Adcy6
entrez
25289
canonical
uniprot
Q03343
canonical
ensembl
ENSRNOG00000054757
resolver
ensp
ENSRNOP00000072881
resolver
ensp
ENSRNOP00000078118
resolver
enst
ENSRNOT00000088323
resolver
genesymbol
Adcy6
resolver
uniprot
A0A0G2K429
resolver
uniprot_entry
A0A0G2K429_RAT
resolver
uniprot_entry
ADCY6_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated by G(s) G alpha protein GNAS (PubMed:17110384, PubMed:9391159). Inhibited by G(i) G alpha protein GNAI1 (By similarity). Is further activated by the complex formed by GNB1 and GNG2 (PubMed:17110384). Activated by forskolin (By similarity). Inhibited by calcium ions, already at micromolar concentrations (By similarity). Inhibited by adenosine, AMP and their analogs (By similarity). Phosphorylation by RAF1 results in its activation (PubMed:15385642). {ECO:0000250|UniProtKB:P30804, ECO:0000250|UniProtKB:Q01341, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:9391159}.
uniprot
proteins
amino_acid_sequence
MSWFSGLLVPKVDERKTAWGERNGQKRPRQATRARGFCAPRYMSCLKNVEPPSPTPAARTRCPWQDEAFIRRAGPGRGVKLGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGPSCWHRLAQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPALPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAANPRSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWHLNNGDPFLWKQLGANVVLFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNGYLKEQCIETFLILGASQKRKEEKAMLVKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKENRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQFLVFPHSALILGIYAGIFLLLLVTVLICAVCSCGSFFPNALQRLSRSIVRSRVHSTAVGVFSVLLVFISAIANMFTCSHTPLRTCAARMLNLTPSDVTACHLRQINYSLGLEAPLCEGTAPTCSFPEYFVGSVLLSLLASSVFLHISSIGKLVMTFVLGFIYLLLLLLGPPATIFDNYDLLLSVHGLASSNETFDGLDCPAVGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
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: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). {ECO:0000250|UniProtKB:O43306, ECO:0000250|UniProtKB:Q01341, ECO:0000269|PubMed:1409703, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:21606183}.
uniprot
proteins
mass_dalton
130506
uniprot
proteins
mutagenesis
MUTAGEN 311; /note="S->A: No effect on phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:11877398"; MUTAGEN 554; /note="S->A: Reduces phosphorylation by PKC and PKC-mediated inhibition."; /evidence="ECO:0000269|PubMed:11877398"; MUTAGEN 660; /note="S->A: Abolishes phosphorylation by PKA and PKA-mediated down-regulation of enzyme activity."; /evidence="ECO:0000269|PubMed:9391159"; MUTAGEN 660; /note="S->A: Reduces phosphorylation by PKC and PKC-mediated inhibition."; /evidence="ECO:0000269|PubMed:11877398"; MUTAGEN 917; /note="T->A: Reduces phosphorylation by PKC, abolishes PKC-mediated inhibition."; /evidence="ECO:0000269|PubMed:11877398
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000269|PubMed:11877398, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:9391159}.
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
11877398
uniprot
proteins
pubmed
1332969
uniprot
proteins
pubmed
1409703
uniprot
proteins
pubmed
15385642
uniprot
proteins
pubmed
17110384
uniprot
proteins
pubmed
21606183
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
9391159
uniprot
proteins
sequence_length
1166
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:9391159}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q01341}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q01341}.
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 672..689; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 700..716; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 741..757; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 818..834; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 837..853; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 895..911; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins