ADCY6
entrez
112
canonical
uniprot
O43306
canonical
ensembl
ENSG00000174233
resolver
ensp
ENSP00000311405
resolver
ensp
ENSP00000350536
resolver
ensp
ENSP00000446730
resolver
ensp
ENSP00000543954
resolver
ensp
ENSP00000581346
resolver
ensp
ENSP00000630756
resolver
ensp
ENSP00000630767
resolver
ensp
ENSP00000630768
resolver
genesymbol
ADCY6
resolver
genesymbol_syn
KIAA0422
resolver
hgnc
HGNC:237
resolver
uniprot
Q9NR75
resolver
uniprot
Q9UDB0
resolver
uniprot_entry
ADCY6_HUMAN
resolver
uniprot_sec
Q9NR75
resolver
uniprot_sec
Q9UDB0
resolver
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 (PubMed:17110384). Activated by forskolin (PubMed:17110384, PubMed:17916776). 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 (By similarity). {ECO:0000250|UniProtKB:P30804, ECO:0000250|UniProtKB:Q01341, ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776}.
uniprot
proteins
amino_acid_sequence
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGPPRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWRRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAYVALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLWCPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTNVIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSCGSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLTPADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLAMIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
uniprot
proteins
disease_involvement
DISEASE: Lethal congenital contracture syndrome 8 (LCCS8) [MIM:616287]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS8 is an axoglial form of arthrogryposis multiplex congenita, characterized by congenital distal joint contractures, reduced fetal movements, and severe motor paralysis leading to death early in the neonatal period. {ECO:0000269|PubMed:24319099}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:17110384, PubMed:17916776). 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). {ECO:0000250|UniProtKB:Q01341, ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776}.
uniprot
proteins
mass_dalton
130615
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:Q03343}.
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
10978539
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15385642
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17110384
uniprot
proteins
pubmed
17916776
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24319099
uniprot
proteins
pubmed
8476432
uniprot
proteins
pubmed
9455477
uniprot
proteins
sequence_length
1168
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17110384}; 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 152..168; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 181..197; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 214..230; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 239..255; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 259..275; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 289..305; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 674..691; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 702..718; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 743..759; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 820..836; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 839..855; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 897..913; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins