{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q01341","uniProtkbId":"ADCY6_MOUSE","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-04-01","entryVersion":194,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Adenylate cyclase type 6"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1379717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23753526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24363043"}],"value":"4.6.1.1"}]},"alternativeNames":[{"fullName":{"value":"ATP pyrophosphate-lyase 6"}},{"fullName":{"value":"Adenylate cyclase type VI"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20466003"}],"value":"Adenylyl cyclase 6"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20466003"}],"value":"AC6"}]},{"fullName":{"value":"Ca(2+)-inhibitable adenylyl cyclase"}}]},"genes":[{"geneName":{"value":"Adcy6"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O43306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1379717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20359598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20371630"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23753526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24277577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24363043"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24854272"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP = 3',5'-cyclic AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15389"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58165"}],"ecNumber":"4.6.1.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1379717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23753526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24363043"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24854272"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O43306"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O43306"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30803"}],"value":"Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30804"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03343"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1379717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23753526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24363043"}],"value":"Activated by G(s) G alpha protein GNAS (By similarity). Inhibited by G(i) G alpha protein GNAI1 (By similarity). Is further activated by the complex formed by GNB1 and GNG2 (By similarity). 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). Phosphorylation by RAF1 results in its activation (By similarity)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O43306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21670265"}],"value":"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)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1379717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21670265"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21670265"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20371630"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21670265"}],"value":"Cell projection, cilium","id":"SL-0066"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17567809"}],"value":"Cell projection, stereocilium","id":"SL-0302"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1379717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17567809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23753526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24277577"}],"value":"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)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17567809"}],"value":"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"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26769"}],"value":"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"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03343"}],"value":"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"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18071070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20359598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20466003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23753526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24158982"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24277577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24854272"}],"value":"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)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00099"}],"value":"Belongs to the adenylyl cyclase class-4/guanylyl cyclase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1165,"modifier":"EXACT"}},"description":"Adenylate cyclase type 6","featureId":"PRO_0000195700"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":688,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":699,"modifier":"EXACT"},"end":{"value":715,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":740,"modifier":"EXACT"},"end":{"value":756,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":757,"modifier":"EXACT"},"end":{"value":816,"modifier":"EXACT"}},"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":817,"modifier":"EXACT"},"end":{"value":833,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":852,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":894,"modifier":"EXACT"},"end":{"value":910,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":911,"modifier":"EXACT"},"end":{"value":1165,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30803"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00099"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00099"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00099"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30803"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00099"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00099"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30803"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1028,"modifier":"EXACT"},"end":{"value":1028,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26769"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1102,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26769"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1109,"modifier":"EXACT"},"end":{"value":1113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26769"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1149,"modifier":"EXACT"},"end":{"value":1149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26769"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O43306"}]},{"type":"Modified residue","location":{"start":{"value":553,"modifier":"EXACT"},"end":{"value":553,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03343"}]},{"type":"Modified residue","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21183079"}]},{"type":"Modified residue","location":{"start":{"value":659,"modifier":"EXACT"},"end":{"value":659,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03343"}]},{"type":"Modified residue","location":{"start":{"value":916,"modifier":"EXACT"},"end":{"value":916,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q03343"}]},{"type":"Glycosylation","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":790,"modifier":"EXACT"},"end":{"value":790,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":875,"modifier":"EXACT"},"end":{"value":875,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Sequence conflict","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"in Ref. 2; AAA37182","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["N"]}},{"type":"Sequence conflict","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"in Ref. 2; AAA37182","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"in Ref. 2; AAA37182","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"GR","alternativeSequences":["RAG"]}},{"type":"Sequence conflict","location":{"start":{"value":737,"modifier":"EXACT"},"end":{"value":737,"modifier":"EXACT"}},"description":"in Ref. 2; AAA37182","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["G"]}},{"type":"Sequence conflict","location":{"start":{"value":881,"modifier":"EXACT"},"end":{"value":881,"modifier":"EXACT"}},"description":"in Ref. 2; AAA37182","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["Q"]}},{"type":"Sequence conflict","location":{"start":{"value":990,"modifier":"EXACT"},"end":{"value":990,"modifier":"EXACT"}},"description":"in Ref. 2; AAA37182","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["M"]}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0115","category":"Biological process","name":"cAMP biosynthesis"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0966","category":"Cellular component","name":"Cell projection"},{"id":"KW-0969","category":"Cellular component","name":"Cilium"},{"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0677","category":"Domain","name":"Repeat"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"1379717","citationType":"journal article","authors":["Yoshimura M.","Cooper D.M.F."],"citationCrossReferences":[{"database":"PubMed","id":"1379717"},{"database":"DOI","id":"10.1073/pnas.89.15.6716"}],"title":"Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells.","publicationDate":"1992","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"6716","lastPage":"6720","volume":"89"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","CATALYTIC ACTIVITY","FUNCTION","ACTIVITY REGULATION","SUBCELLULAR LOCATION","TISSUE SPECIFICITY"]},{"referenceNumber":2,"citation":{"id":"1332848","citationType":"journal article","authors":["Premont R.T.","Jacobowitz