKAFKGWGTNERMIISILAHRNATQRSFIRAVYAANYNKDLLKELDRELSGDFERAVMLWTFEPAERDAYLAKESTKMFTKNNWVLVEIACTRSALELFNAKQAYQARYKTSLEEDVAYHTSGDIRKLLVPLVSTFRYDGDEVNMTLARSEAKILHEKIKEKAYADDDLIRILTTRSKAQISATLNHYKNNFGTSMSKYLKEDSENEYIQLLKAVIKCLTYPEKYFEKVLRQAINKLGTDEWGLTRVVTTRAEFDMERIKEEYIRRNSVPLDRAIAKDTHGDYEDILLALLGHDHA | Expressed in flowers. Up-regulated by cold, heat shock and salt stresses. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin (TC 1.A.31.1) family. |
Q94CK4 | MATIVSPPHFSPVEDAENIKAACQGWGTNENAIISILGHRNLFQRKLIRQAYQEIYHEDLIHQLKSELSGNFERAICLWVLDPPERDALLANLALQKPIPDYKVLVEIACMRSPEDMLAARRAYRCLYKHSLEEDLASRTIGDIRRLLVAMVSAYKYDGEEIDEMLAQSEAAILHDEILGKAVDHEETIRVLSTRSSMQLSAIFNRYKDIYGTSITKDLLNHPTNEYLSALRAAIRCIKNPTRYYAKVLRNSINTVGTDEDALNRVIVTRAEKDLTNITGLYFKRNNVSLDQAIAKETSGDYKAFLLALLGHGKQL | Up-regulated by dehydration and salt stresses. A pair of annexin repeats may form one binding site for calcium and phospholipid. Belongs to the annexin (TC 1.A.31.1) family. |
Q9LQM4 | MSYRSIYRTLRPVLSSSVQSSGLGIGGFRGHLISHLPNVRLLSSDTSSPVSGNNQPENPIRTADGKVISTYWGIPPTKITKPDGSAWKWNCFQPWDSYKPDVSIDVTKHHKPSNFTDKFAYWTVQTLKIPVQLFFQRKHMCHAMLLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALLEEAENERMHLMTFIELSQPKWYERAIVFTVQGVFFNAYFLAYVISPKLAHRITGYLEEEAVNSYTEFLKDIDAGKFENSPAPAIAIDYWRLPKDATLRDVVYVIRADEAHHRDINHYASDIQFKGHELKEAPAPIGYH | Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity). 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O Binds 2 iron ions per subunit. Homodimer; disulfide-linked. Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. Expressed in roots, seedlings, leaves, flowers and sepals. Highest expression in the senescent leaves. Expressed during early rosette development and during flowering. Up-regulated by antimycin A. No effect of ethylene or cold treatment. Unable to fully compensate for the loss of AOX1A when electron flow via the cytochrome pathway is restricted. Belongs to the alternative oxidase family. |
O03376 | MKNVLVRSAARALLGGGGRSYYRQLSTAAIVEQRHQHGGGAFGSFHLRRMSTLPEVKDQHSEEKKNEVNGTSNAVVTSYWGITRPKVRREDGTEWPWNCFMPWDSYHSDVSIDVTKHHTPKSLTDKVAFRAVKFLRVLSDIYFKERYGCHAMMLETIAAVPGMVGGMLLHLKSLRKFQHSGGWIKALLEEAENERMHLMTMVELVKPSWHERLLIFTAQGVFFNAFFVFYLLSPKAAHRFVGYLEEEAVISYTQHLNAIESGKVENVPAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASDIHHQGKELKEAPAPIGYH | Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity). 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O Binds 2 iron ions per subunit. Homodimer; disulfide-linked. Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. Continuous increase of expression in developing cotyledons until day 20. Belongs to the alternative oxidase family. |
Q9ZSQ3 | MAAISGISSGTLTISRPLVTLRRSRAAVSYSSSHRLLHHLPLSSRRLLLRNNHRVQATILQDDEEKVVVEESFKAETSTGTEPLEEPNMSSSSTSAFETWIIKLEQGVNVFLTDSVIKILDTLYRDRTYARFFVLETIARVPYFAFMSVLHMYETFGWWRRADYLKVHFAESWNEMHHLLIMEELGGNSWWFDRFLAQHIATFYYFMTVFLYILSPRMAYHFSECVESHAYETYDKFLKASGEELKNMPAPDIAVKYYTGGDLYLFDEFQTSRTPNTRRPVIENLYDVFVNIRDDEAEHCKTMRACQTLGSLRSPHSILEDDDTEEESGCVVPEEAHCEGIVDCLKKSITS | Acts early in chloroplast biogenesis as a component of a redox chain responsible for phytoene desaturation. Prevents the generation of toxic oxygen radicals and photooxidation of the nascent photosynthetic apparatus. Involved in the differentiation of multiple plastid types, including chloroplasts, amyloplasts, and etioplasts. Might participate in the chloroplast respiratory chain. 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O Binds 2 iron ions per subunit. localized to the stromal thylakoid lamellae. Ubiquitous. Expressed throughout the development of the leaves. Variegated cotyledons and leaves. The amount of white tissue increases with light intensity. Belongs to the alternative oxidase family. Truncated N-terminus. |
Q3MHE7 | MEGGSELLFYVNGRKVTEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKKIRHYPANACLTPICSLYGAAVTTVEGIGSTKTRIHPVQERIAKCHGTQCGFCTPGMVMSLYTLLRNHPEPTLTQLNDALGGNLCRCTGYRPIINACKTFCKTSGCCQSKENGVCCLDQGMNGLPEFEEGNETSLKLFSEEEFLPLDPTQELIFPPELMTMAEKKTQKTRIFGSDRMTWISPVTLKELLEAKVKYPQAPVVMGNTSVGPDMKFKGIFHPVIISPDRIEELSVVNYTDNGLTLGAAVSLAEVKDILANVTRKLPEEKTQMYHALLKHLETLAGPQIRNMASLGGHIVSRHPDSDLNPLLAVGNCTLNLLSKEGRRQIPLNEQFLRKCPSADLKPEEILISVNIPYSRKWEFVSAFRQAQRQQNALAIVNSGMRVCFGKGDGIIRELSIAYGGVGPTTILANNSCQKLIGRPWNEEMLDAACRLILDEVSLPGSAPGGRVEFKRTLIVSFLFKFYLEVSQILKGMDLVHYPSLASKYESALEDLHSRHYWSTLKYQNADLKQLSQDPIGHPIMHLSGIKHATGEAIYCDDMPVVDRELFLTFVTSSRAHAKIVSIDVSAALSLPGVVDILTGEHLPGINTTFGFLTDADQLLSTDEVSCVGQLVCAVIADSEVQARRAAQQVKIVYQDLEPVILTIEEAIQNKSFFEPERKLEYGNVDEAFKMVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDREIDVYVSAQFPKYIQDITASVLKVSANKVMCHVKRVGGAFGGKVTKTGVLAAITAFAANKHGRPVRCILERGEDILITGGRHPYLGKYKAGFMNDGRILALDMEHYNNAGAFLDESLFVIEMGLLKLENAYKFPNLRCRGWACRTNLPSNTALRGFGFPQAGLITEACITEVAAKCGLPPEKVRMINMYKEIDQTPYKQEINTKNLTQCWKECMATSSYTLRKAAVEKFNSENYWKKKGLAMVPLKYPIGLGSVAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPLSSIHLRGTSTETIPNTNPSGGSVVADLNGLAVKDACQTLLKRLKPIISKNPKGTWKDWAQAAFNESISLSATGYFRGYESNINWETGEGHPFEYFVYGAACSEVEIDCLTGAHKNIRTDIVMDVGYSINPALDVGQIEGAFIQGMGLYTIEELNYSPQGVLYTRGPNQYKIPAICDIPMELHISFLPPSENSNTLYSSKGLGESGIFLGCSVFFAIHDAIRAARQERGLPGPLRLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWSVPI | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Expressed at high levels in liver, lung and spleen. Also expressed in kindey, eye, testis, duodenum, esophagus and thymus (at protein level). The N-terminus is blocked. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
H0WDM9 | MEPSTLYFYVNGRRVTEKNVDPETMLLPYLGRNLRLTGTKYGCGGGGCGACTVMVSRYDRGTGQIRHYPACACLTPLCSLHGAAVTTVEGVGSTRTRLHPVQERIAKSHGTQCGFCTPGMVMSLYALLRSHPQPSEEQLLEALAGNLCRCTGYRPILDAGKTFCKTSGCCQSKENGVCCLDQGVNGVQEAEGEQTSQELCSEEEFVPLDPTQELIFPPELMILAQKQPQKSRVFTGDRVTWISPVTLKDLLEAKAKNPRAPVVMGNTSVGPEMKFKGVFHPVIISPDGIEELSVIKQGNEGLTLGAGLSLAQVQDVLADVVQQLPEEKTQTLCALLKQLRTLAGSQIRNMASLGGHIMSRHLDSDLNPVLAAASCTLHVPSQEGDRQIPLDEHFLSRSPSADLRPQEVLLSVTIPYSRKWEFVSAFRQAQRKRSARAIVNVGMRVFFGAGDGVISELCILYGGVGPAIVCATDACRKLVGRHWTEEMLDEACRLVLGEVAIPGAAPGGRVEFRRTLLVSFLFRFYLQVSQSLSRMDPGRYPSLVGKYESALEDLCLGHHQRTFELQSADAKQLPQDPIGRPIMHLSGIKHTTGEAIYCDDMPLVDRELSLAFVTSSRAHAAILSMDLSEALSLPGVVDIVTAEHLGDANSFAKETLLATDKVLCVGHLVCAVIADSEVQAKRAAEKVKIVYQDLEPLILTIEEAIQHDSFFETERKLESGDVAEAFRTAEQVLEGSIHMGGQEHFYMETQSMLAVPKGEDQEIDLYVSTQFPTYIQEIVASTLKLPVNKVMCHVRRVGGAFGGKVGKTAILAAITAFAALKHCRAVRCILERGEDMLITGGRHPYLGKYKVGFRNNGQVVALDMEHYSNAGSTLDESLMVVEMGLLKMENAYKFPNLRCRGHACKTNLPSNTALRGFGFPQSGLITEACIVEVAARCGLSPEEVREVNMYRGTEQTHYGQEIHTQRLAQCWSECKAKATFSLRRAAVDRFNAGSPWKKRGLAMVPLKFPVGLGSVAMGQAAALVHVYLDGSVLLTHGGIEMGQGVHTKMIQVVSRELKMPMANVHLRGTSTETVPNANVSGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKEWAQAAFDQSISLSAIGYFRGYDADMDWEKGKGHPFEYFVYGAACSEVEIDCLTGNHKNIRTDIVMDVGRSINPALDLGQVEGAFIQGMGLYTSEELKYGPQGALYTRGPDQYKIPAVCDVPAELHVFFLPPSKNSNTLYSSKGLGESGVFLGCSVLFAIWDAVSAARRERGLPGTLALSCPLTPEKIRMACEDRFTKMIPRDTPGSYVPWDVVV | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Inhibited by menadione and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor. Homodimer. Expressed in liver. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q9UPG6 | MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Is very potently inhibited by raloxifene (PubMed:26842593). Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione, isovanillin and thioridazine. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor (PubMed:22031625, PubMed:22522748, PubMed:22996261, PubMed:9224775, PubMed:26322824). kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation. Homodimer. Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level). Not detected in preadipocytes but strongly induced in mature adipocytes. In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:22335465). Belongs to the xanthine dehydrogenase family. Was originally thought to be a xanthine dehydrogenase. |
