UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
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A0A1L9WN42
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MLLPSFPVTGVATALLLRNAVHASQPGSSVQKARAYDRFSSRPTRDHAPRVQSSNTSTYRFWNDKTKPHLVESLPDVHFDLGEMYSGSINITSHRNESRSLFYIFQPKIGEPSDDLTIYLNGGPGCSSEQAFFQENGRFTWQPGTYAPVINQYSWVNLTNMLWVDQPVGTGYSVGTPTATNEAEVAADFLEFFSKFQDLYGIKNFRIFVSGESYAGRYVPYISSAMLDKNDTTHFNLSGKPAHPLHHLAPTNAVCTGALLYDACIGQWDWVQAELPAYPFVQQHASLFNFNETFMTSLATTYEECGYQAYFDEYFTFPASGIQPPKYMNYSECDIYNAIYNEAFSPNPCFNPYRVIDECPLLWDVLGFPTDLAYEPAPTTYFNRADVKRALHAPQNIEWELCSTDPVLVGGDGVSGPEQVGDDSPNPTEGSLPRVIEATNRVLIANGDWDYLIITNGTLLAIQNMTWHGQLGFAAAPATPIDIRMPDLQWAGVFDAQEGYGDLDGPQGVMGVQHYERGLMWAETFQAGHKQAQDQGRVSYRHLQWLLGEVDSL
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Serine-type carboxypeptidase; part of the gene cluster that mediates the biosynthesis of aculins (PubMed:26374386). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable). Secondary metabolite biosynthesis. Belongs to the peptidase S10 family.
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Q3J6K9
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MRAVLIEKSDDTQSVSVTELAEDQLPEGDVLVDVAYSTLNYKDALAITGKAPVVRRFPMVPGIDFTGTVAQSSHADFKPGDRVILNGWGVGEKHWGGLAERARVRGDWLVPLPAPLDLRQAAMIGTAGYTAMLCVLALERHGVVPGNGEIVVSGAAGGVGSVATTLLAAKGYEVAAVTGRASEAEYLRGLGAASVIDRNELTGKVRPLGQERWAGGIDVAGSTVLANMLSMMKYRGVVAACGLAAGMDLPASVAPFILRGMTLAGVDSVMCPKTDRLAAWARLASDLDPAKLEEMTTELPFSEVIETAPKFLDGTVRGRIVIPVTP
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Catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA. Is essential for growth with 3-hydroxypropanoate as a sole carbon source. Restores acrylate resistance when expressed in the E.coli strain K12 acuI deletion. NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH Homodimer. Moderately induced by acrylate and dimethylsulfonioproprionate (DMSP), as well as by 3-hydroxypropanoate. Part of the acuR-acuI-dddL operon. Increased sensitivity to acrylate on plates, decreased ability to degrade acrylate (PubMed:21249136). No effect during photoheterotropic (anaerobic/light) growth on succinate, no growth on 3-hydroxypropionate under the same conditions. Loss of 3-hydroxypropanoate and acrylate-dependent oxidation of NADPH (PubMed:22056933). The zinc-binding residues of the alcohol dehydrogenase family are not conserved. Belongs to the zinc-containing alcohol dehydrogenase family. Acrylyl-CoA reductase subfamily.
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Q2M8W1
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MQALLLEQQDGKTLASVQTLDESRLPEGDVTVDVHWSSLNYKDALAITGKGKIIRNFPMIPGIDFAGTVRTSEDPRFHAGQEVLLTGWGVGENHWGGLAEQARVKGDWLVAMPQGLDARKAMIIGTAGFTAMLCVMALEDAGVRPQDGEIVVTGASGGVGSTAVALLHKLGYQVVAVSGRESTHEYLKSLGASRVLPRDEFAESRPLEKQVWAGAIDTVGDKVLAKVLAQMNYGGCVAACGLAGGFTLPTTVMPFILRNVRLQGVDSVMTPPERRAQAWQRLVADLPESFYTQAAKEISLSEAPNFAEAIINNQIQGRTLVKVN
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Probably catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA. NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH Homodimer. 100-fold increased sensitivity to acrylate, about 8-fold increased sensitivity to 3-hydroxypropionate. Acrylate is bacteriostatic, not bacteriocidal. Can be complemented by acuI from a number of other bacteria, including Rhodobacter sphaeroides strain 2.4.1 (AC Q3J6K9) and Ruegeria pomeyroi (AC Q5LS56). The zinc-binding residues of the alcohol dehydrogenase family are not conserved. Belongs to the zinc-containing alcohol dehydrogenase family. Acrylyl-CoA reductase subfamily.
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Q5LS56
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MFNALVVDKDEESGKTQAAVKQLSLTDLPVGEVTVAVEYSTVNYKDGLCIGPGGGLVRKYPHVPGIDFAGTVENSSDERYKPGDKVVLTGWRVGEAHWGGYSQKANVRADWLVPLPEGLDTRQAMAVGTAGFTAMLAVMALEDHGLTPGHGPVLVTGAAGGVGSVATAILAHLGYEVAAVTGRPETADYLTSLGATQIVARDEINETVKRPLESEIWAGCVDAVGGAMLARVLGQMKYGASVAAVGLAGGAGLPATVIPFLLRGVNLLGIDSVMQPYANRLRAWERIARDLPMDKLEAMIRPATLSDLPGLGADILKGQVQGRVVVDVNA
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Probably catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA. Restores acrylate resistance when expressed in an E.coli strain K12 acuI deletion. NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH Homodimer. By dimethylsulfonioproprionate (DMSP) and acrylate. 25-fold increased sensitivity to acrylate, growth is strongly inhibited by 20 mM dimethylsulfonioproprionate (DMSP). The zinc-binding residues of the alcohol dehydrogenase family are not conserved. Belongs to the zinc-containing alcohol dehydrogenase family. Acrylyl-CoA reductase subfamily.
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C0NCM1
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MTASTQNGSPTPPPAAPTATNQESKNMTANPADASESQSPANEKGSGTAESGQKHTSTAANAKDPLRPRRKKAKRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPNEALMPGIRRNFYNQANATRTNANQQQNGPNSNSNKDSRQNVAANFYSPQSASNFDVYTQAKSQQGQGHIPPTVMQDTSINPSAFQAPSPTSTPNFDLSSNPPNRNLSSAMTQTPSSASNQTQDPFGAAFFDPSHPALFNFDIASMNFGNRYGALEFGMLGHMATGAGDTPPSDSATQRGSIGRSSGTFTAQNFGDSTNTQSPFLFGDPVLNDWNPSGQSQTNPRNNNIYNQNTVAGQMGEQHPNAFAIESAPMNFASPGSTESPQMTTMNQFDEANAKFSSRTALMHQTNPHQPPPISTPGLKHQGFQVGVKRRYRSPSSIYESVKEPYSYTSGFHNLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNQDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKEVLLGKEPNLNVNTGGSSPRGSGTFTPRNGNGVDPHSGMSAAGGGGGRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKEDSAALFQGKEAQQGGSDGKGGGGGGDVAATAATTSTSTSNGANSSGHANANRNNTNPKNSSPPSSSSAAAAGPLHGAQLSPKQTWGKRGIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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A6R213
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MTASTQNGSPTPPPAAPTATNQESKNMTANPADASESQSPANEKGGGTAENGQKHTSTAANAKDPLRPRRKKAKRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPNEALMPGIRRNFYNQANATRTNASQQQNGPNSNSNKDSRQNVAANFYSPQSASNFDVYTQAKSQQGQGHIPPTVMQDTSINPSAFQAPSPTSTPNFDLSSNPPNRNLSSAMTQTPSSASNQTQDPFGAAFFDPSHPALFNFDIASMNFGNRYGALEFGMLGHMATGAGDTPPSDSATQRGSIGRSSGTFTAQNFGDSTNTQPPFLFGDPVLNDWNPSGQSQTNPRNNNIYNQNTVAGQMGEQHPNAFAIESAPMNFASPGSTESPQMTTMNQFDEANAKFSSRTALMHQTNPHQPPPISTPGLKHQGFQVGVKRRYRSPSSIYESVKEPYSYTSGFHNLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNQDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKEVLLGKEPNLNVNTGGSSPRGSGTFTPRNGNGVDPHSGMSASGGGGGRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKEDSAALFQGREAQQGGPDGKGGGGGGGDVATTAATTSTSTSNGANSSGHANANRNNTNPNNSSPPSSSSAAAAGPLHGAQLSPKQTWGKRGIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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C5GF27
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MTASTRNGSPSPSPAAPTATEQESKSMTTTPANPPETKSQTNGKGSGTAQSSQKPASTSANAKDPLRPRRKKAKRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPNEALLPGIRGNYYNQANTTRNIPNQRGNASNSNSNKVSRQSVSSANFYTPQAARSYNVYVQAKSQQSHVRPAVMQDASMNPSVFHAQSPSSTQNFDLSSNPQTQNLSSAMSQTASSVSGQNQDPFGAAFFDPSHPALFNFDIASMNFGNRYGALEFGMLGHMATGAGDTPPSDSATQRGSIGRSSGTFTAQNFGDSANNQSPFLFGDPVLNDWNPTGQGQANPRNIYNQNAVAGQMGEQNPHAFAIESAPMNFASPSSTESPQMTTTTPFDEANANFSSRTNLMHPTNTPQQSRISTPGLKHQGLHVGVKRRYRSPSSIYESVKEPYSYTSGFHSLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNQDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKEVLLGKEPNLNVNTGSSLSSASSVRGSSTFTPRNNNTHNSIDPHTGMPTVGGGGASGRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKEDSAALFHGKEETQQGGVDGSSGTGTTTSGDVATTTATGTSTSNGANANTNGNNTNPNDPSSAASSSASSALQGPQQSPRQTWGKRGIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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D4AL61
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MSPHQTTGQESDNMTVNGENAQASSQYIQSNEEMTSAIATEKKASTAKAAKDPSRPKRKKAKRACYACQRGHLTCGDERPCQRCIKRGFQDACHDGVRKKAKYLHDAPNEALMAGVGATLYNQRNAAQNNANGSNTSPGAPQQITSPNFYNTQQSPDYNGFPQNKTELQDSTVGPDNYASQSPVSPTYQISQGLSTQGLSPSLPQSTSETPSAANPAPGQFNSAFFDPSDPALFNFDLASMNFGNHYGALEFGMLGHMATGVGDTPPSESGAQRGSIGQNGSGTFGLTGSNFSESPSNQAPYLFSESGMNDWTQTAPVNRRSMYGSNANLVAGNMSDKPHAFAIESAPANFASPASNESPMMTTSSATFEDTTNSGAFNSRQNVPVSQQRQQPVVSTPQLKQQNLNLGSRRRHKNASSIYDSVKDPYSYTSGFHSLTAFIQRRFSPQKTLRIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKEVLLGKEPNHNVNTGGSSGLMTGSTSRGSYTPRPYSSEVYNSSATATPRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKAESDILAGSNGEADAGLNGEAASNETNELNGSLTNGATTNGRGQRRWGKGEIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNVSCLCLEPLSEP
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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E4UP58
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MSPHQTTGQESDNMAVNGENAPASSQYIQTNNDEMADMVAAEKKAAAAKAAKDPSRPKRKKAKRACYACQRGHLTCGDERPCQRCIKRGFQDACHDGVRKKAKYLHDAPNEVLMAGVGATLYNQRNAAQNNVNGSNTSPGVPQQMTSPNFYSTQQSPDYNSFPQNKNELHDSTVGPENYASQSPVSPTYQIGQGMPNPVLSPSLPQSASETPSTANAAPGQFNSAFFDPSDPALFNFDLASMNFGNHYGALEFGMLGHMATGVGDTPPSDSGAQRGSIGQNGSGTFGLAGSNFAESPSNQTPYLFNESGMNDWTQTAPVNRRSIYGSNANMVAGNMSDKPHAFAIESAPANFASPASNESPMMTTNSATFEDTTNSGAFSSRPNASVSQQRQQPVVSTPQLKQQNLNLGGRRRHKNASSIYDSVKDPYSYTSGFHSLTAFIQRRFSPQKTLRIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWRKEVLLGKEPNHNVNTGGSSGLVTDSTSRGSYTPRPYSSDVYNSSTAATPRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKADSDILAGSNGEADAGQNGEASSSEANELNGSNANGATTNGRGLRRWGKGEIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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C5FP02
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MSPHQTTGQESDNMAVNGENAQASSQYIQLNSEETTDTVAAEKKAAAAKAKDPSRPKRKKAKRACYACQRGHLTCGDERPCQRCIKRGFQDACHDGVRKKAKYLHDAPNEALMAGVGASLYNQRNTTQNSINGANAPSSASQQITSPNFYNAQQSPDYNGYSQTKAELQDSTIGPENFASQSPVSPTYQMGQPMPNQGLSPSLPQSASETPSTANGAPSQFNSAFFDPSDPALFNFDLASMNFGNHYGALEFGMLGHMATGVGDTPPSDNGAQRGSIGQNSSGTFGLAGSNFAESPSNQGPYLFGDSGMNDWTQSAPVNRRNMYGSNANMVAGNMSDKPHAFAIESAPANFASPASNESPMMTTSSATFEDAANATAFNSRQNTSLPQQQQQQRQQPVVSTPQLKQQNLNIGSRRRHKNASSIYDSVKDPYSYTSGFHSLTAFIQRRFSPQKTLRIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWRKEVLLGKEPNHNVNTGGSSGLLTGSTSRGSYTPRPYSSDQFNSSTTATPRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKADSGVIASGNGEVGAAQNNEVGSGEANELNSSSNGTTSTGRGQRRWGKGEIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNGEMECMEVNIITSGQPNYQAFRALVKD
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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A1C602
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MNVEAKESSVAPAGDHGGAVQDPADVRDRLELLKNKANGETNGATPNGTKSTNAKDPSRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPDGALMPGVGGNFYNHPMRHNMPLSSNGANAVNATSQQNSGASFYPTPQSNPYNVYQESTLSQNSFPSQSPVSPTFNMKNTATARSNSLSSSVNQPQSNPAASGPPSQSQNPFAGPFFDPSDPALFNFDLSSMNFENRYGALEFGMLGHMATGAGDSPSESATQRGSIGRSGSAQFATTPITGNPGFGESPGNQQPFMFGNDPLLNEWPNNHPPGQGHMNVGGVYPQNSMMAGHLSKADAPHAFAIESGPASFSSPSATTSPHVNGGYDENALSNAVAHKPNGLPTNGQRPAITTPRLKHQSLQLGVKRRHRNPSTVYESVKEPYAYTNRFHNLTAFIQRRFSSQKTLQIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKDVLLGKEPNLNVNTGGTSIPQSGTSSRGSFTPRISTLEQANPARPQPVFLAELLDDDSVVDFYEDFARLAFGDSRGSVMTTCKLLKYKTKEDMELAQSDDNQRWNNHLRKGGIAGEAGMNQLGFKDGKVECAYCWTVKRDVFDIPMLIVMNYLIPSDGFKSSIPF
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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B0XVV1
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MKTEVNGSAPALAGDHGGVDQDTPDAGDRTEQAKHKTNGATENAPKSANAKDPSRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPDGALMPGVGGNFYNNAMRNNMPLSRNGTTTVNTTTQQNSGSNYYPTPQSNSYNVYQDTPLTQNSFPSQSPVSPTFNMKTTPTARSNSLSSSVNQQPPSTTVSGATQSQNPFAGPFFDPSDPALFNFDLSSMNFENRYGALEFGMLGHMATGAGDSPTDSATQRGSIGRSGSTQYSTTPLTGAPGFGESPGNQQPFLFGNDPLLNEWPNSQAPNQGHLNVSGVYPQGGMMHMAKSDAPHAFAIESGPASFSSPSATTSPHINSGHDESSLSNAAVNKSTGLTANGQRPAITTPSLKHQSLQFGVKRRQRNPSTVYESVKEPYAYTNRFHNLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKDVLLGKEPNLNVNTGGSSAPGSGNTSRGSFTPRSSTLETATPGRPQPVFLAELLDDDSVVEFYEDFARLAFGDSRGSVMTTCKLLKYKTKEDMELAQSDDNQRWNNHLRKGGIAGEAGMNQLGFKDGKVECAYCWTVKRDVFDIPMLIVMNVFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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Q4WHD1
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MKTEVNGSAPALAGDHGGVDQDTPDAGDRTEQAKHKTNGATENAPKSANAKDPSRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPDGALMPGVGGNFYNNAMRNNMPLSRNGTTTVNTTTQQNSGSNYYPTPQSNSYNVYQDTPLTQNSFPSQSPVSPTFNMKTTPTARSNSLSSSVNQQPPSTTVSGATQSQNPFAGPFFDPSDPALFNFDLSSMNFENRYGALEFGMLGHMATGAGDSPTDSATQRGSIGRSGSTQYSTTPLTGAPGFGESPGNQQPFLFGNDPLLNEWPNSQAPNQGHLNVSGVYPQGGMMHMAKSDAPHAFAIESGPASFSSPSATTSPHINSGHDESSLSNAAVNKSTGLTANGQRPAITTPSLKHQSLQFGVKRRQRNPSTVYESVKEPYAYTNRFHNLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKDVLLGKEPNLNVNTGGSSAPGSGNTSRGSFTPRSSTLETATPGRPQPVFLAELLDDDSVVEFYEDFARLAFGDSRGSVMTTCKLLKYKTKEDMELAQSDDNQRWNNHLRKGGIAGEAGMNQLGFKDGKVECAYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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A2QFG8
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MNAEPKEQDSPAPSAERTEASQEISAAGAQADKPKTEANGDGTANGASANGQKPNPKDPSRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPDGALMPGIGGTFYNNPMRNSLPLSRNGANAVNATGQQSAGANFYPTPQSTTYVYQENTINQGSFPSQSPVSPTFNLKATPTARTNSLSSVNPQPPSTSVSGPPGQGQNPFAGPFFDPSDPALFNFDLSSMNFENRYGALEFGMLGHMATGAGDSPSDSATQRGSMGRSGSAQYASTPITGAPGFGESPGNQQPFMFGDPLLNEWPSGQAPGQPHLPGVYPQSGQGSAIPGHLSKADAPHAFAIESGPASFNSPGATTSPQMTTGLEETPFHSAVASKSNGLAPHGQRPMITTPSLKHQNLQVGVRRRQRNPSAIYDSVKEPYAYTSRFHGLTAFIQRRFPPQKTLQIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKDVLLGKEPNLNVNTGGSSMPNSGASSRSFTPRSTVDNTPGRPQPVFLAELLDDDSVVQFYEDFARLAFGDSRGSVMTTCKLLKYKTKEDMEGAAAEDSQRWNNHLRKGGIASEAGMNQLGFKDGKVECAYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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Q2UMM2
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MTVDAQDSTPAPPADRRGAELETGGVGEQSEQPKNKSNGDGNAPAETGQKPNPKDPSRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPDGALMPGIGGNFYNNTMRSNLPLSRNGANAVNATTQPSSSPNFYPTPQSNSYSVYQENTMNQNSFTSQSPVSPTFTLKANPAARNNSLSSQVNQQPPSTGVSGATNPSQNPFAGPFFDPSDPALFNFDLSSMNFENRYGALEFGMLGHMATGAGDSPSDSATQRGSMGRSGSAQFSGTPITGAAAFGESPGGQQPFIFGDPLLNEWSSGQPTGQTHVNVGGVYPQSGQGSVIPGHLTKADAPHAFAIESGPGSFASPNATTSPQITTGFDDATFSSAVTAKSNGLSANGPRPTITTPSLKHQNLQVGVRRRQRNPSSIYENVKEPYAYTNRFHNLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLFEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKDVLLGKEPNLNVNTGGSVPGSGTSSRSFTPRGSVAESTPGRPQPVFLAELLDDDSVVEFYEDFARLAFGDSRGSVMTTCKLLKYKTKEDMENQSDDNQRWNSHLRKGGIASEAGMNQLGFKDGKIECAYCWTVKRDVFDIPMLIVMNASSTNLR
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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Q0CHR0
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MKVESRENQPSAASADRSGADQESGAAERPDPSKKTDDGKPHAPAENGQKPPSNAKDPSRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLQDACTDGVRKKAKYLHDAPDGALMPGVGGNFYSSNNNNSSMRNNLPLSRNGANAVNANAQQNTGANFYPTPQSTSYNVYQENPINQSSFTSQSPVSPTFNLKTNPTARTNSLSSVGQQPPTTTGVSGPNPQNPFAGALFDPSDPALFNFDLSSMNFENRYGALEFGMLGHMATGAGDSPSDSATQRGSMGRSGSAQFSNTPITGQPGFGESPGGQQPFMFGDPLLNEWPGGQASGQAHVNVGGVYPQSGQGSVIPGHLSKTDAPHAFTIESGPNFASPSATTSPQMTSGFDDHALNNAVAKSNGMANGQRPTISTPSLKHQSLQIGAKRRPRNPSSIYESVKEPYAYTNRFHNLTACIQRRFSPQKTLQIAKALASIRPSFIATTKTLNRDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKDVLLGKEPNLNVNTGGSSLPGSGTTSRSFTPRGSVGESTAPGRPQPVFLAELLDDDSVVEFYEDFARLAFGDSRGSVMTTCKLLKYKTKEDMELAQSDDNQRWNNHLRKGGIASEAGMNQLGFKDGKVECAYCWTVKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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A0A179URQ2
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MTASTRNGSPSPSPAAPTAAEQESKSMTTTPANPPETKSQTNGKGSGTAQSSQKPASTSANAKDPLRPRRKKAKRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPNEALLPGIRGNYYNQANTTRNIPNQRGNASNSNSNKVSRQSVSSANFYTPQAARSYNVYVQAKSQQSHVRPAVMQDASMNPSVFHAQSPSSTQNFDLSSNPQTQNLSSAMSQTASSVSGQNQDPFGAAFFDPSHPALFNFDIASMNFGNRYGALEFGMLGHMATGAGDTPPSDSATQRGSIGRSSGTFTAQNFGDSANNQSPFLFGDPVLNDWNPTGQGQANPRNIYNQNAVAGQMGEQNPHAFAIESAPMNFASPSSTESPQMTTTTPFDEANANFSSRTNLMHPTNTPQQSRISTPGLKHQGLHVGVKRRYRSPSSIYESVKEPYSYTSGFHSLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNQDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKEVLLGKEPNLNVNTGSSLSSASSVRGSSTFTPRNNNTHNSIDPHTGMPTVGGGGASGRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKEDSAALFHGKEETQQGGVDGSSGTGTTTSGDVATTTATGTSTSNGANANTNGNNTNPNDPSTAASSSASSGCRARSNHLGKRGGRGALPAKRG
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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A6SP81
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MSGETEIDDPEVSDGASENDYSDHEQELDVIGKEGDNQEMAEQKVRPDGEENGNTVGATATVTKPKFDPKDPLRPRRKKARRACFACQRAHLTCGDERPCQRCIKRGLADACQDGVRKKAKYLHDAPPEALRPVLGPTYNQQVSSNRATAASTPTEPSPGMGNFFSQPDTSPSYPLFGANQQGQMPPPLQNRLSFGSNQPSPISPTFHTAGNRPAGMQGISLPQVSNDSHSAFGGGAFFDPSNPALFNFDLEGLNFGNHYGALEFGMLGHMASGSAETPPQDSSAGMPQNVGDLGFSNNSAFTNNPPFNQIYSHDSLPDFAVGLDRPNGGNVFGNNNPHHGLPHAYAIATSGSQHSPSTDASPAASTMGFESSPTTTNYPAPASHRPAKRQDTKSGPSGKLGPSGILGKRNRDPSSIYDTVHEPYSYTTGFHSLTAFIQKRFSPNKTLRIAKSLASIRPSFISCTKTLNRQDLIFMEKCFQRTLFEYEDFMLNCCTPTVVCRRTGEIAAANKEFTLLTGWRKEVLLGNEANLNTNTGSGGPPSSGSSGRGSFTTPRMRPVNLADSNPNGKTQPIFLAELLDDDSVIEFYEDFARLAFGDSRGSVTTRYKLLRYQTAKDTSQSPEGDKGKRKDIVGFNGAGIGGMGNRIKEIDANNGIESLQQDGKVDCSSCWTIKRDVFDIPMLIVMNFLPCI
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Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). Belongs to the ERT1/acuK family.
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Q83AB0
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MTQKEKNETCIHVTVSGKVQGVFFRESVRKKAEELQLTGWVKNLSHGDVELVACGERDSIMILTEWLWEGPPQAAVSNVNWEEIVVEDYSDFRVR
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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A7ME43
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MAWVHGRVQGVGFRYTTQHEATRLGLTGYARNLDDGSVEVLACGEAEQVEKLIAWLKAGGPRSAHVEKVLTEPHSPTEDYQDFRIRY
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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Q1LIH0
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MTTTTETWQLFAHGRVQGVGYRAACADRATSLGLGGWVRNRVDGRVEVLASGPRERLEALRVWMEAGPPAAQVSKVEVAQAAPQLFDRFDWLPTA
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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Q0K6H7
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MKKETWRLVAHGRVQGVGYRAACADAADDLELGGWVRNRLDGTVEVMAHGTVRQLEALQAWMEQGPPAAQVTLVEVGPGEGEFAGFEFRPTI
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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Q46WU4
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METWHMTAHGRVQGVGYRAGCAQAAIALGVRGWVRNRADGTVEVMASGTIQQLEALRNWMQAGPPAAHVARVDVEPGQGKFEDFDLRPTL
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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Q47GU0
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MARIRRQLIIEGRVQGVGYRWSMAEQARKLGVVGWVRNLADGRVEAMAVGEEMAVLELIAWARRGPSHAIVRQVSVALGDGDFPSFEQRANG
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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Q3Z7Q6
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MHCLKAVVKGKVQGVYFRDFTRTQAIRLGLCGYAQNLESGTDVEVIAEGDKDILLEFLKLLRSGPPHAEVQEVEVSWSSTNGNYGDFHIKY
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
A5FQM9
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MHCLRAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLANGAEVEVVAEGDKDALLEFLNLLRSGPPRAEVKDVETGWETATANYSDFRIKH
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q3ZXY7
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MHCLRAIVKGKVQGVYFRDFTRTQATRLGLCGYAKNLANGAEVEVVAEGDKDALLEFLDLLRSGPPRAEVKDVETSWETATANYSDFRIKH
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q1J123
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MRLTALVSGTVQGVGYRRYVQRHARDLGLSGSAENLPDGRVEVVAEGPPEHLERLLHWLRRGPPHARVADVQTQYSEATGLRDFHVY
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q9RVU3
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MRLTALVSGHVQGVGYRLFVQRYARDLGLHGYAENLSDGKVEVIAEGDEDALNRLLHWLRRGPPHARVQAVDTQYSEETGLREFHIY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
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Q72CU1
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MPRRSYSVIGRVQGVGFRSWTRRTALRLDLRGWVRNEPDGTVRLCADGTDEALATLETALRKGPMFSRVDHVVKHDDPAHEGPLPDTFDIRFRAPGSASE
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
A1VEL6
|
MPRRSYSVIGRVQGVGFRSWTRRTALRLDLRGWVRNEPDGTVRLCADGTDEALATLETALRKGPMFSRVDHVVKHDDPAHEGPLPDTFDIRFRAPGSASE
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q9R7Q1
|
MSKVCIIAWVYGRVQGVGFRYTTQYEAKRLGLTGYAKNLDDGSVEVVACGEEGQVEKLMQWLKSGGPRSARVERVLSEPHHPSGELTDFRIR
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Optimum pH is 5.2-6.5. Thermostable. Retains 85-90 % of its activity after 3 hours of incubation at 90 degrees Celsius. Has a considerably reduced catalytic efficiency compared to other mesophilic acylphosphatases. Shows a considerable resistance against urea denaturation since the full enzymatic activity is maintained in the presence of urea concentrations approaching 6.0 M and that only a slight decreae of 10-15 % was observed with higher urea concentrations. Belongs to the acylphosphatase family.
|
A1A9N7
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MSKVCIIAWIYGRVQGVGFRYTTQYEAKKLGLTGYAKNLDDGSVEVVACGDEGQVEKLIQWLKSGGPRSARVERVLSEPHHPSGELTDFRIR
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q8FJ70
|
MSKVCIIAWVYGRVQGVGFRYTTQYEAKKLGLTGYAKNLDDGSVEVVACGDEGQVEKLMQWLKSGGPRSARVERVLSEPHHPSGELTDFRIR
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
A4W8Y0
|
MMSKVCTIAWVHGTVQGVGFRYSTQREALQLGLTGYARNLDDGSVEVVACGEADNIEQLIAWLKAGGPRSARVEKVFTEPHQPDREYDKFSIRY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q831U6
|
MEKLRMNVQGRVQGVGFRYMTKMVADQLGVTGSVRNEDDGSVSITAIAPEDIMETFIKKIKDSPSPAGRVTYVDIQEDPLLEETEQFKVIQ
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
A7HMJ7
|
MLEVWKKWNVRGVVQGVGFRHFVKNVARAIGVRGYVKNEDDGSVTIVAGGNDEQIKELFRRIMEGNGWSYISDYDEIDLPKQEYKDFHVEF
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q0IBG0
|
MKERWRFLIEGSVQGVGFRNSCRRRALDLGLCGWVRNLKDGVVEIQAEGDELALNELRLWCERGPSAATVKRVLLSKIPVTGNDWFDVRT
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q3AYW4
|
MARRTRNRSEIIARRFVSRQQPTRTQPFVERWRWIIQGQVQGVGFRASCSRRALDMGLKGWVRNLQDGSVEVQAEGPPIALAELRAWCEKGPLGAQVKRVKPCQMPVRGDDWFEVRY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q3AIC0
|
MIEGRVQRVGFRASCNRRALDLGISGWVRNLSDGRVEVQAEGPPLALSELRAWCEVGPPGARVVRVTPSQLPITGDDWFEVRY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q47S76
|
MEKVRLTAWVRGHVQGVGFRWWTRARALELGLTGAATNLDDGRVEVVAEGDRTACERLLELLRSGQTPGRVDSVVERWTNHRGSFTGFEER
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q5JDG7
|
MKRVRAHLRIYGRVQGVGFRWSMSREARKLGVHGWVRNLPDGTVEAVIEGDPERVEALIGWAHQGPPLARVTRVEVKWEEPEGLEGFKVVG
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q9X1Q0
|
MKALKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNMDDGSVFIHAEGDENALRRFLNEVAKGPPAAVVTNVSVEETTPEGYEDFTIKYY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
A5IM19
|
MKALKIRVEGIVQGVGFRYFTRRVAKSLGVKGYVMNMDDGSVFIHAEGDENALRRFLNEVAKGPPAAVVTNVSVEETTPEGYEDFTIKYY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
A1RZ22
|
MRAHIYVSGLVQGVFFRASMQEVARSLGVNGWVRNLPDGRVEAVLEGEEGAVLKVIEWARRGPPLARVERVDVEWEEYRGEFRDFYIKYR
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q72L64
|
MPRLVALVKGRVQGVGYRAFAQKKALELGLSGYAENLPDGRVEVVAEGPKEALELFLHHLKQGPRLARVEAVEVQWGEEAGLKGFHVY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q5SKS6
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MPRLVALVKGRVQGVGYRAFAQKKALELGLSGYAENLPDGRVEVVAEGPKEALELFLHHLKQGPRLARVEAVEVQWGEEAGLKGFHVY
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q97CT1
|
MLTTRRVRFYGRVQGINFRSNTLVKALELGVKGWIKNLPDGSVEALFSGESEQIEKLISYCVSNMPYAEVKRYDVYIEPYTEFQDFQIKR
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q3SKG9
|
MKTLHLQIEGRVQGVWFRESMRREAERLGVDGWVRNRPDGSVEAVVQGTDEAVAALVAWAKMGPPLAHVERVDLSETEGEYSGFEKRSD
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q73PK2
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MDKETLRALHVIVKGRVQGVGFRYWTRSLAKSLNVKGRVRNLADYSVEIIAEADTDTLGEFVYALKHEHPYARVESLNSEEVRARGYTDFRIEV
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q3M4K7
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MPNSTPQSQLIRVHVFVTGRVQGVGFRYSTVDTASQLGLTGWVRNLPDGRVEAVFEGARDIVEEMVRWCHAGPPAAVVQDVAVEYEEPEGLRGFEVKRLVN
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
C3M0B6
|
MEKQCSKFIVSGHVQGVGFCYHTSHQGLKLGLTGYAKNLNNGDVEVVACGTPERLEELYLWLQEGPKTASVRQVRRLSSELEHDYQGFEIL
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family. Lacks the conserved active site Arg in position 20. There is a cysteine in this position.
|
Q9KSA4
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MEKQCSKFIVSGHVQGVGFRYHTSHQGLKLGLTGYAKNLNNGDVEVVACGTPERLEELYLWLQEGPKTASVRQVRRLSSELEHDYQGFEIL
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q87P91
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MNVKCERFIVKGHVQGVGFRYHTSHQGLKLGLTGYAKNLNNGDVEVMACGPKEKIDQFCEWLQEGPRTATVESVTRESVSYKPFRGFKIL
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q8D994
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MAIRCEKFVVSGIVQGVGFRYHTSHQGLKLNLVGYAKNLYNGDVEVIACGEPLKIEEFAKWLEQGPKTARVDELKREEITCREYQGFEIL
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q7ML77
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MAIRCEKFVVSGIVQGVGFRYHTSHQGLKLNLVGYAKNLYNGDVEVIACGEPPKIEEFAKWLEQGPKTARVDELKREEITCREYQGFEIL
|
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
Q8PNV0
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MQAARFVVSGVVQGVYYRACTRQRAVALGLVGHARNQADGSVDVVAAGSAAALDALEAWLCRARRPPRSRRSRARPARFRRLKTL
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an acyl phosphate + H2O = a carboxylate + H(+) + phosphate Belongs to the acylphosphatase family.
|
P19219
|
MPDSINNGHKESHDHRISNDAEMITDEKWQAIINNDAAYNNQFFYAVKSTGIFCKPSCKSRVPKKENVCIFPNTEQALRANFRPCKRCKPTNEKMPDSEWVDLITEYIDKNFTEKLTLESLADICHGSPYHMHRTFKKIKGITLVEYIQQVRVHAAKKYLIQTNKAIGDIAICVGIANAPYFITLFKKKTGQTPARFRQMSKMEETYNGNK
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Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the methylphosphotriester lesions in DNA by a direct and irreversible transfer of the methyl group to one of its own cysteine residues. The methylation of AdaA by methylphosphotriesters in DNA leads to its activation as a transcriptional regulator that activates the transcription of the ada operon which consists of adaA and adaB, and of the adjacent gene alkA. (2'-deoxyribonucleoside 5'-methylphosphotriester)-DNA + L-cysteinyl-[protein] = 2'-deoxyribonucleotide-DNA + H(+) + S-methyl-L-cysteinyl-[protein] Binds 1 zinc ion per subunit. Up-regulated by methylated AdaA itself in response to the exposure to alkylating agents such as MNNG.
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A2QX23
|
MAFRIPFAQSFWQEYLSGQEANLPRLPEVEQVTETVMRILGGNPGRMQLQGTNTYLVGTGKFRILIDTGQGEASWIEALTKQLEANGLEISHVLLTHWHGDHTGGVPDLITYNPELSSRVYKNTPDLGQQAIHDGQKFHVEGATIRAVFTPGHAFDHMCFLLEEENALFTGDNVLGHGYSVVEDLGTYMTSLTRMADLNCALGYPAHGTRIEDLPAKMKEYIQHKESRMRQVLAALERSRARMTATGGGRRAGALTFPELINSMYGGIPDEIEQALTPFLSQVLWKLAEDRKVGFEGEPSQRRWFAVGPPAATAVRL
|
Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960). Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960). 3-(2,4-dioxopentyl)-2,3,6,8,9-pentahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] = 2-acetyl-3,4a,8,10,11,12a-hexahydroxy-1,4,4a,5,12,12a-hexahydrotetracene-1,12-dione + H(+) + holo-[ACP] Binds 2 Zn(2+) ions per subunit. Secondary metabolite biosynthesis. Belongs to the metallo-beta-lactamase superfamily.
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G3KLH5
|
MAFRIPFAQSFWQEYLSGQEANLPRLPEVEQVTETVMRILGGNPGRMQLQGTNTYLVGTGKFRILIDTGQGEASWIEALTKQLEANGLEISHVLLTHWHGDHTGGVPDLITYNPELSSRVYKNTPDLGQQAIHDGQKFHVEGATIRAVFTPGHAFDHMCFLLEEENALFTGDNVLGHGYSVVEDLGTYMTSLTRMADLNCALGYPAHGTRIEDLPAKMKEYIQHKESRMRQVLAALERSRARMTATGGGRRAGALTFPELINSMYGGIPDEIEQALTPFLSQVLWKLAEDRKVGFEGEPSQRRWFAVGPPAATAVRL
|
Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960). Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960). 3-(2,4-dioxopentyl)-2,3,6,8,9-pentahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] = 2-acetyl-3,4a,8,10,11,12a-hexahydroxy-1,4,4a,5,12,12a-hexahydrotetracene-1,12-dione + H(+) + holo-[ACP] Binds 2 Zn(2+) ions per subunit. Secondary metabolite biosynthesis. Belongs to the metallo-beta-lactamase superfamily.
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P19220
|
METNKPTLYWSLLMFKDWNFYIASTLKGLVFVGSQNKPIEELFEWARKRFPGSLLVEDDDKLEPYAVEITQYLEGKRKNFTVPVEYAGTQFQLAVWNALCEIPYGQTKSYSDIANDINKPAAVRAVGAAIGANPVLITVPCHRVIGKNGSLTGYRGGFEMKTLLLDLEKRASSEMDVPH
|
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein] a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein] Up-regulated by methylated AdaA in response to the exposure to alkylating agents such as MNNG. This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles. Belongs to the MGMT family.
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A2QX24
|
MTPPILIIGAGLSGLTVSRILTNASIPNIVFEASTPDRSQGYAISLRDWGYTSLLTALGDLPLRSLTRGVAPDRILGGTGWIDQALRDNHTGNLLVAPDPEAKQCIVRANRNALRTWIADSGDEEVDIRYGHRLRSVQGSMGNVTATFENGAKYQGSLVIAADGVHSSVRSQILPHVSPDIVPVVVYHGELELPRKEFDNLIRPHSGPSNILAGVGDGFNTPITVCNITPTHVHLDWSYSRPSTENKENKDPLYRPHVSAAEAKQIPPALLEEIASRDLARPWSQLLNAEALPTHRVFNWVSRCVSVTREDVNAAQKQGVVFIGDSWHAMPIFGGEGGNHALVDAVELAEALTGKEGNLDAAVTGYYDRAWRRCQEAVRRSRQRFFQLHRPMREWMEIAEKKKMMAAMKGVEAH
|
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960). Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960). 3-(2,4-dioxopentyl)-3,6,8,9-tetrahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] + H(+) + NADPH + O2 = 3-(2,4-dioxopentyl)-2,3,6,8,9-pentahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] + H2O + NADP(+) Secondary metabolite biosynthesis. Belongs to the paxM FAD-dependent monooxygenase family.
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G3KLH4
|
MTPPILIIGAGLSGLTISRILTNASIPNIVFEASTPDRSQGYAISLREWGYTSLLTALGDLPLRSLTRGVAPDRILGGTGWIDQALRDNHTGNLLVAPDPEAKQCIVRANRNALRTWIADSGDEEVDIRYGHRLRSVQGSMGNVTATFDNGAKYQGSLVIAADGVHSSVRSQILPHVSPDIVPVVVYHGELELPRKEFDNLIRPHSGPSNILAGVGDGFNTPITVCNITPTHVHLDWSYSRPSTENKENKDPLYRPHVSAAEAKQIPPALLEEIASRDLARPWSQLLNAEALPTHRVFNWVSRCVSVTREDVNAAQKQGVVFIGDSWHAMPIFGGEGGNHALVDAVELAEALTGKEGNLDAAVTGYYDRAWRRCQEAVRRSRQRFFQLHRPMREWMEIAEKKKMMAAMKGVEAH
|
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960). Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960). 3-(2,4-dioxopentyl)-3,6,8,9-tetrahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] + H(+) + NADPH + O2 = 3-(2,4-dioxopentyl)-2,3,6,8,9-pentahydroxy-1-oxo-1,2,3,4-tetrahydroanthracene-2-carboxyl-[ACP] + H2O + NADP(+) Secondary metabolite biosynthesis. Belongs to the paxM FAD-dependent monooxygenase family.
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P0DTR4
|
MRNRRKAVSLLTGLLVTAQLFPTAALAADSSESALNKAPGYQDFPAYYSDSAHADDQVTHPDVVVLEEPWNGYRYWAVYTPNVMRISIYENPSIVASSDGVHWVEPEGLSNPIEPQPPSTRYHNCDADMVYNAEYDAMMAYWNWADDQGGGVGAEVRLRISYDGVHWGVPVTYDEMTRVWSKPTSDAERQVADGEDDFITAIASPDRYDMLSPTIVYDDFRDVFILWANNTGDVGYQNGQANFVEMRYSDDGITWGEPVRVNGFLGLDENGQQLAPWHQDVQYVPDLKEFVCISQCFAGRNPDGSVLHLTTSKDGVNWEQVGTKPLLSPGPDGSWDDFQIYRSSFYYEPGSSAGDGTMRVWYSALQKDTNNKMVADSSGNLTIQAKSEDDRIWRIGYAENSFVEMMRVLLDDPGYTTPALVSGNSLMLSAETTSLPTGDVMKLETSFAPVDTSDQVVKYTSSDPDVATVDEFGTITGVSVGSARIMAETREGLSDDLEIAVVENPYTLIPQSNMTATATSVYGGTTEGPASNVLDGNVRTIWHTNYAPKDELPQSITVSFDQPYTVGRFVYTPRQNGTNGIISEYELYAIHQDGSKDLVASGSDWALDAKDKTVSFAPVEAVGLELKAIAGAGGFGTAAELNVYAYGPIEPAPVYVPVDDRDASLVFTGAWNSDSNGSFYEGTARYTNEIGASVEFTFVGTAIRWYGQNDVNFGAAEVYVDGVLAGEVNVYGPAAAQQLLFEADGLAYGKHTIRIVCVSPVVDFDYFSYVGE
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One of an enzyme pair that work together to convert the A antigen to the H antigen of the O blood type, which together release galactosamine. Catalyzes the first step in the conversion, generating the substrate for the subsequent enzyme (FpGalNase, AC P0DTR5). Works on many different A antigen subtypes. Glu-90 probably activates a nucleophilic water molecule to start the deacetylation reaction. an N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H2O = acetate + an alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative Inhibited by EDTA. Optimum pH is 8.0. The deacetylase domain is in the N-terminus, while the C-terminus has a CBM32-type carbohydrate-binding domain that is not required for activity on soluble substrates. The CBM32 domain binds preferentially to repeating N-acetyl lactosamine structures. 5 ug/ml of this enzyme pair converts A blood type to O blood type in an hour, and can be removed by centrifugation, showing the pair can be used for production of universal type donor blood. DNA was isolated from a male human fecal sample of AB+ blood type, the sequence was given to UniProtKB by the submitters. Dropping barriers - Issue 220 of December 2019
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Q8NA06
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MASNNHWFQSSQVPSFAQMLKKNLPVQPATKTITTPTGWSSESYGLSKMASKVTQVTGNFPEPLLSKNLSSISNPVLPPKKIPKEFIMKYKRGEINPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELLQLDEPEPRILETSGPPPFPAEPVVLSELAYVSKVHYEGRHIQYAKISQIVKERFNQLISNRSEYLKYSSSLAAFIIERAGQHEVVAIGTGEYNYSQDIKPDGRVLHDTHAVVTARRSLLRYFYRQLLLFYSKNPAMMEKSIFCTEPTSNLLTLKQNINICLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELCLHVAVEGKIYLTVYCPKDGVNRISSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILIGDGNCSDTRGLEIAIKQRVDDALTSKLPMFYLVNRPHISLVPSAYPLQMNLEYKFLSLNWAQGDVSLEIVDGLSGKITESSPFKSGMSMASRLCKAAMLSRFNLLAKEAKKELLEAGTYHAAKCMSASYQEAKCKLKSYLQQHGYGSWIVKSPCIEQFNM
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Required for male fertility and normal male germ cell differentiation (By similarity). Plays a role in spermatogenesis (By similarity). Binds to RNA but not to DNA (By similarity). Belongs to the ADAD family.
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Q9JLB6
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MATAGGSRRAPVPGPRLGLPLAAHLPASLGGEGAKDSVGGEKTSGNNDWFQSSRVPSFAQMLKKNLPVQPSAQTVTLPTGYSSESCSLSNMASKVTQVTGNFPEPLLSKGLSSISNPVLPPKKLPKEFIMKYKRGEINPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELLQLDEPEPRVLEPAGPPPIPAEPVVTPEAAYVSKVQYEGRQVQYAKISQLVKETFGQLISNHSQYLKCSSSLAAFIIERAGHHEVVAIGTGEYNYSQCIKPNGRVLHDTHAVVTARRSLLRYFYRQLLLFYSKNPAMMEKSIFCTEPASNLLTLKQNINLYLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELSLHVAVEGKIYLTVYCSADGVNRVNSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILVGDGNCNDTRGLEIAINQRVDDALTSKLPMFYLVNRPHISLVPTAYPLQINLDHKSLSLNWAQGDNSLEIVDGLNGKITESSPFKSGLSMASRLCKAAMLSRFNLLAKEAKTDDLLEARTYHAAKCMSGPYQEAKALLKAYLQQHGYGSWIVKSPCIEQFSM
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Required for male fertility and normal male germ cell differentiation (PubMed:32665638). Plays a role in spermatogenesis (PubMed:15649457). Binds to RNA but not to DNA (PubMed:15649457). Testis-specific. Detected in round spermatid cells from stage II-XI (at protein level). Expressed in germ cells from mid-pachytene spermatocytes to mid-round spermatids. Mice exhibit spermatozoa retention in stage IX tubules and a reduction in the number of sperm in the epididymis, leading to a reduction in fertility (PubMed:15649457). Show defects in germ-cell development (PubMed:32665638). Belongs to the ADAD family.
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Q3KR54
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MATAGGSRRAPVPGPRLGLPLAAHLPASLGGEGAKDSLGGEKTSGNNDWFQSSRVPSFAQMLKKNLPVQSSAQTVTLPTGYSSESCSLSNMASKVTQVTGNFPEPLLSKGLSSISNPVLPPKKIPKEFIMKYRRGEINPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELLQLDEPEPRALEPAGPPPIPAEPIVTPEAAYISKVQYEGRQVQYAKISQLVKETFSQLISSHSQYLKCSSSLAAFIIERGGHHEVVAIGTGEYNYSQCIKPNGRVLHDTHAVVTARRSLLRYFYRQLLLFYSKNPAMMEKSIFCTEPASNLLTLKQNINLYLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELSLHVAVEGKIYLTVYCSADGVNRVNSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILVGDGNCNDTRGLEIAINQRVDDALTSKLPMFYLVNRPHISLVPTAYPLQINLDHKSLSLNWAQGDNSLEIVDGLSGKITESSPFKSGLSMASRLCKAAMLSRFNLLAKEAKTDDLLEARTYHAAKCLSGPYQEAKALLKAYLQQHGYGSWIVKSPCIEQFSM
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Required for male fertility and normal male germ cell differentiation (By similarity). Plays a role in spermatogenesis (By similarity). Binds to RNA but not to DNA (By similarity). Belongs to the ADAD family.
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Q32NG0
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MASNRNWSQHSSVPSFAQMLKKNLPDPGTSPAVNQTSTLSTCCLYNQPDCGTARVTRITGNFPEPFLSKMIVPPSLSSLTPRKVTKEFMVKYRRGDLNPISALYQFAQMQRMEIELKETVTTGNVFGAYFAFCAVVDGLEYKTGMGQNKKEAKANAAKLALDELLLHEDPALIDSENQSLNVIENPPPLPMNPRGTTETSTISRTRTDKRTFIHEKISSIIKETFTNLVSKYPEYENCGSSLAAFVIEKGGQHWEVVAIGTGEFNYGQSLQSDGRVLHDSHAMVVARRSLLRYFYRQLLLLYSGNNGMMDKSIFCTEPATNLLALKPNLNIFLYMNQLPKGAAQTNPQLCLSPHSLSAHEANDKLSLHVSVEGKNIPASYYSGEIVHNLYSMSSTDKLTRWEVLGVQGALLSIFIQPVYINSIIIGNAACSDTRGLEIAVKQRIDDALTSRLPMFYLVNRPYMSIVSSTHLTNNDTANKTLSLNWSQGDACVEVVDAAIGRTVEGSPFKSGSCLASRLCKAAMLCRFNLVVKESKRNAIPSGLSYHEAKRLAGPYQEAKCLLNSYFKQQGFGSWIAKPPIIGEFTM
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May be required for male fertility and normal male germ cell differentiation (By similarity). May play a role in spermatogenesis. Binds to RNA but not to DNA (By similarity). Belongs to the ADAD family.
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Q8NA94
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MASASQGADDDGSRRKPRLAASLQISPQPRPWRPLPAQAQSAWGPAPAPATYRAEGGWPQVSVLRDSGPGAGAGVGELGAARAWENLGEQMGKAPRVPVPPAGLSLPLKDPPASQAVSLLTEYAASLGIFLLFREDQPPGPCFPFSVSAELDGVVCPAGTANSKTEAKQQAALSALCYIRSQLENPESPQTSSRPPLAPLSVENILTHEQRCAALVSAGFDLLLDERSPYWACKGTVAGVILEREIPRARGHVKEIYKLVALGTGSSCCAGWLEFSGQQLHDCHGLVIARRALLRFLFRQLLLATQGGPKGKEQSVLAPQPGPGPPFTLKPRVFLHLYISNTPKGAARDIYLPPTSEGGLPHSPPMRLQAHVLGQLKPVCYVAPSLCDTHVGCLSASDKLARWAVLGLGGALLAHLVSPLYSTSLILADSCHDPPTLSRAIHTRPCLDSVLGPCLPPPYVRTALHLFAGPPVAPSEPTPDTCRGLSLNWSLGDPGIEVVDVATGRVKANAALGPPSRLCKASFLRAFHQAARAVGKPYLLALKTYEAAKAGPYQEARRQLSLLLDQQGLGAWPSKPLVGKFRN
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Required for male fertility and normal male germ cell differentiation. Diffusely cytoplasmic early in pachytene spermatocytes and coalesces into several perinuclear granules by late pachynema. Belongs to the ADAD family.
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Q95JT2
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MASASQGADDGSRRKPRLAASLQISPEPRPWRPLPPQAQGAWEPAPAMDHAEGGQPQVSVLRDSGPGAGAGVGELGAAQAWENLGEQMGRTPRVPVPPAGLSLPLKDPPASQAVSLLTEYAASLGIILLFREDQQPGPCFPFSVSAELDGVVCPAGTANSKTEAKQQAALSALCYIRSQLESPESPQTSSRPPPPPLSVDSILTHGQRCAALVSAGFDLLLDERSPYWACKGTVAGVILEREIPGARGHVKEIYKLVALGTGSSCCAGWLEFSGQQLHDCHGLVIARRALLRFLFRQLLLATQGGAKGKEQSVLAPQPGPGPPFTLKPRVFLHLYISNTPKGAARDIYLPPTSEGGLPHSPPMRLQAHVLGQLKPVCYVAPSLCDTHVGCLSASDKLARWAVLGLGGALLAHLVSPLYSTSLILADSCHDPPTLSRAIHTRPCLDSVLGPCLPPPYVRTALHLFSGPPVAPSEPTPDTCHGLSLNWSLGDPGIEVVDVATGRVKANAALGPPSRLCKASFLRAFHQVARAVGKPYLLALKTYEAAKAGPYQEARRQLSLLLDQQGLGAWPSKPLVGKFRN
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Required for male fertility and normal male germ cell differentiation. Diffusely cytoplasmic early in pachytene spermatocytes and coalesces into several perinuclear granules by late pachynema. Belongs to the ADAD family.
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B2RQL4
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MASVDEGGRRRPRLAASLQISPGPWKPSGGQEPTEAGDAAPRTAEHGVAGAQEAHREACKALGGSVLSPGPAGDFPGALHGLSMLPKDPPPAQAVALLTQCMANLGVSLTFLEDQTAGPGSSFSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYIQKQLERPEPLVTPRQPLLTSLSIETILTHEQRCAAVVSAGLDRLLSESSPYQACKGTVAAVILEREVQGSIGHSKETYELVALGTGSSSCAGWLEFSGRRLHDCHGLVIARRALLRFFFRQLLLVTQGGPKGQERSVLTPQPGPGPPFALKPGVFLHLYVSNTPKGAAHDIYLPLASEDSVLHSPAFRLQAHVCGQLKPVSYVAPALRDTHVGCLSASDKLARWAILGLGGGLLAHFLPPLYATSLVLADPCHDPSTLNRVIHSRPRLDSVLGSCLPCPYVRTTLHLFAGPLVAPSDPGPSTCHSLSLNWSLGDPDIEVVDVATGRVKTDSSVGPPSRLCKAAFLSAFRQVARALEKPQLLSLQTYEAAKAVPYREARQQLSLLLDQQGLGAWPSKPLVGKFRH
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Required for male fertility and normal male germ cell differentiation. Diffusely cytoplasmic early in pachytene spermatocytes and coalesces into several perinuclear granules by late pachynema. Testis-specific (at protein level). Male mice are sterile and show defects in germ-cell development. Belongs to the ADAD family. Truncated N-terminus.
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A2QX25
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MSSVTLTTTTTTTSTPPKPTPKDEPQEQIYTPWRLFIYDIWVLGIVSTLAWGCRISTYLIPLFRSNVGKKHLDIGAGTGYYLNQARIPSTTQLTIVDNETHALNVALARCKHPSTQTHGIVTDILQPSPFPETYLTNNDKKFDSVSMYYLLHCLPVPVASKCKIFTHLKKYMTEDGVVHGANVLGKGVRKDNWFARIIRRGCLNHGVFHNEEDNAYEFERALRENFWEVETWVVGSVFVFRAKRPILDA
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O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960). Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960). 2-acetyl-3,4a,8,10,11,12a-hexahydroxy-1,4,4a,5,12,12a-hexahydrotetracene-1,12-dione + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + TAN-1612 Secondary metabolite biosynthesis. Belongs to the methyltransferase superfamily.
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G3KLH3
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MSSVTLTTTTTTTSTPPKPTPKDEPQEQIYTPWRLFIYDIWVLGIVSTLAWGCRISTYLIPLFRSNVGKKHLDIGAGTGYYLNQARISSTTQLTIVDNETHALNVALARCKHPVTQTHGIVTDILQPSPFPETYLTNNDQKFDSVSMYYLLHCLPVPVASKCKIFTHLKKYMTEDGVVHGANVLGKGVRKDNWFARIIRRGCLNHGVFHNEEDNAYEFERALRENFWEVETWVVGSVFVFRAKRPILDA
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O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB (PubMed:21866960). Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612 (PubMed:21866960). 2-acetyl-3,4a,8,10,11,12a-hexahydroxy-1,4,4a,5,12,12a-hexahydrotetracene-1,12-dione + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + TAN-1612 Secondary metabolite biosynthesis. Belongs to the methyltransferase superfamily.
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Q6GN35
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MAGEGALQFYRDLPKVELHAHLNGSISTATMKKLMARKPHLDIQHGMTMIDKGQKRTLEECFQMFKIIHQITDTAEDILLVTKDVIKEFAADGVKYLELRSTPRDTPAGLTKQAYVETVLEGIKQCKEEGVDIDVRFLLAIDRRGGPTAAKETVKLAEDFFCSSNELVLGLDLSGDPTVGHGRDFMEPLNKARQSGLKLALHLSEIPSQTEETELLLGLPPDRIGHGTFLTTSAHIVEIVKKQHIPLELCITSNIKGQTVSSYNEHHFGFWYNLHHPFVLCTDDKGVFATDLSVEYEIAAKTFNLTPHHVWDLSYQAIDYTFASADVKANLKEKWLLLKPDVFRHAL
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Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A). H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine Binds 1 zinc ion per subunit. Monomer. Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Extended N-terminus.
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Q9M0Z1
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MEWIQSLPKIELHAHLNGSIRDSTLLELARVLGEKGVIVFADVEHVIQKNDRSLVEVFKLFDLIHKLTTDHKTVTRITREVVEDFALENVVYLELRTTPKRSDSIGMSKRSYMEAVIQGLRSVSEVDIDFVTASDSQKLHNAGDGIGRKKIYVRLLLSIDRRETTESAMETVKLALEMRDVGVVGIDLSGNPLVGEWSTFLPALQYAKDNDLHITLHCGEVPNPKEIQAMLDFKPHRIGHACFFKDEDWTKLKSFRIPVEICLTSNIVTKSISSIDIHHFADLYNAKHPLILCTDDFGVFSTSLSNEYALAVRSLGLSKSETFALARAAIDATFAEDEVKQQLRFIFDSASPEHV
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Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine (PubMed:29884623, PubMed:30721978, PubMed:31318636). Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A) (PubMed:29884623). Does not possess deaminase activity toward adenosine, AMP, N6-methyladenosine, or N6-mATP in vitro (PubMed:29884623). H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine Binds 1 zinc ion per subunit. kcat is 0.21 sec(-1) with N(6)-methyl-AMP as substrate. Monomer. Slight reduction of root growth (PubMed:29884623). 10-fold increase of the ratio N(6)-methyl-AMP/AMP in leaf cells (PubMed:29884623). Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
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Q0VC13
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MMEAEEQPWKTTFYSKLPKVELHAHLNGSISSNTIRKLIAKKPDLKIHDQMTMIDKGEKRTLEECLQMFQIIHLLTTTPEDVLMVTKDVIKEFADDGVKYLELRSTPRGEDATGMTKKTYVESILEGIKQSKEENVDIDVRYLISIDRRGGSSAAKEAVKLAEEFFLSAEDTVLGLDLSGDPSAGQAKDFLEPLLEAKKSGLKLALHLSEIPNQKTETQVLLNLFPDRIGHGTFLSSSEEGSPDLVDFVRQHQIPLELCLTSNVKSQTVPAYDQHHFGFWYSVAHPAVICTDDKGVFATRLSQEYQLVAETFHLTQSQVWDLSYESISYIFASDSTKADLRKKWSHLKPHF
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Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A). H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine Binds 1 zinc ion per subunit. Monomer. Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
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Q8IG39
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MPNNSKHKKKQQRRQQEAQKKSRAKQIETDKKNDEFLDTELDEVSPLVIDDDMTEFKNMPKVELHAHLSGSLSPETIKLIMESDETRAEEIMKKYKLEKPENMTGVFDCFPVIHAILRKPEAIRIAIRQTIKEFEEDNCVYLELRTSPKETDFMTYEDYLQVCIESFEAAKHEFPRIKTFLIVSLDRRMPFETAAHILGLIGEAQQRTNVIVGVELSGDPHLDGRRLLKLFVAARRFHGLGITIHLAEVLQNMADVEDYLNLRPDRIGHGTFLHTDPYTEYLTNKYKIPLEICLSSNVYSKTTTNYRNSHFNYWRKRGVPVFICTDDKGVIPGATLTEEYYKAAITFDLSTEELIGINQDALLNSFAYKYNVTDLTETFRKINNNVLD
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Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A). H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine Binds 1 zinc ion per subunit. Monomer. Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
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Q8NFM3
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MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
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Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:15385642, PubMed:26206488, PubMed:24700542). Mediates signaling downstream of ADRB1 (PubMed:24700542). Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (PubMed:24740569). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin (PubMed:24700542). Activated by GNAS. Activity is further increased by interaction with the G-protein beta and gamma subunit complex formed by GNB1 and GNG2 (PubMed:26206488). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (By similarity). Phosphorylation by RAF1 results in its activation (PubMed:15385642). Interacts with GNAS, GNB1 and GNG2 (PubMed:26206488). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with RAF1 (PubMed:15385642). Detected in pancreas islets (at protein level). Expressed in the brain, with high expression in the corpus striatum (PubMed:26085604). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylated by RAF1. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q5BL06
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MSGSKSVSPPGYAAQTAASPAPRGGPEHRAAWGEADSRANGYPHAPGGSTRGSTKRSGGAVTPQQQQRLASRWRGGDDDEDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDGGRGSRRQRRGAAGGGSTRAPPAGGSGSSAAAAAAAGGTEVRPRSVELGLEERRGKGRAAEELEPGTGIVEDGDGSEDGGSSVASGSGTGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQIAYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAISLHTNSQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGDRNAYLKEHSIETFLILSCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSLFMLSFYLSCFLLLALVVFVSVIYACVKLFPTPLQTLSRKIVRSKKNSTLVGVFTITLVFLSAFVNMFMCNSKNLVGCLAEEHNITVNQVNACHVMESAFNYSLGDEQGFCGSPQPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIEFIYVLIVEVPGVTLFDNADLLVTANAIDFSNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKAGKTHIKAIADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
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Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin. Activated by GNAS. Activity is further increased by interaction with the G protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (By similarity). Phosphorylation by RAF1 results in its activation (By similarity). Interacts with GNAS, GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (PubMed:21670265). Interacts with RAF1 (By similarity). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylated by RAF1. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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P40144
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MSGSKGVSPPGYAAQTAAAPASRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQQQQRLASRWRGDDDDEPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAAGGGSTRAPPAGGGCGGGSAAAAAAAGGTEVRPRSVELGLEERRGKGRAVDELEAGAVEGGEGAEDGGSSADSSNGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSTLHLAIALRTNAQDRFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESTNPEDEVDEFLGRAIDARSIDRLRSEHVRRFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICCVQITIVPHSMFMLSFYLACFLLLTLVVFVSMIYSCVKLFPRPLQSLSRKIVRSKMNSTLVGVFTITLVFLSAFVNMFMCNSKDLLDCLAAEHNISVIHVNACHVVESAFNYSLGNEQGFCGNSRPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELTYVLIVEVPRVTLFDNADLLVTANAIDISSNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
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Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin. Activated by GNAS. Activity is further increased by interaction with the G protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (By similarity). Phosphorylation by RAF1 results in its activation (By similarity). Interacts with GNAS, GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with RAF1 (By similarity). Myocardial tissue. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. The N-terminus is blocked. Phosphorylated by RAF1. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q04400
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MSGSKSVSPPGYAAQTAASPAPRGGPEHRAAWGEADSRANGYPHAPGGSTRGSTKRSGGAVTPQQQQRLASRWRGGDDDEDPPLSGDDPLVGGFGFSFRSKSAWQERGGDDGGRGSRRQRRGAAGGGSTRAPPAGGSGSSAAAAAAAGGTEVRPRSVEVGLEERRGKGRAAEELEPGTGTVEDGDGSEDGGSSVASGSGTGTVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQVVYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAISLHTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISSVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSLFMLSFYLSCFLLLALVVFISVIYACVKLFPTPLQTLSRKIVRSKKNSTLVGVFTITLVFLSAFVNMFMCNSKNLVGCLAEEHNITVNQVNACHVMESAFNYSLGDEQGFCGSPQSNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFSNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKAGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
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Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:1409703). Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin. Activated by GNAS. Activity is further increased by interaction with the G protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (By similarity). Phosphorylation by RAF1 results in its activation (By similarity). Interacts with GNAS, GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with RAF1 (By similarity). Detected in brain and kidney. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylated by RAF1. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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P30804
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MSWFSGLLVPKVDERKTAWGERNGQKRPRRGTRTSGFCTPRYMSCLRDAQPPSPTPAAPPRCPWQDEAFIRRGGPGKGTELGLRAVALGFEDTEAMSAVGAAGGGPDVTPGSRRSCWRRLAQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAYVALLACAATLFVALMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAANPRSPSVGLWCPVFFVYITYTLLPIRMRAAVFSGLGLSTLHLILAWQLNRGDAFLWKQLGANMLLFLCTNVIGICTHYPAEVSQRQAFQETRGYIQARLHLPDENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAARAGRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLVFPHSTVMLGIYASIFVLLLITVLTCAVYSCGSLFPKALRRLSRSIVRSRAHSTVVGIFSVLLVFTSAIANMFTCNHTPIRTCAARMLNVTPADITACHLQQLNYSLGLDAPLCEGTAPTCSFPEYFVGNMLLSLLASSVFLHISSIGKLAMIFVLGLIYLVLLLLGPPSTIFDNYDLLLGVHGLASSNDTFDGLDCPAAGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQAGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKRYQLECRGVVKVKGKGEMTTYFLNGGPPS
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Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:1528892, PubMed:17110384). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity). Signaling mediates cAMP-dependent activation of protein kinase PKA (By similarity). This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity). Contributes to bone cell responses to mechanical stimuli (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin. Inhibited by calcium ions, already at micromolar concentrations. Inhibited by adenosine, AMP and their analogs (PubMed:1528892). Activated by GNAS (PubMed:17110384). Is further activated by the complex formed by GNB1 and GNG2 (PubMed:17110384). Phosphorylation by RAF1 results in its activation (By similarity). Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (By similarity). Interacts with RAF1. Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By similarity). Detected in brain and heart. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC on Ser-553, Ser-659 and Thr-916 inhibits catalytic activity. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q9UDB0
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MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGPPRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWRRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAYVALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLWCPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTNVIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSCGSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLTPADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLAMIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
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Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:17916776, PubMed:17110384). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:17916776). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity). Signaling mediates cAMP-dependent activation of protein kinase PKA. This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (PubMed:17916776). Contributes to bone cell responses to mechanical stimuli (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin (PubMed:17916776, PubMed:17110384). Inhibited by calcium ions, already at micromolar concentrations (By similarity). Inhibited by adenosine, AMP and their analogs (By similarity). Activated by GNAS (PubMed:17110384). Is further activated by the complex formed by GNB1 and GNG2 (PubMed:17110384). Phosphorylation by RAF1 results in its activation (By similarity). Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (By similarity). Interacts with RAF1 (PubMed:15385642). Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (PubMed:17110384). Detected in peripheral blood mononuclear leukocytes (at protein level) (PubMed:17916776). Detected in thyroid (PubMed:10978539). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA at Ser-662 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC at Ser-556, Ser-662 and Thr-919 inhibits catalytic activity. The disease is caused by variants affecting the gene represented in this entry. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Extended N-terminus.
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Q01341
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MSWFSGLLVPKVDERKTAWGERNGQKRPRHANRASGFCAPRYMSCLKNAEPPSPTPAAHTRCPWQDEAFIRRAGPGRGVELGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGPSCWHRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPAQPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQLGANVVLFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGGRRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQCIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLVFPYSTLILGIYAAIFLLLLVTVLICAVCSCGSFFPKALQRLSRNIVRSRVHSTAVGIFSVLLVFISAIANMFTCNHTPIRTCAARMLNLTPADVTACHLQQLNYSLGLDAPLCEGTAPTCSFPEYFVGNVLLSLLASSVFLHISSIGKLAMTFILGFTYLVLLLLGPPAAIFDNYDLLLGVHGLASSNETFDGLDCPAVGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
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Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:18071070, PubMed:24363043). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:18071070). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption (PubMed:20466003, PubMed:20864687). Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion (PubMed:24854272). Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (PubMed:23753526). Signaling mediates cAMP-dependent activation of protein kinase PKA and promotes increased phosphorylation of various proteins, including AKT (PubMed:18071070, PubMed:23753526). Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility (PubMed:18071070). May contribute to normal heart function (PubMed:18071070, PubMed:20359598). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity). Contributes to bone cell responses to mechanical stimuli (PubMed:20371630, PubMed:24277577). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin (PubMed:18071070, PubMed:20466003, PubMed:20864687, PubMed:23753526, PubMed:24363043). Inhibited by calcium ions, already at micromolar concentrations (PubMed:1379717, PubMed:18071070). Inhibited by adenosine, AMP and their analogs (By similarity). Activated by GNAS. Is further activated by the complex formed by GNB1 and GNG2 (By similarity). Phosphorylation by RAF1 results in its activation (By similarity). Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (PubMed:21670265). Interacts with RAF1. Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By similarity). Detected in kidney tubules (PubMed:20466003). Detected in primary bone cells with osteocyte morphology (PubMed:24277577). Detected in heart (at protein level) (PubMed:18071070). Highly expressed in heart (PubMed:1379717, PubMed:18071070). Detected in kidney, pancreas acini and ducts (PubMed:23753526). Expressed in cochlear outer and inner hair cells (PubMed:17567809). Weakly detectable in brain, intestine, lung and spleen (PubMed:1379717). In the inner ear, between 16 dpc and P1, present along the sterocilia of outer hair cells, but almost undetectable in inner hair cell hair bundle. From P3 onward, expression in outer hair cell bundles is restricted to their base and it is also expressed at the base of inner hair cell stereocilia. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC on Ser-553, Ser-659 and Thr-916 inhibits catalytic activity. Mutant mice are born at the expected Mendelian rate, present no obvious phenotype and are fertile (PubMed:18071070, PubMed:20466003, PubMed:23753526, PubMed:24277577). Their hearts display a decrease in left ventricular pressure, both at the basal level and after activation of beta-adrenergic receptors (PubMed:18071070). Besides, their hearts show defects in sarcoplasmic Ca(2+) uptake and storage, and decreased levels of protein phosphorylation (PubMed:18071070). Male mice show increased mortality after transversal aortic constriction (PubMed:20359598). In contrast, female mice do not show increased mortality after transversal aortic constriction, and develop less heart hypertrophy and fibrosis than wild-type (PubMed:20359598). Compared to wild-type, mutant mice drink more and produce greater volumes of urine with decreased osmolarity, but there is no difference in the total quantity of excreted urinary solutes and no difference in blood plasma composition (PubMed:20466003, PubMed:20864687). The impaired urinary water homeostasis is due to retention of AQP2 in intracellular vesicles and decreased AQP2 levels at the cell membrane (PubMed:20466003). Mutant mice display increased urinary inorganic phosphate excretion, but normal plasma phosphate levels (PubMed:24854272). Mutant mice display increased plasma levels of PTH and FGF23, the two principal regulators of urinary phosphate excretion (PubMed:24854272). Mutant mice display no obvious skeleton defects, but display less bone formation after load stress than wild-type (PubMed:24277577). Mutant mice lacking both Adcy6 and Pkd1 survive longer and have less severe polycystic kidney disease than mice lacking only Pkd1 (PubMed:24158982). Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q03343
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MSWFSGLLVPKVDERKTAWGERNGQKRPRQATRARGFCAPRYMSCLKNVEPPSPTPAARTRCPWQDEAFIRRAGPGRGVKLGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGPSCWHRLAQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPALPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAANPRSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWHLNNGDPFLWKQLGANVVLFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNGYLKEQCIETFLILGASQKRKEEKAMLVKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKENRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQFLVFPHSALILGIYAGIFLLLLVTVLICAVCSCGSFFPNALQRLSRSIVRSRVHSTAVGVFSVLLVFISAIANMFTCSHTPLRTCAARMLNLTPSDVTACHLRQINYSLGLEAPLCEGTAPTCSFPEYFVGSVLLSLLASSVFLHISSIGKLVMTFVLGFIYLLLLLLGPPATIFDNYDLLLSVHGLASSNETFDGLDCPAVGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
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Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:1409703, PubMed:15385642, PubMed:17110384, PubMed:21606183). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:21606183). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity). Signaling mediates cAMP-dependent activation of protein kinase PKA (PubMed:21606183). This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity). Contributes to bone cell responses to mechanical stimuli (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by forskolin (PubMed:9391159). Inhibited by calcium ions, already at micromolar concentrations (By similarity). Inhibited by adenosine, AMP and their analogs (By similarity). Activated by GNAS (PubMed:9391159, PubMed:17110384). Is further activated by the complex formed by GNB1 and GNG2 (PubMed:17110384). Phosphorylation by RAF1 results in its activation (PubMed:15385642). Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (By similarity). Interacts with RAF1 (PubMed:15385642). Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By similarity). Detected in brain and kidney (PubMed:1409703). Detected in vascular smooth muscle cells (PubMed:21606183). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylation by RAF1 increases enzyme activity (PubMed:15385642). Phosphorylation by PKA on Ser-660 inhibits the GNAS-mediated increase in catalytic activity (PubMed:9391159). Phosphorylation by PKC on Ser-554, Ser-660 and Thr-917 inhibits catalytic activity (PubMed:11877398). Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Extended N-terminus.
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O02856
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MPAKGRYFLNEGEEGPDQDALYEKYRLTSQHGPLLLMLLLVAIAACTTLIVITFSYGDPSRHRAVLGTAFFTLAMFVLLYALVYVECLDRRGLRISALLIWGCLVTLGYVLVFDFDSPRKDTLCLWGRCPSSSFVVFVVYTLLPFSMWGAVTAGLVSSISHLLVLAMHQEDFTSPVGLKLLATAVVFVCGNLTGAFHKHHMQDASHDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKERGDRRYLPDNNFHNLYVKRHQNVSILYADIVGFTRLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPNHARNCVKMGLDMCEAIKQVREATGVDISMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPQPSQHNSKNKGNATLKMRASVRMTRYLESWGAARPFAHLNQRESVSSSETLVSHGRRPKAVPLRRHRTPDRSASPKGRSEDDSYDDEMLSAIEGLSSTRPCCSKSDDFSTFGSIFLEKGFEREYRLAPIPRVRYYFACASLVFVCILLIHVLLLYSMKTLGVSFGLVACVLGLVLGLCFADVFLRCCPALGKLRAIAESVETQPLLRVSLAILTIGSLLVIAVVNLPLMPFRDRGLTAGNETGLRAVSGWEMSPCYLLPYYTCSCILAFIACSVFLRMSLELKVVLLTVALVAYLVLFNVYPSWQWDCCGHSLGNLTGTNGTLSSSSCSWHLKTMTNFYLVLFYTTLIMLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVPSGPENQDLERQHAHIGIMVEFSTALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLIDVKGKGELRTYFVCTDTAKFQGLGLN
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Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors. Functions in signaling cascades activated namely by thrombin and sphingosine 1-phosphate and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G alpha protein with GNA13 (By similarity). Also, during inflammation, mediates zymosan-induced increase intracellular cAMP, leading to protein kinase A pathway activation in order to modulate innate immune responses through heterotrimeric G proteins G(12/13) (By similarity). Functions in signaling cascades activated namely by dopamine and C5 alpha chain and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G protein with G beta:gamma complex (By similarity). Functions, through cAMP response regulation, to keep inflammation under control during bacterial infection by sensing the presence of serum factors, such as the bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha production. However, it is also required for the optimal functions of B and T cells during adaptive immune responses by regulating cAMP synthesis in both B and T cells (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by the G protein alpha subunit. Activated by the G protein beta and gamma subunit complex. Activated by GNA13 and GNA12. Ethanol and phorbol 12,13-dibutanoate significantly potentiate adenylate cyclase activity generated in response to the activation of the prostanoid receptor by the agonist prostaglandin E1(1-) in a PKC-dependent manner (By similarity). Inhibited by lithium (By similarity). Found exclusively in the retinal pigment epithelium. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylated by PRKCD. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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A0AVA6
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MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRASVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRSEDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACASLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISERVETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLPYYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKPNGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
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Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors (Probable). Functions in signaling cascades activated namely by thrombin and sphingosine 1-phosphate and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G alpha protein with GNA13 (PubMed:23229509, PubMed:18541530). Also, during inflammation, mediates zymosan-induced increase intracellular cAMP, leading to protein kinase A pathway activation in order to modulate innate immune responses through heterotrimeric G proteins G(12/13) (By similarity). Functions in signaling cascades activated namely by dopamine and C5 alpha chain and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G protein with G beta:gamma complex (PubMed:23842570, PubMed:23229509). Functions, through cAMP response regulation, to keep inflammation under control during bacterial infection by sensing the presence of serum factors, such as the bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha production. However, it is also required for the optimal functions of B and T cells during adaptive immune responses by regulating cAMP synthesis in both B and T cells (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by the G protein alpha subunit (PubMed:18541530). Activated by the G protein beta and gamma subunit complex (PubMed:23229509). Activated by GNA13 and GNA12 (PubMed:18541530). Ethanol and phorbol 12,13-dibutanoate significantly potentiate adenylate cyclase activity generated in response to the activation of the prostanoid receptor by the agonist prostaglandin E1(1-) in a PKC-dependent manner (PubMed:12454008). Inhibited by lithium (By similarity). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylated by PRKCD. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q3U3P2
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MPAKGRYFLNEGDEGPDQAALYEKYRLTSLHGPLLLLLLLVAAATCIALISIAFSHEDLRRHQVVLGTAFLMLTLFVALYVLVYVECLVQRWLRALALLTWACLMVLGSVLMWDSLENEAHAWEQVPFFLFVVFVVYALLPLSRRAAIVAGVTSTVSHLLVFGAVTRAFQTSMSSTQLGLQLLANAVILLGGNFTGAFHKHQLQDASRDLFIYTVKCIQIRRKLRVEKRQQENLLLSVLPAHISMGMKLAIIERLKEGGDRHYMPDNNFHSLYVKRHQNVSILYADIVGFTRLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDICEAIKQVREATGVDISMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLNHLDKAYEVEDGHGEQRDPYLKEMNIRTYLVIDPRSQQPPPPSHHLSKPKGDATLKMRASVRVTRYLESWGAARPFAHLNHRESVSSSETPISNGRRQKAIPLRRHRAPDRSASPKGRLEDDCDDEMLSAIEGLSSTRPCCSKSDDFHTFGPIFLEKGFEREYRLVPIPRARYDFACASLVFVCILLVHLLVMPRMATLGVSFGLVACLLGLVLSFCFATEFSRCFPSRSTLQAISESVETQPLVRLVLVVLTVGSLLTVAIINMPLTLNPGPEQPGDNKTSPLAAQNRVGTPCELLPYYTCSCILGFIACSVFLRMSLELKAMLLTVALVAYLLLFNLSPCWHVSGNSTETNGTQRTRLLLSDAQSMPSHTLAPGARETAPSPSYLERDLKIMVNFYLILFYATLILLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKAAEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSAPSGHENQDLERKHVHIGVLVEFSMALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
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Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors (Probable). Functions in signaling cascades activated namely by thrombin and sphingosine 1-phosphate and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G alpha protein with GNA13 (PubMed:18541530). Also, during inflammation, mediates zymosan-induced increase intracellular cAMP, leading to protein kinase A pathway activation in order to modulate innate immune responses through heterotrimeric G proteins G(12/13) (PubMed:23178822). Functions in signaling cascades activated namely by dopamine and C5 alpha chain and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G protein with G beta:gamma complex (By similarity). Functions, through cAMP response regulation, to keep inflammation under control during bacterial infection by sensing the presence of serum factors, such as the bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha production. However, it is also required for the optimal functions of B and T cells during adaptive immune responses by regulating cAMP synthesis in both B and T cells (PubMed:20505140). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by the G protein alpha subunit. Activated by the G protein beta and gamma subunit complex. Activated by GNA13 and GNA12. Ethanol and phorbol 12,13-dibutanoate significantly potentiate adenylate cyclase activity generated in response to the activation of the prostanoid receptor by the agonist prostaglandin E1(1-) in a PKC-dependent manner (By similarity). Inhibited by lithium (PubMed:18205980). Most abundant in heart, spleen and lung. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Phosphorylated by PRKCD. Knockout Adcy7 homozygous mice die during embryogenesis (more than 93%). To obtain adult animals with Adcy7-deficient immune systems, the hematopoietic stem cells obtained from the rare adult Adcy7 homozygous mice are transplanted into lethally irradiated wild-type animals. All chimeric mice survived the transplant procedure and appeared healthy. Adcy7-deficient mice appear to be hypersensitive to lipopolysaccharide-induced endotoxic shock and display a higher mortality rate. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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P40145
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MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGSGSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASGSGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHTYLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAHCCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPEDIVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINETYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEVSLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLILKDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLVQSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
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Catalyzes the formation of cAMP in response to calcium entry leadings to cAMP signaling activation that affect processes suche as synaptic plasticity and insulin secretion. Plays a role in many brain functions, such as learning, memory, drug addiction, and anxiety modulation through regulation of synaptic plasticity by modulating long-term memory and long-term potentiation (LTP) through CREB transcription factor activity modulation. Plays a central role in insulin secretion by controlling glucose homeostasis through glucagon-like peptide 1 and glucose signaling pathway and maintains insulin secretion through calcium-dependent PKA activation leading to vesicle pool replenishment. Also, allows PTGER3 to induce potentiation of PTGER4-mediated PLA2 secretion by switching from a negative to a positive regulation, during the IL1B induced-dedifferentiation of smooth muscle cells. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). At rest, the N- and C-terminal domains interact, as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain. Upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain. Fully calcium-saturated calmodulin then leaves the N-terminal domain, binding solely to the C-terminal domain, and the whole autoinhibitory complex dissociates, resulting in activation of adenylate cyclase. As local calcium concentrations decrease, the calmodulin becomes calcium free and binds once more to the N-terminal domain, whereupon the whole system returns to rest with the re-association of the autoinhibitory complex. In non-excitable cells, activated by capacitative calcium entry (CCE) through store-operated channels, namely through interaction with ORAI1 and STIM1; membrane raft and caveolae localization and membrane integrity are indispensable. CCE-mediated adenylate cyclase activity is decreased by AKAP5 and AKAP7. CCE-mediated adenylate cyclase activity is up-regulated by AKAP9 and the mitochondrially targeted AKAP1. In excitable cells, activated during membrane depolarization through L-type voltage-gated calcium channels (VGCC), leading to calcium entry; the L-type alpha subunit is sufficient. Activated via stimulation of the GLP1R. Synergistically activated by calcium/calmodulin and GNAS. Stimulated by forskolin. Inhibited by PKA directly bound to AKAP5 at membrane raft. Inhibition by acute activation of OPRM1 and activation by chronic activation of OPRM1 is mediated by pertussis toxin-sensitive G(i) and G(o) G alpha proteins and G beta-gamma dimer. Activity is inhibited by G beta-gamma dimer. Homodimer; via transmembrane domain. Monomer. Heterodimer. Oligemer; via transmembrane domain. Interacts with PRKAR2A and AKAP5; inhibits adenylate cyclase activity through PKA phosphorylation. Interacts with PPP2CA and PPP2R1A; does not mediate the inhibitory effects of PKA on adenylate cyclase activity; interaction is dependent of catalytically active PPP2CA; antagonizes interaction with calmodulin. Interacts with AKAP5 (palmitoylated form); promotes the phosphorylation of ADCY8 after store-operated calcium entry (SOCE) stimulation at membrane raft. Interacts with ORAI1; interaction is calcium store depletion independent; interaction occurs in membrane raft; interaction increases markedly after store depletion; positively regulates SOCE-induced adenylate cyclase activity; contributes to the targeting of ADCY8 to discrete regions of the plasma membrane that are shielded from other calcium events. Interacts with STIM1. Interacts with actin; interaction is calcium independent; interaction is affected by calcium-calmodulin; interaction controls the distribution and regulation of ADCY8. Interacts with calmodulin; at rest, interacts via N-terminal domain; upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain forming an autoinhibitory complex; fully calcium-saturated calmodulin leaves the N-terminal domain, binding solely to the C-terminal domain leading to dissociation of autoinhibitory complex and resulting in activation of adenylate cyclase; antagonizes interaction with PPP2CA; interaction is calcium dependent. Interacts with PPP2R5D. Localized to dendritic arbors (By similarity). Monomeric N-glycosylated species localizes in membrane raft. In contrast, monomeric unglycosylated forms are enriched in clathrin-coated pits and vesicles. Dimers are also localized outside of membrane rafts. Membrane raft localization and integrity is indispensable for CCE-stimulated adenylate cyclase activity (By similarity). Detected in brain cortex (PubMed:1715695). Expressed in islet (PubMed:25403481). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. The two transmembrane clusters are necessary and suficient for the plasma membrane targeting and oligomers assembly. The N-terminal and C-terminal domains interact at rest as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain; the binding is specifically inhibited by fully calcium-saturated calmodulin, resulting in activation of AC8. Phosphorylated by PKA; mediates inhibition of adenylate cyclase activity at membrane raft; does not influence either CALM1 or PPP2CA interaction with ADCY8. N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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G3X8V9
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MELSDVHCLSGSEELYTIQPTPPAGDDGSGSRPQRLLWQTAVRHITEQRFIHGHRGGGGGGVSRKASNPAGSGPNHHAPQLSSDSVLPLYSLGPGERAHNTGGTKVFPERSGSGSASGSGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDNTSHTYLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVTLQVLIPRLAVFSINQVLAQVVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRRDHAHCCVEMGLSMIKTIRFVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEESLLCLPEDIVKESVSCSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLLFITAIQSLLPSSRLMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINETYLARNVIIFASILINFLGAVLNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETIYAGLFLSYDNLNHSGEDFLGTKEASLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLILKDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLVQSLNRQRQKQLLNENSNSGIIKSHYNRRTLLTPSGPEPGAQAEGTDKSDLP
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Catalyzes the formation of cAMP in response to calcium entry leadings to cAMP signaling activation that affect processes suche as synaptic plasticity and insulin secretion (PubMed:10864938, PubMed:25403481, PubMed:10482244, PubMed:14585998, PubMed:18448650). Plays a role in many brain functions, such as learning, memory, drug addiction, and anxiety modulation through regulation of synaptic plasticity by modulating long-term memory and long-term potentiation (LTP) through CREB transcription factor activity modulation (PubMed:10482244, PubMed:14585998, PubMed:18448650, PubMed:10864938, PubMed:12441059, PubMed:20638449, PubMed:27234425, PubMed:18222416). Plays a central role in insulin secretion by controlling glucose homeostasis through glucagon-like peptide 1 and glucose signaling pathway and maintains insulin secretion through calcium-dependent PKA activation leading to vesicle pool replenishment (PubMed:25403481). Also, allows PTGER3 to induce potentiation of PTGER4-mediated PLA2 secretion by switching from a negative to a positive regulation, during the IL1B induced-dedifferentiation of smooth muscle cells (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). At rest, the N- and C-terminal domains interact, as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain. Upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain. Fully calcium-saturated calmodulin then leaves the N-terminal domain, binding solely to the C-terminal domain, and the whole autoinhibitory complex dissociates, resulting in activation of adenylate cyclase. As local calcium concentrations decrease, the calmodulin becomes calcium free and binds once more to the N-terminal domain, whereupon the whole system returns to rest with the re-association of the autoinhibitory complex (PubMed:14585998). In non-excitable cells, activated by capacitative calcium entry (CCE) through store-operated channels, namely through interaction with ORAI1 and STIM1; membrane raft and caveolae localization and membrane integrity are indispensable. CCE-mediated adenylate cyclase activity is decreased by AKAP5 and AKAP7. CCE-mediated adenylate cyclase activity is up-regulated by AKAP9 and the mitochondrially targeted AKAP1. In excitable cells, activated during membrane depolarization through L-type voltage-gated calcium channels (VGCC), leading to calcium entry; the L-type alpha subunit is sufficient. Activated via stimulation of the GLP1R. Synergistically activated by calcium/calmodulin and GNAS. Stimulated by forskolin. Inhibited by PKA directly bound to AKAP5 at membrane raft. Inhibition by acute activation of OPRM1 and activation by chronic activation of OPRM1 is mediated by pertussis toxin-sensitive G(i) and G(o) G alpha proteins and G beta-gamma dimer. Activity is inhibited by G beta-gamma dimer (By similarity). Homodimer; via transmembrane domain (PubMed:19158400). Monomer (PubMed:19158400). Heterodimer. Oligemer; via transmembrane domain. Interacts with PRKAR2A and AKAP5; inhibits adenylate cyclase activity through PKA phosphorylation. Interacts with PPP2CA and PPP2R1A; does not mediate the inhibitory effects of PKA on adenylate cyclase activity; interaction is dependent of catalytically active PPP2CA; antagonizes interaction with calmodulin. Interacts with AKAP5 (palmitoylated form); promotes the phosphorylation of ADCY8 after store-operated calcium entry (SOCE) stimulation at membrane raft. Interacts with ORAI1; interaction is calcium store depletion independent; interaction occurs in membrane raft; interaction increases markedly after store depletion; positively regulates SOCE-induced adenylate cyclase activity; contributes to the targeting of ADCY8 to discrete regions of the plasma membrane that are shielded from other calcium events. Interacts with STIM1. Interacts with actin; interaction is calcium independent; interaction is affected by calcium-calmodulin; interaction controls the distribution and regulation of ADCY8. Interacts with calmodulin; at rest, interacts via N-terminal domain; upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain forming an autoinhibitory complex; fully calcium-saturated calmodulin leaves the N-terminal domain, binding solely to the C-terminal domain leading to dissociation of autoinhibitory complex and resulting in activation of adenylate cyclase; antagonizes interaction with PPP2CA; interaction is calcium dependent. Interacts with PPP2R5D (By similarity). Localized to dendritic arbors (PubMed:17335981). Monomeric N-glycosylated species localizes in membrane raft. In contrast, monomeric unglycosylated forms are enriched in clathrin-coated pits and vesicles. Dimers are also localized outside of membrane rafts. Membrane raft localization and integrity is indispensable for CCE-stimulated adenylate cyclase activity (By similarity). Abundantly expressed within the olfactory bulb, thalamus, habenula, CA1 region of the hippocampus, and hypothalamus (PubMed:10864938). Strongly expressed in pyramidal cells of CA1 and weakly in CA3 and the dentate gyrus. Strongly and homogeneously expressed in all cell layers of the anterior cingulate cortex (ACC). Widely expressed in the insular cortex. Weakly expressed in the spinal dorsal horn (PubMed:12441059). Abundantly present in the CA1/CA2 region in the hippocampus neonatal and intensifies by adulthood. Weakly expressed in the cerebellum at postnatal day 7 and decreased further by postnatal day 14 (PubMed:17335981). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. The two transmembrane clusters are necessary and suficient for the plasma membrane targeting and oligomers assembly. The N-terminal and C-terminal domains interact at rest as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain; the binding is specifically inhibited by fully calcium-saturated calmodulin, resulting in activation of AC8. Phosphorylated by PKA; mediates inhibition of adenylate cyclase activity at membrane raft; does not influence either CALM1 or PPP2CA interaction with ADCY8. N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity. Adcy8 knockout mice are fertile and seem normal. However mice reveal a tendency for both male and female to be somewhat smaller from day of life 45 and 30 respectively while food intake is normal. From there, females remain 10-15% smaller. In contrast, male transiently grew more slowly between day of life 45 and 92, after which point differences are not significant. Mice are less nervous. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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P40146
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MELSDVHCLSGSEELYTIHPTPPAADGGSGSRPQRLLWQTAVRHITEQRFIHGHRGGGGGGSRKASNPAGSGPNHHAPQLSSDSVLPLYSLGSGERAHNTGGTKVFPERSGSGSASGSGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHTYLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVTLQVLIPRLAVFSINQVLAQVVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEARLRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADVKGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAHCCVEMGLSMIKTIRFVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKLESGGIPGRIHISKATLDCLSGDYNVEEGHGKERNEFLRKHNIETYLIKQPEESLLSLPEDIVKESVSCSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHVQSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAFIVLLFITAIQSLLPSSRLMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINETYLARNVIIFASILINFLGAVINILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTGVLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETIYAGLFLSYDNLNHSGEDFLGTKEASLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKDLREHNENMLRNILPGHVARHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDELLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKHSFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLILKDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLVQSLNRQRQKQLLNENSNSGIIKSHYNRRTLLTPSGPEPGAQAEGTDKSDLP
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Catalyzes the formation of cAMP in response to calcium entry leadings to cAMP signaling activation that affect processes suche as synaptic plasticity and insulin secretion (PubMed:8163524, PubMed:24086669, PubMed:22494970, PubMed:21046358, PubMed:13680124, PubMed:25381556). Plays a role in many brain functions, such as learning, memory, drug addiction, and anxiety modulation through regulation of synaptic plasticity by modulating long-term memory and long-term potentiation (LTP) through CREB transcription factor activity modulation (PubMed:8163524). Plays a central role in insulin secretion by controlling glucose homeostasis through glucagon-like peptide 1 and glucose signaling pathway and maintains insulin secretion through calcium-dependent PKA activation leading to vesicle pool replenishment (PubMed:21046358, PubMed:13680124, PubMed:25381556). Also, allows PTGER3 to induce potentiation of PTGER4-mediated PLA2 secretion by switching from a negative to a positive regulation, during the IL1B induced-dedifferentiation of smooth muscle cells (PubMed:16741924). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). At rest, the N- and C-terminal domains interact, as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain. Upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain. Fully calcium-saturated calmodulin then leaves the N-terminal domain, binding solely to the C-terminal domain, and the whole autoinhibitory complex dissociates, resulting in activation of adenylate cyclase. As local calcium concentrations decrease, the calmodulin becomes calcium free and binds once more to the N-terminal domain, whereupon the whole system returns to rest with the re-association of the autoinhibitory complex (PubMed:8163524, PubMed:8557635, PubMed:19305019). In non-excitable cells, activated by capacitative calcium entry (CCE) through store-operated channels, namely through interaction with ORAI1 and STIM1; membrane raft and caveolae localization and membrane integrity are indispensable (PubMed:19158400, PubMed:11744699, PubMed:19171672, PubMed:22494970, PubMed:20410303). CCE-mediated adenylate cyclase activity is decreased by AKAP5 and AKAP7. CCE-mediated adenylate cyclase activity is up-regulated by AKAP9 and the mitochondrially targeted AKAP1 (PubMed:20410303). In excitable cells, activated during membrane depolarization through L-type voltage-gated calcium channels (VGCC), leading to calcium entry; the L-type alpha subunit is sufficient (PubMed:24086669, PubMed:25381556). Activated via stimulation of the GLP1R (PubMed:25381556). Synergistically activated by calcium/calmodulin and GNAS (PubMed:13680124). Stimulated by forskolin (PubMed:16186630, PubMed:13680124). Inhibited by PKA directly bound to AKAP5 at membrane raft (PubMed:22976297, PubMed:21771783). Inhibition by acute activation of OPRM1 and activation by chronic activation of OPRM1 is mediated by pertussis toxin-sensitive G(i) and G(o) G alpha proteins and G beta-gamma dimer. Activity is inhibited by G beta-gamma dimer (PubMed:16186630). Homodimer; via transmembrane domain (PubMed:19158400, PubMed:11856299). Monomer (PubMed:19158400). Heterodimer (PubMed:11856299). Oligemer; via transmembrane domain (PubMed:11856299). Interacts with PRKAR2A and AKAP5; inhibits adenylate cyclase activity through PKA phosphorylation (PubMed:22976297). Interacts with PPP2CA and PPP2R1A; does not mediate the inhibitory effects of PKA on adenylate cyclase activity; interaction is dependent of catalytically active PPP2CA; antagonizes interaction with calmodulin (PubMed:22976297, PubMed:16258073). Interacts with AKAP5 (palmitoylated form); promotes the phosphorylation of ADCY8 after store-operated calcium entry (SOCE) stimulation at membrane raft (PubMed:21771783, PubMed:20410303). Interacts with ORAI1; interaction is calcium store depletion independent; interaction occurs in membrane raft; interaction increases markedly after store depletion; positively regulates SOCE-induced adenylate cyclase activity; contributes to the targeting of ADCY8 to discrete regions of the plasma membrane that are shielded from other calcium events (PubMed:22494970). Interacts with STIM1 (PubMed:22494970). Interacts with actin; interaction is calcium independent; interaction is affected by calcium-calmodulin; interaction controls the distribution and regulation of ADCY8 (PubMed:22399809). Interacts with calmodulin; at rest, interacts via N-terminal domain; upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain forming an autoinhibitory complex; fully calcium-saturated calmodulin leaves the N-terminal domain, binding solely to the C-terminal domain leading to dissociation of autoinhibitory complex and resulting in activation of adenylate cyclase; antagonizes interaction with PPP2CA; interaction is calcium dependent (PubMed:19305019, PubMed:16258073, PubMed:22399809). Interacts with PPP2R5D (PubMed:22976297). Localized to dendritic arbors (By similarity). Monomeric N-glycosylated specieslocalized in membrane raft. In contrast, monomeric unglycosylated forms are enriched in clathrin-coated pits and vesicles. Dimers are also localized outside of membrane rafts. Membrane raft localization and integrity is indispensable for CCE-stimulated adenylate cyclase activity (PubMed:19158400). Brain (PubMed:13680124, PubMed:8557635). Expressed in insulin-producing cells (PubMed:13680124). Reduces by glucose (PubMed:21046358). Up-regulated during vascular smooth muscle cell de-differentiation by IL1B (PubMed:16741924). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. The two transmembrane clusters are necessary and suficient for the plasma membrane targeting and oligomers assembly (PubMed:11856299). The N-terminal and C-terminal domains interact at rest as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain; the binding is specifically inhibited by fully calcium-saturated calmodulin, resulting in activation of AC8 (PubMed:19305019). Phosphorylated by PKA; mediates inhibition of adenylate cyclase activity at membrane raft; does not influence either CALM1 or PPP2CA interaction with ADCY8. N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity. N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity. EC50 is approximately 4 times more sensitive to stimulation by calcium/calmodulin than isoform 1 and 2. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q9DGG6
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MASPPHQQLLHHHSTEVSCDSSGDSNSVTVRINPRQQQALSAKRCKYSISSSCSSGESGGVGRGGGGGLRRQKKLPQLFERASSRWWDPKFDSTNLEEASMERCFPQTQRRFRYALFYIGSACLLWGIYFGVHMREKQMVFMVPALCFLLVCVAFFAFTFTKAYARRYVWTSGYTLLVFALTLAPQFQPWTLGERQRVQPRPAAPVDTCLSQVGSFSMCVEVLLLLYTVMHLPLYLSLFLGLSYSVLFETSAFRDESCTLLGGGAVYWELLSKAFLHVCIHAIGIHLFIMSEVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDDESENSVKRHSTSSPKNRKKKPSIQKTPIIFRPFKMQQIEQVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEDTKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGKVTERVGQSAVADQLKGLKTYLISGQKVKEPHCSCSQALLQLGGWGWSQMQAAPSAENTADSTKALKHVEKPKPCPSCSTTLVPPCDVSIDEGAIQNGCQDEHKNSTKAPGGHSPKTQNGLLSPPQEEKLSNSQTSLYEMLQEKGRWGGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPISKLSLNFLDQDLEMAYRTSYQEEVMRNAPVKTFASATFSSLLDVFLSTTVFLILSVTCFLKHGMVASPPPPAAVVVFVIAILLEVLSLVISVRMVFFLEEVMACTKRLLELISGWLPRHFLGAILVSLPALAVFSHFTSDFETNIHYTMFMCCAILIAIVQYCNFCQLSSWMRSLLATVVGAVLLILLYVSLCPDSSVETLHLDLAQNLSSRKSPCNSSMPADVKRPADLIGQEVILAVFLLLLLVWFLNRSFEVSYRLHYHGDVEADLHRTKIQSMRDQPDSCVRNIIPYHVADELKVSQSYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPHYSSIEKIKTIGATYMAASGLNTSQCQDSNHPHGHLQTLFEFAKEMMRVVDDFNNNMLWFNFKLRIGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTIGVECRIQVSEETYRILSKMGYDFDYRGTVNVKGKGQMKTYLYPKCMDNGIVPHHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQNSDKTAHATDNSETKDALPSSKKLQKEPTKAEERCRFGKAVEKTDCEEAGTEEVNELTKLNVSKSV
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Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Insensitive to calcium/calmodulin, forskolin and somatostatin. Stimulated by beta-adrenergic receptor activation. Activity is down-regulated by calcium/calcineurin. Detected in embryonic heart (at protein level). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q9UGP2
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MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDSGGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYALFYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKRHATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVSSGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKNSTKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTFASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIRMVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGSAALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSERNPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEERGRFGKAIEKDDCDETGIEEANELTKLNVSKSV
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Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors (PubMed:9628827, PubMed:12972952, PubMed:15879435, PubMed:10987815). Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and beta-adrenergic receptors (PubMed:9628827). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Insensitive to calcium/calmodulin, forskolin and somatostatin. Stimulated by beta-adrenergic receptor activation (PubMed:9628827). Activity is down-regulated by calcium/calcineurin (PubMed:10987815). Detected in skeletal muscle, pancreas, lung, heart, kidney, liver, brain and placenta (PubMed:9628827, PubMed:10987815). Expressed in multiple cells of the lung, with expression highest in airway smooth muscle (PubMed:12972952). The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Extended N-terminus.
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Q61279
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MASSPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNTHPKHCKYSISSSCSSSGDSGGLPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSMNLEEACLERCFPQTQRRFRYALFYVGFACLLWSIYFAVHMKSKVIVMVVPALCFLVVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVWTPLSGRVDSSNHTLTATPADTCLSQVGSFSICIEVLLLLYTVMQLPLYLSLFLGVVYSVLFETFGYHFRNEDCYPSPGPGALHWELLSRALLHVCIHAIGIHLFVMSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKRHATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEQTKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGRVIERLGQSVVADQLKGLKTYLISGQRAKESHCSCAEALLSGFEVIDDSRESSGPRGQGTASPGSVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGTVQNGCQDEPKTSTKASGGPNSKTQNGLLSPPAEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTFASATFSSLLDVFLSTTVFLILSITCFLKYGATATPPPPAALAVFGADLLLEVLSLIVSIRMVFFLEDVMTCTKWLLEWIAGWLPRHCIGAILVSLPALAVYSHITSEFETNIHVTMFTGSAVLVAVVHYCNFCQLSSWMRSSLATIVGAGLLLLLHISLCQDSSIVMSPLDSAQNFSAQRNPCNSSVLQDGRRPASLIGKELILTFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPDYNSIEKIKTIGATYMAASGLNTAQCQEGGHPQEHLRILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDNGVVPQHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQYSDKASLGSDDSTQAKEARLSSKRSWREPVKAEERFPFGKAIEKDSCEDIGVEEASELSKLNVSKSV
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Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and by beta-adrenergic receptors. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Insensitive to calcium/calmodulin, forskolin and somatostatin. Stimulated by beta-adrenergic receptor activation. Activity is down-regulated by calcium/calcineurin. Detected in brain, spleen, lung, liver and testis (at protein level). Detected in brain, especially in hippocampus, cerebellum and neocortex. Found in decreasing order in skeletal muscle, heart, adrenal gland, ovary and brain; and to a lesser extent, in kidney, liver, testis, lung, thymus and spleen. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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P98999
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MASPVNQQLLHHTEVRCDGSGDGSSVTVRINRQHHQAPSRRCKYSISSSCSSGESGVKKTGGSGGARRQKKLPQLFERSTSNWWNPKFDSNNLEEACVERCFPQTQRRFRYALMYLSVAGLLWSIYFSVHMKTKLVSHLVPTLCFLIVCLGFFFFTFTKSYARHCTAISLLVTLLVFTLTLASQFQVLNPGLGSDSLSNLTSFSATGSSSCLSQVGSFSICVEVLLLLYTVMHLPLYLSACLGVAYSILFETFGYHFRDESCFVLLVGRMAHWELLSKALLHVCIHAIGVHLFIMSEVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDDESENSVKRHSASSPKSRKKKSSIQKTPIIFRPFKMQRIEQVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRPDHAYCCIEMGLGMIEAIDQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEKTARYLDDRYLMEDSMVVERLGQIVAADQLKGLKTFLISGGRTRVPSCSCSQTLIPVQEGTDLSSPSLAPHVQAAISETSDSHTNCTQPETLKSCPSCGETAARDGPEEGVSAANGGGEEWKGGAPRPSAIGASLKDPERSPESSTGDTLTNSQASLYDMLQEKGRWCGVSMDQSALLPLRFKNIREKTDAHFVEVIKEDSLMKDYFFKPPINPLSLNFLDKELETSYRASYQEEVIRMAPVKTFASATFSSLQDVLLNYFIFVLLSVACLLKPGTNTVSPPTLALVLLSVCGLLGFLSLLVSVRMAFYLEDMLLCTRRLLEIISGWVPRHFIGTVLVCLPAAVIFSYLSSDFYTDIHYTMFLCSALLIPMVQYCNFCQLSSSALLLATITGATMLILIYLPLCPQRPPLDPGTDIEANLSTSNSSYETLDNPRTELPFTRLGQEIAVAYFLLLLLVWFLNREFDVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQSYSKNHDDAGVIFASIVNFSEFYEENYEGGKECYRALNELIGDFDELLSKPHYSCIEKIKTIGATYMAASGLNPSQCQDSSQPHRHLQTLFEFAKEMMSVVDEFNNNMLWFNFKLRIGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQASEESYRVLVKMGYDFDYRGTVNVKGKGQMKTYHFPKCTDNGGLVPHHQLCISPDIRVQVDGSIGRSPTDEISSLVTGGKGAVELGSGEAERKREKAEERGRDGGAR
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Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Detected in oocytes. The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q9NNX0
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MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFTAMTEKFSSAMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVIKCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDETHSHFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCTTFMHYYPSGEHKNLLRLACTLKPDPELEMSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLMFEDQDKAEEIGPAIQDAYMHITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELTHALECAMDIFDFCSQVHKIQTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNLAARMMMYYPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNRKEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRIIAISLNKISFHQTFYTIQMFMANVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIFHVQFPISREISRMSTLKKQKQLEILFMKILKLIVKEERIIFIIDEAQFVDSTSWRFMEKLIRTLPIFIIMSLCPFVNIPCAAARAVIKNRNTTYIVIGAVQPNDISNKICLDLNVSCISKELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLNMVTLHSDKESEEVCHLTSGVRLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQKALKQNDPSFEVHYRSLSLKPSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEEDAHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSNSEIPETSAFFPENRSPEEIREKILNFFDHVLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGENDKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKKDKSWSQTFESATFYSLKGEVCFNMGQIVLAKKMLRKALKLLNRIFPYNLISLFLHIHVEKNRHFHYVNRQAQESPPPGKKRLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSLYHHLAGYKGVWFKYEVMAMEHIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGSRALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVLGRLWELSVTQEHIFSKAFFYFVCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFYKFSNRAKNLLPRRTMTLTYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLVAQNTTGPVFCPRLYHLMAYVCILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESWYSTSELKEDQWLQTILSLPSWEKIVAGRVNIQDLQKNKFLMRANTVDNHF
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Catalyzes the formation of the signaling molecule cAMP (PubMed:12609998, PubMed:15659711, PubMed:24616449, PubMed:25040695, PubMed:24567411). May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (PubMed:15659711, PubMed:17591988). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (By similarity). Involved in ciliary beat regulation (PubMed:17591988). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit (PubMed:25040695). Is also active with manganese (in vitro) (PubMed:12609998, PubMed:15659711, PubMed:24616449). Activated by manganese or magnesium ions (PubMed:12609998, PubMed:24616449). In the presence of magnesium ions, the enzyme is activated by bicarbonate (PubMed:12609998, PubMed:15659711, PubMed:24567411). In the presence of manganese ions, the enzyme is inhibited by bicarbonate (PubMed:15659711). In the absence of magnesium and bicarbonate, the enzyme is weakly activated by calcium (PubMed:15659711). Calcium mildly increases the enzyme activity, also in the presence of magnesium ions (PubMed:15659711, PubMed:25040695). Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane-associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. Detected in airway epithelial cells and testis (at protein level) (PubMed:17591988). Weakly expressed in multiple tissues. Expressed in brain, heart, kidney, liver, lung, pancreas, peripheral blood leukocytes, placenta, skeletal muscle, stomach, thymus, airway epithelial cells, duodenum, jejunum and ileum. Very low level of expression in bone. The N-terminal guanylate cyclase domains are required for enzyme activity. Fragments or isoforms containing the first 470 amino acid residues are fully active. Cleavage may occur to generate the active 48 kDa form. Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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Q3V0F8
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MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYISAIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEAEEGLDIRVKIGLAAGHITMLVFGDETRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFTKCMGFMDYYPSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKVEVIGSAIQAACVHITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNIAARMMMYYPGIVSCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNRYEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQILMANVLGLDTCKHYKERQTNLQNRVKTLLDEKFHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILAQTVREERIIFIIDEAQFVDGTSWAFIEKLIRSMPIFIVMSLAPFSEVPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIPRELDSYLVEGSCGIPYYCEELLKNLDHHRVLLFQQAETEQKTNVTWNNMFKHSVRPTDDMQLFTSISEGQKEVCYLVSGVRLNNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFNCFRSSKDLQLALKQNVPTFEVHYRSLALKLKEGLTYGEEEELREMEGEVVECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEESAHRCNHCRNVDFIPYHHFIVDIRLNTLDMDTVKRMVTSQGFKIDEEEAIFSKSELPRKYKFPENLSITEIREKILHFFDNVILKMKSSPNDIIPLESCQCKELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTNEDSWSQTFEYATFYSLKAEVCFNMGQMVLAKKMLRKALKLLNRMFPCNLLTLTFQMHVEKNRLSHFMNQHTQEGSVPGKKLAQLYLQASCFSLLWRIYSLNFFFHYKYYGHLAAMMEMNTSLETQNDFQIIKAYLDFSLYHHLAGYQGVWFKYEILVMEQLLNLPLKGEAIEIMAYTADTLGHIKFLMGHLDLAIELGSRAHRMWSLLRNPNKYQMVLCRLSKPLFLKSRYKHLVQVLGWLWDLSVTEEDIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFNKFSDRAKHLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVEILKALETLVAQNTTGPVFYPRLYHLMAYVCILMGDGHSCDFFLNTALELSETHGNLLEKCWLSMSKEWWYSASELTGDQWLQTVLSLPSWDKIVSGKGGQRKRSWSWFCPPNFSMVSWSQPQCA
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Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (PubMed:14976244, PubMed:16054031). Involved in ciliary beat regulation (By similarity). ATP = 3',5'-cyclic AMP + diphosphate Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). Activated by manganese or magnesium ions. In the presence of magnesium ions, the enzyme is activated by bicarbonate. Calcium mildly increases the enzyme activity, also in the presence of magnesium ions. Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane-associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. Expressed in testis. The N-terminal guanylate cyclase domains are required for enzyme activity. Fragments containing the first 470 amino acid residues are fully active. Mice are infertile because of a severe sperm-motility defect. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
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A2RFA9
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MKLIYTEMSYSMTEILVNEARKAADQGYRVFYIAPNSLSFEKEREVLTLLPERGTFSIIVTRFVQMSRYFTVESSPSKQHLDDTTLAMIFYRALMQLKPEDLPSYGRLQNNSVFIEQLVELYKELKNAQLSVHDLTGLDHPQKQEDLIKIIELAETIMIQQDYNQDSPLQSFARAIKLGLLNNQLSKTVVVIDGFSRFSAEEDYLLSLLNNNCQEVIIGSYVSQKAYQKSFIKGNIYEASLHFLQDLAQKYHIKPVFATSNQVFKPAFSRLTQLFEATHDFSQVDWQLQKNDLDHFSLWQCHHQKEEIEHVAKSIRQKLYEGYRYKDILVLLGDMDAYQLQIGPIFDKFEIPYYLGKAEPMAAHPLVQFIESLERSQRYNWRREDILNMLKSGLFGCFDDSDIDRFEEYTQFADIKGFTKFSKPFTINSSRQYPLDFLNEMRQDIVLPLQELFKSQKQLGASLVDKLILFLKKIRLAENMQGLAQSQLEVEKNEEVWKRFTDILTSFHHIFGQEKLRLSDCLALIKTGMKSAQYRVVPATLDVVTIKSYDLVQPHSKPFVYAIGLTQSHFPKQIHHSGLLSDQERARINEIRNYRHFDIASAENSKKNHQTALSLFNAATKELVLSVPTVINETFDDLSPYLKELINFGLPLLDKGKNYLSYDNSDIGNYKALLSQIIAINRQDLIEMSDQDKMFWTVVLRYLRKQLRKQQLELPTSDYRLSTKPLSKEVIEVCFPKGIPLKLSATALTVFYNNQYNYFLKYVLNLNKTESIHPDSRIHGQYLHRVFERLMKDHTQEPFDNKLKQAIYHTNQESFFQQVYQDNAEAEYSLAILEDIVRSTAPTLQLNQNIKVIDQEKNFHLDMGNEILVHGIIDRIDQLSDGSLGVVDYKSSANQFDIGTFYNGLSPQLVTYLAALKQIAPHDINQLFGAMYLHLQDPKLDLVTFKQIDNTLVESIYKALTYKGIFSEVEKEHLSTGAYQTKNALYSNDELETLLNYNKYLYLKAAKHIKKGHFLINPYTSDGKTVQGDQLKAITRFEADLDMAQARRLVTLPAKEKKECFLTLMRKESHL
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The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. This subunit has 5' -> 3' nuclease activity. ATP + H2O = ADP + H(+) + phosphate Heterodimer of AddA and RexB. Belongs to the helicase family. AddB/RexB type 2 subfamily.
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B1IBR5
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MKLLYTDIRTSLTEILTREAEELVAAGKRVFYIAPNSLSFEKERAVLEYLSQQASFSITVTRFAQMARYLVLNDLPAKTTLDDIGLGLAFYKCLAELDPKDLRVYGAIKQDPQLIQQLIELYHEMTKSQMSFLDLENLTDEDKRADLLLIFEKVTAYLNQGQLAQGSQLSHLIEAIENDKVSSDFNQIALVIDGFTRFSAEEERVVDLLHGKGVEIVIGAYASKKAYTSPFSEGNLYQASVKFLHHLASKYQTPAQDCSQTHEKMDSFDKASRLLESSYDFSELALDVDEKDRENLQIWSCLTQKEELELVARSIRQKLHENSDLSYKHFRILLGDVASYQLSLKTIFDQYQIPFYLGRSEAMAHHPLTQFVESILALKRYRFRQEDLINLLRTDLYTDLSQSDIDAFEQYIRYLGINGLPAFQQTFTKSHHGKFNLERLNVLRLRILAPLETLFASRKQKAENLLQKWSVFLKEGAVTKQLQDLTTTLEAVEQERQTEVWKAFCHVLEQFATVFAGSQVSLEDFLALLHSGMSLSQYRTIPATVDTVLVQSYDLIAPLTADFVYAIGLTQDNLPKISQNTSLLTDEERQNLNQTTEEGVQLLIASSENLKKNRYTMLSLVNSARKQLFLSAPSLFNESESKESAYLQELIHFGFRRREKRMNHKGLSKEDMGSYHSLLSSLVAYHQQGEMSDTEQDLTFVKVLSRVIGKKLDLQGLENPAIPTSPSSKTLTKDTLQALYPAKQEFYLSTSGLTEFYLNEYSYFLRYVLGLQEELRLRPDARSHGNFLHRIFERALQLPNEDSFDQRLEQAIQETSQEREFEAIYQESLEAQFTKEVLLDVARTTGHILRHNPAIETIKEEANFGGKDQAFIQLDNGRSVFVRGKVDRIDRLKANGAIGVVDYKSSLTQFQFPHFFNGLNSQLPTYLAALKREGEQNFFGAMYLEMAEPVQSLMAVKSLAGAVVEASKSMKYQGLFLEKESSYLGEFYNKNKANQLTDEEFQLLLDYNAYLYKKAAEKILAGRFAINPYTENGRSIAPYVQQHQAITGFEANYHLGQARFLEKLDLADGKRLVGEKLKQAWLEKIREELNR
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The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. This subunit has 5' -> 3' nuclease activity. ATP + H2O = ADP + H(+) + phosphate Heterodimer of AddA and RexB. Belongs to the helicase family. AddB/RexB type 2 subfamily.
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B8ZQ31
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MKLLYTDIRTSLTEILTREAEELVAAGKRVFYIAPNSLSFEKERAVLECLSQQASFSITVTRFAQMARYLVLNDLPAKTTLDDIGLGLAFYKCLAELDPKDLRVYGAIKQDPQLIQQLIELYHEMTKSQMSFLDLENLTDEDKRADLLLIFEKVTAYLNQGQLAQGSQLSHLIEAIENDKVSSDFNQITLVIDGFTRFSAEEERVVDLLHGKGVEIVIGAYASKKAYTSPFSEGNLYQASVKFLHHLASKYQTPAQDCSQTHEKMDSFDKASRLLESSYDFSELALDVDEKDRENLQIWSCLTQKEELELVARSIRQKLHENSDLSYKHFRILLGDVASYQLSLKTIFDQYQIPFYLGRSEAMAHHPLTQFVESILALKRYRFRQEDLINLLRTDLYTDLSQSDIDAFEQYIRYLGINGLPAFQQIFTKSHHGKFNLERLNVLRLRILAPLETLFASRKQKAENLLQKWSVFLKEGAVTKQLQDLTTTLEAVEQERQAEVWKAFCHVLEQFATVFAGSQVSLEDFLALLHSGMSLSQYRTIPATVDTVLVQSYDLIAPLTADFVYAIGLTQDNLPKISQNTSLLTDEERQNLNQATEEGVQLLIASSENLKKNRYTMLSLVNSARKQLFLSAPSLFNESESKESAYLQELIHFGFRRREKRMNHKGLSKEDMGSYHSLLSSLVAYHQQGEMSDTEQDLTFVKVLSRVIGKKLDLQGLENPAIPTSPSSKTLAKDTLQALYPAKQEFYLSTSGLTEFYRNEYSYFLRYVLGLQEELRLRPDARSHGNFLHRIFERALQLPNEDSFDQRLEQAIQETSQEREFEAIYQESLEAQFTKEVLLDVARTTGHILRHNPAIETIKEEANFGGKDQAFIQLDNGRSVFVRGKVDRIDRLKANGAIGVVDYKSSLTQFQFPHFFNGLNSQLPTYLAALKREGKQNFFGAMYLEMAEPVQSLMAVKSLAGAVVEASKSMKYQGLFLEKESSYLGEFYNKNKANQLTDEEFQLLLDYNAYLYKKAAEKILAGRFAINPYTENGRSIAPYVQQHQAITGFEANYHLGQARFLKKLDLADGKRLVGEKLKQAWFEKIREELNR
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The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. This subunit has 5' -> 3' nuclease activity. ATP + H2O = ADP + H(+) + phosphate Heterodimer of AddA and RexB. Belongs to the helicase family. AddB/RexB type 2 subfamily.
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