O.","Iyengar R."],"citationCrossReferences":[{"database":"PubMed","id":"1332848"},{"database":"DOI","id":"10.1210/endo.131.6.1332848"}],"title":"Lowered responsiveness of the catalyst of adenylyl cyclase to stimulation by GS in heterologous desensitization: a role for adenosine 3',5'-monophosphate-dependent phosphorylation.","publicationDate":"1992","journal":"Endocrinology","firstPage":"2774","lastPage":"2784","volume":"131"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA] OF 10-1165"]},{"referenceNumber":3,"citation":{"id":"17567809","citationType":"journal article","authors":["Michalski N.","Michel V.","Bahloul A.","Lefevre G.","Barral J.","Yagi H.","Chardenoux S.","Weil D.","Martin P.","Hardelin J.P.","Sato M.","Petit C."],"citationCrossReferences":[{"database":"PubMed","id":"17567809"},{"database":"DOI","id":"10.1523/jneurosci.0342-07.2007"}],"title":"Molecular characterization of the ankle-link complex in cochlear hair cells and its role in the hair bundle functioning.","publicationDate":"2007","journal":"J. Neurosci.","firstPage":"6478","lastPage":"6488","volume":"27"},"referencePositions":["TISSUE SPECIFICITY","SUBCELLULAR LOCATION","DEVELOPMENTAL STAGE"]},{"referenceNumber":4,"citation":{"id":"18071070","citationType":"journal article","authors":["Tang T.","Gao M.H.","Lai N.C.","Firth A.L.","Takahashi T.","Guo T.","Yuan J.X.","Roth D.M.","Hammond H.K."],"citationCrossReferences":[{"database":"PubMed","id":"18071070"},{"database":"DOI","id":"10.1161/circulationaha.107.730069"}],"title":"Adenylyl cyclase type 6 deletion decreases left ventricular function via impaired calcium handling.","publicationDate":"2008","journal":"Circulation","firstPage":"61","lastPage":"69","volume":"117"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","ACTIVITY REGULATION","CATALYTIC ACTIVITY","TISSUE SPECIFICITY"]},{"referenceNumber":5,"citation":{"id":"21183079","citationType":"journal article","authors":["Huttlin E.L.","Jedrychowski M.P.","Elias J.E.","Goswami T.","Rad R.","Beausoleil S.A.","Villen J.","Haas W.","Sowa M.E.","Gygi S.P."],"citationCrossReferences":[{"database":"PubMed","id":"21183079"},{"database":"DOI","id":"10.1016/j.cell.2010.12.001"}],"title":"A tissue-specific atlas of mouse protein phosphorylation and expression.","publicationDate":"2010","journal":"Cell","firstPage":"1174","lastPage":"1189","volume":"143"},"referencePositions":["PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573","IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]"],"referenceComments":[{"value":"Brain","type":"TISSUE"},{"value":"Brown adipose tissue","type":"TISSUE"},{"value":"Heart","type":"TISSUE"},{"value":"Kidney","type":"TISSUE"},{"value":"Pancreas","type":"TISSUE"}]},{"referenceNumber":6,"citation":{"id":"20371630","citationType":"journal article","authors":["Kwon R.Y.","Temiyasathit S.","Tummala P.","Quah C.C.","Jacobs C.R."],"citationCrossReferences":[{"database":"PubMed","id":"20371630"},{"database":"DOI","id":"10.1096/fj.09-148007"}],"title":"Primary cilium-dependent mechanosensing is mediated by adenylyl cyclase 6 and cyclic AMP in bone cells.","publicationDate":"2010","journal":"FASEB J.","firstPage":"2859","lastPage":"2868","volume":"24"},"referencePositions":["SUBCELLULAR LOCATION","FUNCTION"]},{"referenceNumber":7,"citation":{"id":"20466003","citationType":"journal article","authors":["Chien C.L.","Wu Y.S.","Lai H.L.","Chen Y.H.","Jiang S.T.","Shih C.M.","Lin S.S.","Chang C.","Chern Y."],"citationCrossReferences":[{"database":"PubMed","id":"20466003"},{"database":"DOI","id":"10.1016/j.febslet.2010.05.004"}],"title":"Impaired water reabsorption in mice deficient in the type VI adenylyl cyclase (AC6).","publicationDate":"2010","journal":"FEBS Lett.","firstPage":"2883","lastPage":"2890","volume":"584"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","SUBCELLULAR LOCATION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","TISSUE SPECIFICITY"]},{"referenceNumber":8,"citation":{"id":"20359598","citationType":"journal article","authors":["Tang T.","Lai N.C.","Hammond H.K.","Roth D.M.","Yang Y.","Guo T.","Gao M.H."],"citationCrossReferences":[{"database":"PubMed","id":"20359598"},{"database":"DOI","id":"10.1016/j.jacc.2009.11.066"}],"title":"Adenylyl cyclase 6 deletion reduces left ventricular hypertrophy, dilation, dysfunction, and fibrosis in pressure-overloaded female mice.","publicationDate":"2010","journal":"J. Am. Coll. Cardiol.","firstPage":"1476","lastPage":"1486","volume":"55"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION"]},{"referenceNumber":9,"citation":{"id":"20864687","citationType":"journal article","authors":["Rieg T.","Tang T.","Murray F.","Schroth J.","Insel P.A.","Fenton R.A.","Hammond H.K.","Vallon V."],"citationCrossReferences":[{"database":"PubMed","id":"20864687"},{"database":"DOI","id":"10.1681/asn.2010040409"}],"title":"Adenylate cyclase 6 determines cAMP formation and aquaporin-2 phosphorylation and trafficking in inner medulla.","publicationDate":"2010","journal":"J. Am. Soc. Nephrol.","firstPage":"2059","lastPage":"2068","volume":"21"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION"]},{"referenceNumber":10,"citation":{"id":"21670265","citationType":"journal article","authors":["Choi Y.H.","Suzuki A.","Hajarnis S.","Ma Z.","Chapin H.C.","Caplan M.J.","Pontoglio M.","Somlo S.","Igarashi P."],"citationCrossReferences":[{"database":"PubMed","id":"21670265"},{"database":"DOI","id":"10.1073/pnas.1016214108"}],"title":"Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases.","publicationDate":"2011","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"10679","lastPage":"10684","volume":"108"},"referencePositions":["SUBCELLULAR LOCATION","INTERACTION WITH AKAP5; ADCY5; PDE4C AND PKD2"]},{"referenceNumber":11,"citation":{"id":"23753526","citationType":"journal article","authors":["Sabbatini M.E.","D'Alecy L.","Lentz S.I.","Tang T.","Williams J.A."],"citationCrossReferences":[{"database":"PubMed","id":"23753526"},{"database":"DOI","id":"10.1113/jphysiol.2012.249698"}],"title":"Adenylyl cyclase 6 mediates the action of cyclic AMP-dependent secretagogues in mouse pancreatic exocrine cells via protein kinase A pathway activation.","publicationDate":"2013","journal":"J. Physiol. (Lond.)","firstPage":"3693","lastPage":"3707","volume":"591"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","TISSUE SPECIFICITY"]},{"referenceNumber":12,"citation":{"id":"24277577","citationType":"journal article","authors":["Lee K.L.","Hoey D.A.","Spasic M.","Tang T.","Hammond H.K.","Jacobs C.R."],"citationCrossReferences":[{"database":"PubMed","id":"24277577"},{"database":"DOI","id":"10.1096/fj.13-240432"}],"title":"Adenylyl cyclase 6 mediates loading-induced bone adaptation in vivo.","publicationDate":"2014","journal":"FASEB J.","firstPage":"1157","lastPage":"1165","volume":"28"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","TISSUE SPECIFICITY"]},{"referenceNumber":13,"citation":{"id":"24158982","citationType":"journal article","authors":["Rees S.","Kittikulsuth W.","Roos K.","Strait K.A.","Van Hoek A.","Kohan D.E."],"citationCrossReferences":[{"database":"PubMed","id":"24158982"},{"database":"DOI","id":"10.1681/asn.2013010077"}],"title":"Adenylyl cyclase 6 deficiency ameliorates polycystic kidney disease.","publicationDate":"2014","journal":"J. Am. Soc. Nephrol.","firstPage":"232","lastPage":"237","volume":"25"},"referencePositions":["DISRUPTION PHENOTYPE"]},{"referenceNumber":14,"citation":{"id":"24854272","citationType":"journal article","authors":["Fenton R.A.","Murray F.","Dominguez Rieg J.A.","Tang T.","Levi M.","Rieg T."],"citationCrossReferences":[{"database":"PubMed","id":"24854272"},{"database":"DOI","id":"10.1681/asn.2013101102"}],"title":"Renal phosphate wasting in the absence of adenylyl cyclase 6.","publicationDate":"2014","journal":"J. Am. Soc. Nephrol.","firstPage":"2822","lastPage":"2834","volume":"25"},"referencePositions":["DISRUPTION PHENOTYPE","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION"]},{"referenceNumber":15,"citation":{"id":"24363043","citationType":"journal article","authors":["Bogard A.S.","Birg A.V.","Ostrom R.S."],"citationCrossReferences":[{"database":"PubMed","id":"24363043"},{"database":"DOI","id":"10.1007/s00210-013-0950-4"}],"title":"Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that selectively regulates IL-6 expression in airway smooth muscle cells: differential regulation of gene expression by AC isoforms.","publicationDate":"2014","journal":"Naunyn Schmiedebergs Arch. Pharmacol.","firstPage":"329","lastPage":"339","volume":"387"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M93422","properties":[{"key":"ProteinId","value":"AAA37174.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"M96653","properties":[{"key":"ProteinId","value":"AAA37182.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"PIR","id":"A49201","properties":[{"key":"EntryName","value":"A49201"}]},{"database":"AlphaFoldDB","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"197975","properties":[{"key":"Interactions","value":"1"}]},{"database":"CORUM","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"Q01341","properties":[{"key":"Number of interactors","value":"1114"}]},{"database":"STRING","id":"10090.ENSMUSP00000093939","properties":[{"key":"Description","value":"-"}]},{"database":"GlyCosmos","id":"Q01341","properties":[{"key":"glycosylation","value":"3 sites, No reported glycans"}]},{"database":"GlyGen","id":"Q01341","properties":[{"key":"glycosylation","value":"5 sites, 1 N-linked glycan (1 site)"}]},{"database":"iPTMnet","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"PhosphoSitePlus","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"SwissPalm","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"10090-ENSMUSP00000093939","properties":[{"key":"Description","value":"-"}]},{"database":"ProteomicsDB","id":"285724","properties":[{"key":"Description","value":"-"}]},{"database":"Pumba","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"DNASU","id":"11512","properties":[{"key":"Description","value":"-"}]},{"database":"AGR","id":"MGI:87917","properties":[{"key":"Description","value":"-"}]},{"database":"MGI","id":"MGI:87917","properties":[{"key":"GeneName","value":"Adcy6"}]},{"database":"eggNOG","id":"KOG3619","properties":[{"key":"ToxonomicScope","value":"Eukaryota"}]},{"database":"InParanoid","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.6.1.1","properties":[{"key":"OrganismId","value":"3474"}]},{"database":"Reactome","id":"R-MMU-163615","properties":[{"key":"PathwayName","value":"PKA activation"}]},{"database":"Reactome","id":"R-MMU-170660","properties":[{"key":"PathwayName","value":"Adenylate cyclase activating pathway"}]},{"database":"Reactome","id":"R-MMU-170670","properties":[{"key":"PathwayName","value":"Adenylate cyclase inhibitory pathway"}]},{"database":"Reactome","id":"R-MMU-400042","properties":[{"key":"PathwayName","value":"Adrenaline,noradrenaline inhibits insulin secretion"}]},{"database":"Reactome","id":"R-MMU-418597","properties":[{"key":"PathwayName","value":"G alpha (z) signalling events"}]},{"database":"Reactome","id":"R-MMU-5610787","properties":[{"key":"PathwayName","value":"Hedgehog 'off' state"}]},{"database":"BioGRID-ORCS","id":"11512","properties":[{"key":"hits","value":"7 hits in 76 CRISPR screens"}]},{"database":"PRO","id":"PR:Q01341","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000589","properties":[{"key":"Component","value":"Unplaced"}]},{"database":"RNAct","id":"Q01341","properties":[{"key":"moleculeType","value":"protein"}]},{"database":"GO","id":"GO:0005929","properties":[{"key":"GoTerm","value":"C:cilium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005768","properties":[{"key":"GoTerm","value":"C:endosome"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"ISS:BHF-UCL"}]},{"database":"GO","id":"GO:0031528","properties":[{"key":"GoTerm","value":"C:microvillus membrane"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20466003"}]},{"database":"GO","id":"GO:0042383","properties":[{"key":"GoTerm","value":"C:sarcolemma"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0032420","properties":[{"key":"GoTerm","value":"C:stereocilium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004016","properties":[{"key":"GoTerm","value":"F:adenylate cyclase activity"},{"key":"GoEvidenceType","value":"IDA:MGI"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17593019"}]},{"database":"GO","id":"GO:0008294","properties":[{"key":"GoTerm","value":"F:calcium- and calmodulin-responsive adenylate cyclase activity"},{"key":"GoEvidenceType","value":"IDA:MGI"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"1379717"}]},{"database":"GO","id":"GO:0019901","properties":[{"key":"GoTerm","value":"F:protein kinase binding"},{"key":"GoEvidenceType","value":"ISS:BHF-UCL"}]},{"database":"GO","id":"GO:0005080","properties":[{"key":"GoTerm","value":"F:protein kinase C binding"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0097110","properties":[{"key":"GoTerm","value":"F:scaffold protein binding"},{"key":"GoEvidenceType","value":"IPI:MGI"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"20164376"}]},{"database":"GO","id":"GO:0005102","properties":[{"key":"GoTerm","value":"F:signaling receptor binding"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0000149","properties":[{"key":"GoTerm","value":"F:SNARE binding"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0007191","properties":[{"key":"GoTerm","value":"P:adenylate cyclase-activating dopamine receptor signaling pathway"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0007189","properties":[{"key":"GoTerm","value":"P:adenylate cyclase-activating G protein-coupled receptor signaling pathway"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"20466003"}]},{"database":"GO","id":"GO:0007192","properties":[{"key":"GoTerm","value":"P:adenylate cyclase-activating serotonin receptor signaling pathway"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0097746","properties":[{"key":"GoTerm","value":"P:blood vessel diameter maintenance"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0006171","properties":[{"key":"GoTerm","value":"P:cAMP biosynthetic process"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"20466003"}]},{"database":"GO","id":"GO:0071870","properties":[{"key":"GoTerm","value":"P:cellular response to catecholamine stimulus"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:1904322","properties":[{"key":"GoTerm","value":"P:cellular response to forskolin"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"20466003"}]},{"database":"GO","id":"GO:0071380","properties":[{"key":"GoTerm","value":"P:cellular response to prostaglandin E stimulus"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:1904117","properties":[{"key":"GoTerm","value":"P:cellular response to vasopressin"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"20466003"}]},{"database":"GO","id":"GO:0035556","properties":[{"key":"GoTerm","value":"P:intracellular signal transduction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0072660","properties":[{"key":"GoTerm","value":"P:maintenance of protein location in plasma membrane"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0010977","properties":[{"key":"GoTerm","value":"P:negative regulation of neuron projection development"},{"key":"GoEvidenceType","value":"IMP:ParkinsonsUK-UCL"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"21986494"}]},{"database":"GO","id":"GO:0035811","properties":[{"key":"GoTerm","value":"P:negative regulation of urine volume"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"20466003"}]},{"database":"GO","id":"GO:0003091","properties":[{"key":"GoTerm","value":"P:renal water homeostasis"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"20466003"}]},{"database":"CDD","id":"cd07302","properties":[{"key":"EntryName","value":"CHD"},{"key":"MatchStatus","value":"2"}]},{"database":"FunFam","id":"3.30.70.1230:FF:000001","properties":[{"key":"EntryName","value":"Adenylate cyclase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.1230:FF:000002","properties":[{"key":"EntryName","value":"Adenylate cyclase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.1230","properties":[{"key":"EntryName","value":"Nucleotide cyclase"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR001054","properties":[{"key":"EntryName","value":"A/G_cyclase"}]},{"database":"InterPro","id":"IPR018297","properties":[{"key":"EntryName","value":"A/G_cyclase_CS"}]},{"database":"InterPro","id":"IPR032628","properties":[{"key":"EntryName","value":"AC_N"}]},{"database":"InterPro","id":"IPR030672","properties":[{"key":"EntryName","value":"Adcy"}]},{"database":"InterPro","id":"IPR009398","properties":[{"key":"EntryName","value":"Adcy_conserved_dom"}]},{"database":"InterPro","id":"IPR029787","properties":[{"key":"EntryName","value":"Nucleotide_cyclase"}]},{"database":"PANTHER","id":"PTHR45627","properties":[{"key":"EntryName","value":"ADENYLATE CYCLASE TYPE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45627:SF11","properties":[{"key":"EntryName","value":"ADENYLATE CYCLASE TYPE 6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16214","properties":[{"key":"EntryName","value":"AC_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06327","properties":[{"key":"EntryName","value":"Adcy_cons_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00211","properties":[{"key":"EntryName","value":"Guanylate_cyc"},{"key":"MatchStatus","value":"2"}]},{"database":"PIRSF","id":"PIRSF039050","properties":[{"key":"EntryName","value":"Ade_cyc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00044","properties":[{"key":"EntryName","value":"CYCc"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55073","properties":[{"key":"EntryName","value":"Nucleotide cyclase"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00452","properties":[{"key":"EntryName","value":"GUANYLATE_CYCLASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50125","properties":[{"key":"EntryName","value":"GUANYLATE_CYCLASE_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSWFSGLLVPKVDERKTAWGERNGQKRPRHANRASGFCAPRYMSCLKNAEPPSPTPAAHTRCPWQDEAFIRRAGPGRGVELGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGPSCWHRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPAQPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQLGANVVLFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGGRRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQCIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLVFPYSTLILGIYAAIFLLLLVTVLICAVCSCGSFFPKALQRLSRNIVRSRVHSTAVGIFSVLLVFISAIANMFTCNHTPIRTCAARMLNLTPADVTACHLQQLNYSLGLDAPLCEGTAPTCSFPEYFVGNVLLSLLASSVFLHISSIGKLAMTFILGFTYLVLLLLGPPAAIFDNYDLLLGVHGLASSNETFDGLDCPAVGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS","length":1165,"molWeight":130319,"crc64":"24EE1BB45DF1E87E","md5":"5EBD5600F7294BEEA4F49ABFBE6E5A4E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"TISSUE SPECIFICITY":1,"DEVELOPMENTAL STAGE":1,"DOMAIN":1,"PTM":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Topological domain":4,"Transmembrane":12,"Binding site":12,"Modified residue":5,"Glycosylation":3,"Sequence conflict":6},"uniParcId":"UPI0000028950"}}