D6BND8 | MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITNRIRHHPANACLIPICSLYGTAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCETSGCCQSKENGVCCLDQRINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQPQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPQMKFKGVFHPVIISPDRIEELSVVNHTHNGLTLGAGLSLAQVKDILADVVQKLPGEKTQTYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKLEFVSAFRQAQRQENALAIVNSGMRVFFGEGHGIIRELSISYGGVGPATICAKNSCQKLIGRHWNEEMLDTACRLVLEEVSLSGSAPGGRVEFKRTLIISFLFKFYLEVSQILKKMDPIRYPSLADKHESALEDLHSKHHCSTLKYQHMGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDVITAEHLSDVNSFCFFTEAEEFLATDKVFCVGQLVCAVLADSEVQAKRAAKQVKIVYQDLEPLILTIKEAIQHNSFFEPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVKRVGGAFGGKAFKTGVIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGNSLDESLLVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAGLITESCIMEVAAKCGLSPEKVRMINMYKEIDQTPYKQEINAKNLIQCWRECMAVSSYSLRKAAVEKFNAENYWKKKGLAMVPLKYPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELGMPISNVHLRGTSTETVPNANVSGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESISLSAVGYFRGYESDINWEKGEGHPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGVLHTRGPDQYKIPAICDTPTEFHISLLPPSENSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARRERGLHGPLSLNSPLTPEKIRMACEDKFTKMIPRDEPGSCVPWNVPI | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis (By similarity). an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Detected at high levels in liver, also detected in lung, kidney, lacrimal gland and olfactory mucosa. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q9Z2Z5 | MDPIQLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKASACCQSKENGVCCLDQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERVTWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQKLPEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFLRKCPEADLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLIGRPWNEGMLDTRCRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKREDPGHSPSLAGNHESALDDLHSKHPWRTLTHQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQEANTFGTETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLILTIEEAIQHKSFFKSERKLECGNVDEAFKIVDQILEGEIHIGGQEHFYMETQSMLVVPKGEDGEIDIYVSTQFPKYIQDIVAATLKLSANKVMCHVRRVGGAFGGKVGKTSILAAITAFAASKHGRAVRCILERGEDMLITGGRHPYLGKYKAGFMNEGRILALDVEHYCNGGCSLDESLWVIEMGLLKLDNAYKFPNLRCRGWACRTNLPSNTALRGFGFPQAGLVTEACITEVAIKCGLSPEQVRTINMYKHVDTTHYKQEFSAKALSECWRECMAKCSYFERKAAIGKFNAENSWKKRGMAVIPLKFPVGIGSVAMGQAAALVHIYLDGSALVSHGGIEMGQGVHTKMIQVVSRELRMPMSSVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPIISKNPQGTWKDWAQTAFDQSISLSAVGYFRGYESNIDWEKGEGHPFEYFVFGAACSEVEINCLTGDHKNIRTNIVMDVGHSINPALDIGQVEGAFIQGMGLYTIEELSYSPQGTLYSRGPNQYKIPAICDIPTEMHISFLPPSEHSNTLYSSKGLGESGVFLGCSVFFAIHDAVKAARQERGISGPWKLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPCNIPV | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use xanthine and hypoxanthine as substrate. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and pH 7.5) (PubMed:19401776). However in this article, the measures are done with the recombinant protein, which is only 20% active, due to an incomplete saturation of the molybdenum cofactor with the sulfido ligand (PubMed:19401776). Homodimer. Highest expression in esophagus. Moderately low expression in lung, liver, heart, Harderian gland, olfactory mucosa, skin and testis. In brain, expression is very high in choroid plexus, high in hind brain and low in hippocampus and cerebellum. In spinal cord expression is strongest in anterior horns. Low expression detected in spleen and eye. AOX1 expression in the livers of mice is approximately seven times greater in males than females. Expressed in adult liver but not in neonatal or embryonic liver. Not detected in preadipocytes but strongly induced in mature adipocytes. Repressed by pioglitazone, fenofibrate and PPARA agonists. Induced by testosterone. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q9XTA9 | MEPAPELLFYVNGRKVVEKQVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNRVTKKIRHYPVNACLTPICSLYGAAVTTVEGIGSTTTRLHPVQERIAKFHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLADALGGNLCRCTGYRPIIEAYKTFCKTSDCCQNKENGFCCLDQGINGLPEVEEENQTRPNLFSEEEYLPLDPTQELIFPPELMTMAEKQPQRTRVFSGERMMWISPVTLKALLEAKSTYPQAPVVMGNTSVGPGVKFKGIFHPVIISPDSIEELNVVSHTHSGLTLGAGLSLAQVKDILADVVQKVPEENAQTYRALLKHLGTLAGSQIRNMASLGGHIISRHLDSDLNPLLAVGNCTLNVLSKEGERQIPLDEQFLSRCPEADLKPQEILASVHIPYSRKWEFVLAFRQAQRKQNALAIVNSGMRVFFGEGDGIIRELAISYGGVGPTIICAKNSCQKLIGRSWNEEMLDTACRLILDEVSLPGSAPGGKVEFKRTLIISFLFKFYLEVSQILKRMAPGLSPHLADKYESALQDLHARYSWSTLKDQDVDARQLSQDPIGHPVMHLSGVKHATGEAIYLDDMPAVDQELFMAFVTSPRAHAKIVSTDLLEALSLPGVVDIVTAEHLQDGNTFYTEKLLAADEVLCVGQLVCAVIAESEVQAKQAAKQVKIVYEDLEPVILSIEEAIEQKSFFEPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSVLVVPKGEDQEMDVYASTQFPKYIQDMVAAVLKLPVNKVMCHVKRVGGAFGGKVFKASIMAAIAAFAANKHGRAVRCILERGEDMLITGGRHPYLGKYKAGFMNDGRIVALDVEHYSNGGCSLDESLLVIEMGLLKMENAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAGLITECCITEVAAKCGLSPEKVRAINFYKEIDQTPYKQEINAKNLTQCWNECLAKSSYFQRKVAVEKFNAENYWKQRGLAIIPFKYPRGLGSVAYGQAAALVHVYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELKMPMSNVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPIINKNPQGTWKEWAQAAFDKSISLSATGYFRGYDSNIDWDKGEGHPFEYFVYGAACSEVEIDCLTGDHKTIRTDIVMDVGYSINPALDIGQVEGAFIQGMGLYTIEELHYSPQGILYSRGPNQYKIPAICDIPAELNVTFLPPSEKSNTLYSSKGLGESGVFMGCSVFFAIREAVCAARQARGLSAPWKLSSPLTPEKIRMACEDKFTKMIPRDKPGSYVPWNVPV | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use hypoxanthine and all-trans-retinol as substrate. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate all-trans-retinal + H2O + O2 = all-trans-retinoate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Inhibited by hydralazine and menadione. Not inhibited by BOF-4272 or allopurinol, xanthine dehydrogenase potent inhibitors. In contrast to guinea pig, human and rat, isovanillin is not an inhibitor but a substrate for AOX1 in rabbit. Homodimer. Very high expression in liver and lung. High expression in kidney, pancreas, brain stem and spinal cord. Moderate expression in heart, testis, eye, cerebral cortex and cerebellum. Low expression in stomach and muscle. The N-terminus is blocked. The reaction follows an ordered Bi-Bi kinetic mechanism. During retinal oxidation, incorporates the oxygen of water into retinoate, but not that of molecular oxygen (PubMed:8305467). AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q9R240 | MDPPQLLFYVNGQKVVENNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKSIRHHPVNACLTPICSLYGTAVTTVEGIGNTRTRLHPVQERIAKCHSTQCGFCTPGMVMSMYALLRNHPEPSLDQLTDALGGNLCRCTGYRPIIDACKTFCRASGCCESKENGVCCLDQGINGSAEFQEGDETSPELFSEKEFQPLDPTQELIFPPELMRIAEKQPPKTRVFYSNRMTWISPVTLEELVEAKFKYPGAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELSIINQTGDGLTLGAGLSLDQVKDILTDVVQKLPEETTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGKRQIPLSEQFLRKCPDSDLKPQEVLVSVNIPCSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIKELSILYGGVGPTTIGAKNSCQKLIGRPWNEEMLDTACRLVLDEVTLAGSAPGGKVEFKRTLIISFLFKFYLEVLQGLKREDPGHYPSLTNNYESALEDLHSKHHWRTLTHQNVDSMQLPQDPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQDATTFGTETLLATDKVHCVGQLVCAVIADSETRAKQAAKHVKVVYRDLEPLILTIEEAIQHKSFFESERKLECGNVDEAFKIADQILEGEIHIGGQEHFYMETQSMLVVPKGEDGEIDIYVSTQFPKHIQDIVAATLKLSVNKVMCHVRRVGGAFGGKVGKTSIMAAITAFAASKHGRAVRCTLERGEDMLITGGRHPYLGKYKVGFMRDGRIVALDVEHYCNGGSSLDESLWVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSHTALRGFGFPQAGLVTEACVTEVAIRCGLSPEQVRTINMYKQIDNTHYKQEFSAKTLFECWRECMAKCSYSERKTAVGKFNAENSWKKRGMAVIPLKFPVGVGSVAMGQAAALVHIYLDGSALVSHGGIEMGQGVHTKMIQVVSRELKMPMSSVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPIISKNPQGTWKDWAQTAFDQSVSLSAVGYFRGYESNINWEKGEGHPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGHSINPALDIGQVEGAFIQGMGLYTIEELSYSPQGILYSRGPNQYKIPAICDIPTEMHISFLPPSEHSNTLYSSKGLGESGVFLGCSVFFAIHDAVRAARQERGISGPWKLTSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNIPV | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. Is a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also catalyzes nitric oxide (NO) production; under anaerobic conditions, reduces nitrite to NO with NADH or aldehyde as electron donor, but under aerobic conditions, NADH is the preferred substrate. These reactions may be catalyzed by several isozymes. May play a role in adipogenesis. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Inhibited by menadione and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor. Inhibited by the flavonoids quercetin, myricetin and genistein. Nitric oxide generation is inhibited by raloxifene and competitively inhibited by an increase in oxygen levels. Optimum pH is 6.0 for nitrite oxide generation. Activity decreases below pH 5.0 and above pH 8.0 (PubMed:19801639). Homodimer. Expression in liver (at protein level). Also detected in heart, lung, spleen and kidney. The N-terminus is blocked. The sequence variants between males and females could be due to differences between individual animals, reflect gender differences or arise from technical problems (PubMed:9920943). The sequence shown here is that of a Sprague-Dawley female. Male and female rats possess kinetically distinct forms which may be due to differences in redox states. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. The experimental design does not allow to distinguish AOX1 from AOX3 in rat liver as the effector of the superoxide and nitric oxide production (PubMed:17353002 and PubMed:19801639). |
H9TB19 | MPHPPGSDVLVFFVNGRKVTERDVDPEVTLLTYLRRNLGLTGTKSACGGGSCGTCTVMLSRFDLASRKPRHIAVTACLVPLCSLHGAAVTTVEGVGSIRTRVHPVQERIAKSHGTQCGFCTPGMVMSLYALLRSHPQPSEEQLLEALAGNLCRCTGYRPILESGRTFCLDSASCGQHGARQCCLDQPGDGTCPPGRNGPQAHMCSELIPRTEFQPWDPTQEPIFPPELMRMAESPVQPSLTFRGDRVTWVSPGSLQELLALRARHPEAPLVLGNTALGPAQRSQGRVHPLLISPARIPELSTVTETSDGLTIGASCSLAQLQDILAKSISQLPVEKTQTLRALAKALRSVAGLQVRNLASLGGHVMSLHSYSDLNPILAVGQAALHLRSEGGARLISLDEHFLAGVVSASLQPGEILESVHIPHSQKWEFVFSFRQAQAPQNASPHVSAGMRVRFTEGTDTIEDLSIAYGGVGTTTVMAPQACQRLLGRHWTEETLDEACRLVLGEVTIPGAAPGGRVEFRRTLLVSFLFRFYLQVLQELKAHRFLKPPCTPRTLSDTWKYPQLPDQTLGALEDVPIMVPRGVQMYERVDPQQPPQDPVGRSIMHLSGLKHATGEAVFCDDLPRVDKELFMALVTSTRPHAKIVSVDPAEALRLPGVVAIVTAEDIPGTNGTEDDKLLAVDKVLCVGQVICAVVAETDVQARQATGSVRVTYEDLEPVVLSIQDAIGHSSFLCPEKKLELGNTEEAFEDVDHILEGEVHVGGQEHFYMETQRVLVIPKVEDQELDIYASTQDPAHMQKTVSSTLNVPLNRVTCHVKRVGGGFGGKQGRSAMLGAIAAVGAIKTGRPVRLVLDRDEDMLITGGRHPLFGKYKVGFMDSGRIKALDIQCYINGGCVLDYSELVIEFLILKLENAYKIRNLRFRGRACRTNLPSNTAFRGFGFPQGALVIESCITAVAAKCGLLPEKVREKNMYRTVDKTIYKQAFSPEPLHRCWAECLEQADVPGRRALADAFNRQSPWRKRGIAVVPMKFSVGFAATSYHQAAALVHIYTDGSVLVTHGGNELGQGIHTKMLQVASRELRVPLCRLHIQETSTATVPNTVTTAASVGADVNGRAVQNACQTLLKRLEPIMKKNPEGTWEAWVEAAFEQRISLSATGYFRGYKAFMDWEKGEGEPFPYCVFGAACSEVEIDCLTGAHRKLRTDIVMDAGCSLNPALDIGQVEGAFLQGAGLYTTEELHYSPEGALLSGGPEEYKIPTAADVPEKLNVTLLPSAQAQTGLTIYSSKGLGESGMFLGSSVFFAIQDAVAAARRDRGLAEDFTVPREDPGTCKPWSISVA | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Detected in kidney, Harderian gland and olfactory mucosa. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
G7PL56 | MRCASRSDELVFFVNGRKVMERNVDPEGTLLTFLRKNLRLTGTKYACGRGGCGACTVMVSKHDPVSRKIQRHFSVTACLMPICSLYGAAVTTVEGVGSIKTRLHPVQERIAKSHGTQCGFCTPGMVMSMYTLLRNHPQPSEEQLTEALGGNLCRCTGYRPILESGRTFCMESNSCQQKGTGKCCLDWGENDSSRLGKKNEICTKLFAKEEFQSLDPTQELIFPPELLRMAENPEKRTLTFYGERVTWISPGTLKDLLELKVKHPEAPLVVGNTSLGPAMKSQRQFHPVLLSPARISELSMVTKTSDGLTIGAGCSLAQTQDILAERIAELPEEKTQTYRALLKHLRSLAGQQIRNMASLGGHVISRHCCSDLNPVLAVSNATLNLISAEGTRQIPLNEHFLAGLASADLKPEEILESVHIPHSQKWEFVSAFRQAQCQQNALPHVNAGMRVLLKEGTDSIEDLSIAYGGVGAATISAHRSCQQLLGRRWNELMLDEACRLLLDEVSLPGSAPGGRVEFKRTLVVSFLFKFYLEVLQELKKLVKLFSVAVGADSRHRSEVSDQFLSALEDFPVTIPQGVQTYQNVDPHQPLQDPVGRPIMHLSALKHATGEAMFCDDIPVVDKELFMALVTSSRAHAKIISIDVSKALELPEVVDVITAEDIPGTNGAEGDKLLAVEEVTCVGQIICAVVAETDVQAKRATEKIEITYEDLEPVIFTIKDAIKHNSFLCPEKKLEQGNVEEAFEKVDQTIEGEVHVGGQEHFYMETQRVLVIPKTEDKELDIYVSTQDPAHVQKTVSSTLNIPINRITCHVKRVGGGFGGKVGKPAVFGAIAAVGAIKTGHPIRLVLDREDDMLITGGRHPLFGKYKVGFTNNGRIKALDIECYINGGCTLDDSELVTEFLILKLENAYKIRNLRFRGRACMTNLPSNTAFRGFGFPQGALVTESCITAVAAKCGLPPEKIREKNMYKTVDKTIYKQAFNPETLIRCWNECLDKSSFHSRRMQVEEFNKKNYWKKKGIAIIPMKFSVGFAATSYHQAAALVHIYTDGSVLVTHGGNELGQGIHTKMLQVASRELKIPMSCIHISETSTATVPNTIATAASVGADVNGRAVQNACQILLKRLEPIIKKHPEGTWENWIEAAFEQRISLSATGYFRGYKAFMDWEKGVGDPFPYYVYGAACSEVEIDCLTGAHKKIRTDIIMDACCSLNPAIDIGQIEGSFIQGMGLYTTEELKYSPEGILYSRSPDEYKIPTITDVPEEFNVSLLPSSQTPLTIYSSKGLGESGMFLGSSVFFAIADAVATVRRERDIAEDFMVQSPATPERVRMACADRFTKMIPRDDPETFKPWSIPIA | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Only detected at very few levels in nasal mucosa. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
B9EKC6 | MPCPAQISDDLEFFVNGRKVTEKNVDPEVTLLAFLRKNLCLTGTKDACGTGGCGACTVMVSQHDPVCKKTRHFSVMACLVPLCSLHGAAVTTVEGVGSIKTRLHPVQERIAKSHGTQCGFCTPGMVMSIYTLLRNHPQPSEEQLMEALGGNLCRCTGYRPILESGRTFCMEPDGCPQKGTGQCCLDQKESDSSGSKSDICTKLFVKDEFQPLDPTQELIFPPELLRMAENPEKQTLTFYGERITWIAPGTLQELLVLKAKYPEAPLISGNTALGPAMKSQGHFYPVLLSPARIPDLRMVTKTSGGLTIGACCSLAQVKDILAESISELPQEKTQTYRALLKHLRSLAGQQIRNMASLGGHVISRHCYSDLNPILSVGNTTLNLLSEEGPRQIPLSGHFLAGLASADLKPEEILGSVYIPHSQKREFVSAFRQAQCHQNALPDVNAGMRVLFREGTDVIEELSIAYGGVGPTTVSAQRSCQQLLGRRWNALMLDEACRLLLDEVSLPGSALGGKVEFRRTLIVSLFFKFYLEVLQELKADQKLPPESTDSQRYPEIADRFLSSLGDFQVTLPRGVQTYQRVDSHQPLQDPVGRPIMHLSGLKHATGEAVFCDDIPRVDKELFMALVTSTRAHARIISIDSSEVLDLPGVVDVITAEDIPGNNGEEDDKLLAVDKVLCVGQVICAVVAETDVQAKRATEKIKITYEDLKPVIFTIEDAIKHNSFLCPEKKLEQGNIEEAFENVDQVAEGTVHVGGQEHFYMETQRVLVIPKTEDKELDMYVSTQDPAHVQKTVSSTLNIPISRITCHVKRVGGGFGGKVGRPAVFGAIAAVGAVKTGHPIRLVLDREDDMLITGGRHPLFAKYKVGFMNSGRIKALDIECYINGGCTLDDSELVTEFLVLKLENAYKIRNLRLRGRACMTNLPSNTAFRGFGFPQGALVTESCITAVAAKCGLPPEKIREKNMYKTVDKTIYKQAFNPDPLIRCWNECLDKSSFHIRRTRVDEFNKKSYWKKRGIAIVPMKFSVGFAATSYHQAAALVHIYTDGSVLVAHGGNELGQGIHTKMLQVASRELKIPLSYLHICETSTTTVPNTIATAASVGADVNGRAVQNACQILLKRLEPVIKKNPEGTWRDWIEAAFEKRISLSATGYFRGYKAFMDWEKGEGDPFPYYVYGAACSEVEIDCLTGAHKKIRTDIVMDACCSLNPAIDIGQIEGAFIQGMGLYTTEELLYSPEGVLYSRSPDKYKIPTVTDVPEQFNVSLLPSSQTPLTLYSSKGLGESGMFLGSSVFFAIVDAVAAARRQRDIAEDFTVKSPATPEWVRMACADRFTDMIPRDDPKTFKPWSIPIA | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Expressed in olfactory mucosa epithelium (at protein level). Detected in skin. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
D4A6S5 | MPCPSQSSDELEFFVNGKKVTEKNVDPEVTLLAFLRKNLRLTGTKYACGTGSCGACTVMVSQHDPVCKKTRHFSVMACLVPLCSLHGAAVTTVEGVGSIKTRLHPVQERLAKSHGTQCGFCSPGMVMSMYALLRNHPQPSEEQLLEALGGNLCRCTGYRPILESGRTFCMESDGCLQKGTGQCCLDQKEGDSSGSKSDICTELFVKDEFQPLDPTQELIFPPELLRMAENPEKQTLTFYGERITWIAPGTLQELLVLKAKYPEAPLISGNTALGPAMKSQGHFYPVLLSPARIPDLRMVTKTSGGLTIGACCSLAQVKDVLAESISELPEEKTQTYRALLKHLRSLAGQQIRNMASLGGHVISRHYYSDLNPILSVGNATLNLLSEEGLRQIPLNGHFLAGLANEDLKPEEILGSVYIPHSQKREFVSAFRQAQCHQNALPDVNAGMRVLFKEGTDIIEELSIAYGGVGPTTVSAHRSCQQLLGRRWNALLLDEACRLLLDEVSLPGSAVGGKVEFRRTLIVSFFFKFYLEVLQELKADKRLLPESTDSQRYPEIADGSRSSLGDFQVTLPQGVQTYQRVNSHQPLQDPVGRPIMHLSGLKHATGEAVFCDDIPRVDKELFMALVTSTRAHARIISIDSSEVLDLPGVVDVITAEDIPGNNGEEDDKLLAVDKVLCVGQVVCAVVAETDVQAKRATKKIKITYEDLKPVLFTIEDAIQHNSFLCPEKKLEQGNMEEAFENVDQIVEGKVHVGGQEHFYMETQRVLVIPKTEDKELDMYVSTQDPAHVQKTVSSALNIPLSRITCHVKRVGGGFGGKVGRPAVFGAIAAVGAVKTGRPIRLVLDREDDMLITGGRHPLFAKYKVGFMNSGRIKALDIECYINGGCTLDDSELVTEFLVLKLENAYKIRNLRLRGRACMTNLPSNTAFRGFGFPQGALVTESCITAVAAKCGLPPEKIREKNMYKTVDKTIYKQAFNPEPLIRCWNECLDKSSFAIRRTRVDEFNKKSYWRKRGIAVVPMKFSVGFAATSYHQAAALVHIYTDGSVLVAHGGNELGQGIHTKMLQVASRELKIPMSYLHTSETCTAAVPNTIATAASVGADVNGRAVQNACQILLKRLEPVIKKNPEGTWRDWIEAAFEQRISLSATGYNRGYKAFMDWEKGEGDPFPYYVYGAACSEVEIDCLTGAHKKMRTDIVMDACCSLNPAIDVGQIEGAFIQGMGLYTTEDVHYSPEGVLYSRSPDKYKIPTVTDVPEQFNVSLLPSSQTPLTIYSSKGLGESGMFLGSSVFFAIADAVAAARRQRDIAEDFTVKSPATPERVRMACADRFTDMIPRDDPKTFKPWSIPIA | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q8VI15 | MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEGKCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGERTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNTKQGLTLGAGLSLTQVKNVLSDVVSRLPKEKTQIYCALLKQLKTLAGQQIRNVASLGGHIISRLPTSDLNPILGIGNCILNVASTEGIQQIPLNDHFLAGVPDAILKPEQVLISVFVPRSSKWEFVSAFRQAPRQQNAFATVNAGMKVVFKEDTNTITDLGILYGGIGATVISADKSCRQLIGRCWDEEMLDDAGKMICEEVSLLMAAPGGMEEYRKTLAISFLFMFYLDVLKQLKTRDPHKYPDISQKLLHILEDFPLTMPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFCDDMSVLPGELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGREEESLYAQDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIEPMIVTVQDALQYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDIYVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRPIRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVRELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFVQSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYSSKGLGEAGTFLGCSVFFAIAAAVAAAREERGLSPIWAINSPATAEVIRMACEDQFTNLVPQTDSKCCKPWSIPVA | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Inhibited by potassium cyanide, menadione, benzamidine, raloxifene and norharmane. kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine oxidation (PubMed:21705476). kcat is 41.1 min(-1) for phthalazine oxidation, 41.9 min(-1) for benzaldehyde oxidation, 14.7 min(-1) for N1-methylnicotinamide oxidation and 51.7 min(-1) for phenanthridine oxidation (PubMed:23019336). Homodimer. Highly expressed in liver (at protein level). In liver, the expression is greater in males than females. Induced by testosterone. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q5QE80 | MSRSKESDELIFFVNGKKVIERNADPEVNLLFYLRKIIQLTGTKYGCGGGDCGACTVMISRYNPISKKISHFSAAACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESARSFSPNSACCPMNEKWKCCLDEGKNEPERKNSVCTKLYEKEEFQPLDPTQELIFPPELMRMAEDSPNTVLTFRGERTTWIAPGTLNDLLELKMEYPSAPLVIGNTCLGLDMKFKDVSYPIIISPARILELFVVTNTNEGLTLGAGLSLTQVKNILSDVVSRLPKERTQTYRALLKHLRTLAGQQIRNVASLGGHIISRLPTSDLNPIFGVGNCKLNVASTEGTQQIPLNDHFLAGVPEAILKPEQVLISVFVPLSRKWEFVSAFRQAPRQQNAFAIVNAGMRVAFKEDTNTITDLSILYGGIGATVVSAKSCQQLIGRCWDEEMLDDAGRMIREEVSLLTAAPGGMVEYRKTLAISFLFKFYLDVLKQLKRRNPHRCPDISQKLLQVLEDFPLTMPHGTQSFKDVDSQQPLQDQSGRPIMHQSGIKHATGEAVFCDDMSVLAGELFLAVVTSSKPHARIISLDASEALASPGVVDVITAQDVPGDNGREEESLYAQDEVICVGQIVCAVAADSYARAKQATKKVKIVYEDMEPMIVTVQDALQHESFIGPEKKLEQGNVQLAFQSADQILEGEVHLGGQEHFYMETQSVRVIPKGEDMEMDIYVSSQDAAFTQEMVARTLGIPKNRITCHVKRVGGGFGGKTSKPGLLASVAAVAAQKTGRPIRFILERGDDMLITGGRHPLLGKYRVGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTGTWVSAVAAKCHLPPEKVRELNMYKTIDRTIHKQEFDPTNLIKCWETCMENSSYYSRKKAVDEFNQQSFWKKRGIAIIPMKFSVGFPKTFYHQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMNTMTVPNTITTGGSTGADVNGRAVQNACQILMKRLEPIISQNPNGDWEEWINEAFIQSISLSATGYFRGYQADMDWEKGEGDIYPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVSDIPEEFHVSLLTPTQNPKAIYSSKGLGEAGMFLGSSVFFAIAAAVAAARKERGLPLILAINSPATAEVIRMACEDQFTNLVPKTDSKCCKPWSIPVA | Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. Is a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also catalyzes nitric oxide (NO) production; under anaerobic conditions, reduces nitrite to NO with NADH or aldehyde as electron donor, but under aerobic conditions, NADH is the preferred substrate. These reactions may be catalyzed by several isozymes. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. The experimental design does not allow to distinguish AOX1 from AOX3 in rat liver as the effector of the superoxide and nitric oxide production (PubMed:17353002 and 19801639). |
H9TB18 | MPSLSGSDELIFFVNGKKVVVKKPDPEVTLLFYLRRELHLTGTKFACGEGGCGACTVMVSRYSASSKQIRHYPVTACLVPICSLHGAAVTTVEGVGSIRTRVHPVQERLAKCHGTQCGFCSPGMVMSIYTLLRNHPDPTPEQVTEALGGNLCRCTGYRPIVESGKTFCANPTVCQVKRPGRCCLEQEEEEAGSVHTREKMCTKLYDKDEFQPLDPSQEPIFPPELIRMAEDPNKRRLTFQGERTTWLAPATLPDLLELRAEFPQAPLIMGNTTVGPDIKFKGEFHPVFVSPLELPELCVLNSEGDGVTVGSGHSLAQLSDALQSIVSQQPSERTETCRALLNHLRTLAGVQIRSMATLGGHVATRATVSDLNPILAAGKTTIHLVSKEGERQIPLDGAFLEGSPRAGLRPGEIVLSVFIPYSSQWQFVSGLRQAQRQENAMAIVNAGMSVRLEDGSSTIRDLQVFYGGIGPTVLSASRTCGQLVGRQWDDQMLGEACRGILDELRLPPGAKGGQVEFRHTLMLSLLFKFYLRVQRALSKLDPQKFPDIPEEYTSALEEFPIGTPQGTQIFRCVDPHQPPQDPVGHPVMHQAGLKHATGEAAFVDDLPLVSQELFLAVVTSTRAHAKIISIDTGEALALPGVVAVITAEDVPGENNHQGEIFYAQREVVCVGQIVCTVAADTYAHAREAAQKVKVEYEDIEPRIITIEQALEHSSFLSPERKIEQGNVEQAFKHVDQVIEGEVHVEGQEHFYMETQTILAVPRAEDKEMVLHLGTQFPTHVQEFVATALNVPRNRIACHMRRAGGAFGGKVTKPALLGAVAAVAAKKTGRPIRFVLERGDDMLITAGRHPLLGRYKVGFMKSGLIKAVDLEFYINGGCTPDESQLVIEYVVLKSENAYYIPNFRCRGRACKTNLPSNTAFRGFGFPQATVVVEAYMTAVASHCDLLPEEVREMNMYKRPSQTAYRQRFDPEPLRRCWKDCLEHSSFHARKRAAEDFNRQSRWKKRGLAMIPMKYTIGVPVAYYHQAAALVHIYLDGSVLLTHGGCELGQGLHTKMMQVASRELGIPTSYIHLSETSTVTVPNAVFTAGSMGTDINGKAVQNACQTLMARLQPVIRRNPKGKWEEWIKKAFEESISLSATGYFRGFQTNMDWDKERGDAFPYYVYGAACAEVDVDCLSGAHKLLRADIFMDAAFSINPAVDIGQIEGAFVQGMGLYTTEELKYSPKGKLRSQGTNDYKIPTVTEIPEEFHVTLVHSRNPVAIYSSKGLGEAGMFLGSSVISAIWDAVAAARKERKGAESVPETLAVRSPATPEWIRMACVDQFTDMIPRDDPSTFTPWSICVS | Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles (By similarity). an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Detected in liver, testis, kidney, brain, Harderian gland and olfactory mucosa. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q8VI17 | MPSVSESDELIFFVNGKKVIEKNPDPEKNLLFYTRKVLNLTGTKYSCGTGGCGACTVMVSRYNPKTRKIHHYPATACLVPICWLHGAAITTVEGVGSIKKRVHPVQERLAKCHGTQCGFCSPGMVMSIYTLLRNHPEPTPDQITEALGGNLCRCTGYRPIVESGKTFSQKSTVCQMKGSGKCCMDPDEKCLESREKKMCTKLYNEDEFQPFDPSQEPIFPPELIRMAEDPNKRRLTFQGKRTTWIIPVTLNDLLELKASYPEAPLVMGNTTVGPGIKFNDEFYPVFISPLGVPELNLMDTTNNGVTIGAGYSLAQLKDTLDFLVSEQPKEKTKTFHALQKHLRTLAGPQIRNMATLGGHTASRPNFSDLNPILAAGNATINVVSREGKDRQLPLNGPFLEKLPEADLKPEEVILSIFIPYTAQWQFVSGLRLAQRQENAFAIVNAGMSVEFEEGTNTIKDLKMFFGSVAPTVVSASQTCKQLIGRQWDDQMLSDACQLVLQEIRIPPDAEGGMVEYRRTLIISLLFKFYLKVQRWLNEMDPQKFPDIPGKFVSALDDFPIETPQGIQMFQCVDPKQPQKDPVGHPIMHQSGIKHATGEAIFIDDMPPIDQELCLAVVTSTRAHAKITSLDVSEALACPGVVDVITAEDVPGENDHNGEILYAQSEVICVGQIICTVAADTYIHAKEAAKRVKIAYDDIEPTIITIEEALEHNSFLSPEKKIEQGNVDYAFKHVDQIVEGEIHVEGQEHFYMETQTILAIPQTEDKEMVLHLGTQFPTHVQEFVSAALNVPRSRIACHMKRAGGAFGGKVTKPALLGAVCAVAANKTGRPIRFILERSDDMLITAGRHPLLGKYKIGFMNNGEIRAADVEYYTNGGCTPDESELVIEFVVLKSENTYHIPNFRCRGRACKTNLPSNTAFRGFGFPQATVVVEAYIAAVASKCNLLPEEVREINMYKKTSKTAYKQTFNPEPLRRCWKECLEKSSFFARKKAAEEFNGNNYWKKRGLAVVPMKFSVAVPIAFYNQAAALVHIFLDGSVLLTHGGCELGQGLHTKMIQVASRELNVPKSYVHFSETSTTTVPNSAFTAGSMGADINGKAVQNACQILMDRLRPIIRKNPKGKWEEWIKMAFEESISLSATGYFKGYQTNMDWKKEEGDPYPYYVYGAACSEVEVDCLTGAHKLLRTDIFVDAAFSINPALDIGQVEGAFIQGMGFYTTEELKYSPKGVLYSRGPEDYKIPTITEIPEEFYVTLVHSRNPIAIYSSKGLGEAGMFLGSSVLFAIYDAVTTARKERGLSDIFPLNSPATPEVIRMACTDQFTEMIPRDDPSTFTPWSIHVS | Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans-retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate all-trans-retinal + H2O + O2 = all-trans-retinoate + H(+) + H2O2 Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. Highly expressed in Harderian glands and sebaceous glands with detectable levels in the epidermis and other keratinized epithelia (at protein level). Detected in testis. The expression is 3 times greater in females than in males. Repressed by testosterone in Harderian glands. In skin, induced by UVB light. Mice are viable, fertile and born at the expected Mendelian rate. However, they show a deficiency of retinoic acid synthesis in both the Harderian gland and skin. The Harderian gland's transcriptome of knockout mice demonstrates overall down-regulation of direct retinoid-dependent genes as well as perturbations in pathways controlling lipid homeostasis and cellular secretion, particularly in sexually immature animals. The skin is characterized by thickening of the epidermis in basal conditions and after UVB light exposure. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
Q5QE79 | MPSSSDELIFFVNGKKVIEKNPVPEMNLLFYVRKVLHLTGTKYSCGGGGCGACTVMISRYNPESKKIYHYPATACLVPVCSLHGAAVTTVEGVGSIKRRIHPVQERLAKCHGTQCGFCSPGMVMSIYTLLRNHPEPTPDQITEALGGNLCRCTGYRPIVESGKTFSPESSVCQMKGSGKCCMDLDEGCSESTKERMCTKLYNEDEFQPLDPSQEPIFPPELIRMAEDPHKRRLTFQGERTIWIMPVTLNGLLELKASYPEAPLVMGNTAVGPGMKFNNEFHPVFISPLGLPELNLVDTANSGGVTIGARHSLAQMKDILHSLTLEQPKEKTKTHQALLKHLRTLAGPQIRNMATLGGHVVSRPDFSDLNPILAAGNATINVISKEGQRQIPLNGPFLERLPEASLKPEEVALSVFIPYSGQWQYVSGLRLAQRQENAFAIVNAGMSVEFEEGTNTIKDLQMLFGSVAPTVVSASQTCKQLIGRQWDDQMLSDACQLVLEEIRIPPDAEGGMVEYRRTLIISLLFKFYLKVRRWLSEMDPQKFPDIPEKFVSALDDLPIETPQGIQMFQCVDPNQPEQDPVGHPIMHQSGIKHATGEAKFVDDMPRINQELCLTVVTSTRAHAKITSIDVSEALAYPGVVDVITAEDVPGDNNHSGEIFYAQNEVICVGQIICTVAADTYIHAKEAAKRVKITYDDIEPAIITIEQALEHNSFLSSEKKIEQGNVDYAFKHVDHIIEGEIHVEGQEHFYMETQTILAIPQTEDKEMVLHVGTQFPTHVQEYVSAALKVPRNRIACQMKRTGGAFGGKVTKPALLGAVCAVAAHKTGRPIRFILDRSNDMLITAGRHPLLGKYKIGFMNNGKIKAADVEYYTNGGCTPDESEMVIEFIVLKSENAYHIPNFRCRGRACKTNLPSNTAFRGFGFPQATVVVEAYIAAVASKCNLLPEEIREINMYKQISKTAYKQTFNPEPLRRCWKECLQKSSFFARKQAAEEFNKNNYWKKKGLAVVPMKFSVAVPMAFYNQAAALVHIFLDGSVLLTHGGCELGQGLHTKMIQVASRELNIPKSYVHLVETSTVTVPNAVFTAGSMGADINGKAVQNACQTLLDRLQPIIKKNPKGKWEEWVKKAFEESISLSATGYFKGYQTNMDWEKEEGDPYPYYVYGAACSEVEVDCLTGAHKLLRTDIFMDAAFSINPALDIGQVEGAFIQGMGFYTIEELKYSPKGVLYSRGPDDYKIPTVTEIPEEFYVTMVRSRNPIAIYSSKGLGEAGMFLGSSVLFAIYDAVTTARKERGLSDIFPLNSPATPEVIRMACKDQFTDMIPRDDPSTFTPWSIHVS | Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles (By similarity). an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate Binds 2 [2Fe-2S] clusters per subunit. Binds 1 FAD per subunit. Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Homodimer. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. |
D3DVY7 | MVHAFLIHTLRAPNTEDTGLCRVLYSCVFGAEKSPDDPRPHGAERDRLLRKEQILAVARQVESMCRLQQQASGRPPMDLQPQSSDEQVPLHEAPRGAFRLAAENPFQEPRTVVWLGVLSLGFALVLDAHENLLLAEGTLRLLTRLLLDHLRLLAPSTSLLLRADRIEGILTRFLPHGQLLFLNDQFVQGLEKEFSAAWPR | As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862, it is required for efficient homologous recombination DNA double-strand break repair. Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11. |
A2ANC8 | MVHAFLIHTLRAPNLEDTGLCRVLYSCVFGAEKSPDDPRSHGAERDRLFRKEQILAVARQVESLCRLQQQAAGCSSTDLQPQFSAEPVSLHEAPHGAFHLAAGDPFQEPRTVLWLGILSLGFALVLDTHENLLLAERTLRLLARLLLDHLRLLTPAVSTGAAYCRAHPSR | As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11 (By similarity). |
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