Q01341
uniprot
Q01341
canonical
activity_regulation
ACTIVITY REGULATION: 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). {ECO:0000250|UniProtKB:P30804, ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687, ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24363043}.
uniprot
proteins
amino_acid_sequence
MSWFSGLLVPKVDERKTAWGERNGQKRPRHANRASGFCAPRYMSCLKNAEPPSPTPAAHTRCPWQDEAFIRRAGPGRGVELGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGPSCWHRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPAQPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQLGANVVLFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGGRRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQCIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLVFPYSTLILGIYAAIFLLLLVTVLICAVCSCGSFFPKALQRLSRNIVRSRVHSTAVGIFSVLLVFISAIANMFTCNHTPIRTCAARMLNLTPADVTACHLQQLNYSLGLDAPLCEGTAPTCSFPEYFVGNVLLSLLASSVFLHISSIGKLAMTFILGFTYLVLLLLGPPAAIFDNYDLLLGVHGLASSNETFDGLDCPAVGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
uniprot
proteins
ec_number
4.6.1.1
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:O43306, ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20359598, ECO:0000269|PubMed:20371630, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687, ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24277577, ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:24854272}.
uniprot
proteins
mass_dalton
130319
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:Q03343}.
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
1332848
uniprot
proteins
pubmed
1379717
uniprot
proteins
pubmed
17567809
uniprot
proteins
pubmed
18071070
uniprot
proteins
pubmed
20359598
uniprot
proteins
pubmed
20371630
uniprot
proteins
pubmed
20466003
uniprot
proteins
pubmed
20864687
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21670265
uniprot
proteins
pubmed
23753526
uniprot
proteins
pubmed
24158982
uniprot
proteins
pubmed
24277577
uniprot
proteins
pubmed
24363043
uniprot
proteins
pubmed
24854272
uniprot
proteins
sequence_length
1165
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:21670265}; Multi-pass membrane protein {ECO:0000269|PubMed:21670265}. Cell projection, cilium {ECO:0000269|PubMed:20371630, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:21670265}. Cell projection, stereocilium {ECO:0000269|PubMed:17567809}.
uniprot
proteins
transmembrane_region
TRANSMEM 150..166; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 179..195; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 212..228; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 237..253; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 257..273; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 287..303; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 671..688; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 699..715; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 740..756; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 817..833; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 836..852; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 894..910; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins