ADCY7
entrez
113
canonical
uniprot
P51828
canonical
ensembl
ENSG00000121281
resolver
ensp
ENSP00000254235
resolver
ensp
ENSP00000378187
resolver
ensp
ENSP00000457409
resolver
ensp
ENSP00000501053
resolver
ensp
ENSP00000653923
resolver
ensp
ENSP00000653924
resolver
ensp
ENSP00000700875
resolver
ensp
ENSP00000700877
resolver
enst
ENST00000254235
resolver
enst
ENST00000394697
resolver
enst
ENST00000566433
resolver
enst
ENST00000673801
resolver
genesymbol
ADCY7
resolver
genesymbol_syn
KIAA0037
resolver
hgnc
HGNC:238
resolver
uniprot
A0AVA6
resolver
uniprot
B3KSJ0
resolver
uniprot
F5H4D1
resolver
uniprot
Q86YI0
resolver
uniprot_entry
ADCY7_HUMAN
resolver
uniprot_entry
B3KSJ0_HUMAN
resolver
uniprot_entry
F5H4D1_HUMAN
resolver
uniprot_entry
Q86YI0_HUMAN
resolver
uniprot_sec
A0AVA6
resolver
activity_regulation
ACTIVITY REGULATION: Activated by G(s) G alpha protein (GNAS) (PubMed:18541530). Inhibited by G(i) G alpha protein GNAI1 (Probable). Activated by GNA13 and GNA12 (PubMed:18541530, PubMed:23229509). 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). Activated by TLR9, promoting synthesis of cyclic di-AMP (c-di-AMP) (By similarity). {ECO:0000250|UniProtKB:P51829, ECO:0000269|PubMed:12454008, ECO:0000269|PubMed:18541530, ECO:0000269|PubMed:23229509, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRASVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRSEDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACASLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISERVETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLPYYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKPNGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
uniprot
proteins
ec_number
2.7.7.85
uniprot
proteins
ec_number
4.6.1.1
uniprot
proteins
function
FUNCTION: Adenylate cyclase that mediates formation of both cyclic AMP (cAMP) and cyclic di-AMP (c-di-AMP) (PubMed:11113152, PubMed:18541530, PubMed:23229509). Acts as a key mediator of G protein-coupled receptor signaling by catalyzing the formation of cAMP downstream of G protein-coupled receptors (PubMed:18541530, PubMed:23229509). Functions in G protein-coupled receptor signaling cascades activated by thrombin, sphingosine 1-phosphate, dopamine and anaphylatoxin C5a (PubMed:18541530, PubMed:23229509, PubMed:23842570). Mediates regulation of cAMP synthesis through synergistic action of the G alpha protein G(s) (GNAS) with G(13) (GNA13) (PubMed:18541530, PubMed:23229509). Also involved in inflammation by acting as a diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into c-di-AMP (By similarity). Following activation by TLR9, mediates formation of c-di-AMP, which directly activates NLRP3, thereby promoting assembly and maturation of the NLRP3 inflammasome (By similarity). 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). {ECO:0000250|UniProtKB:P51829, ECO:0000269|PubMed:11113152, ECO:0000269|PubMed:18541530, ECO:0000269|PubMed:23229509, ECO:0000269|PubMed:23842570}.
uniprot
proteins
mass_dalton
120308
uniprot
proteins
mutagenesis
MUTAGEN 477..482; /note="KMRASV->NAAIRS: Does not affect cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation. Reduces by 40% cAMP biosynthetic process in response to C5 alpha chain stimulation."; /evidence="ECO:0000269|PubMed:23229509"; MUTAGEN 485..489; /note="TRYLE->NAAIR: Reduces cAMP biosynthetic process in response to C5 alpha chain stimulation and more severely in response to sphingosine 1-phosphate stimulation."; /evidence="ECO:0000269|PubMed:23229509"; MUTAGEN 491..496; /note="WGAARP->NAAIRS: Does not affect cAMP biosynthetic process in response to C5 alpha chain stimulation. Reduces by 40?60% cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation."; /evidence="ECO:0000269|PubMed:23229509"; MUTAGEN 494..499; /note="ARPFAH->NAAIRS: Does not affect cAMP biosynthetic process in response to C5 alpha chain stimulation. Reduces by 40?60% cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation."; /evidence="ECO:0000269|PubMed:23229509"; MUTAGEN 564..569; /note="SKSDDF->NAAIRS: Reduces cAMP biosynthetic process in response to C5 alpha chain stimulation and more severely in response to sphingosine 1-phosphate stimulation."; /evidence="ECO:0000269|PubMed:23229509
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PRKCD. {ECO:0000269|PubMed:12454008}.
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
11113152
uniprot
proteins
pubmed
12454008
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15581358
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
18541530
uniprot
proteins
pubmed
23229509
uniprot
proteins
pubmed
23842570
uniprot
proteins
pubmed
7584026
uniprot
proteins
sequence_length
1080
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 34..54; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 63..83; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 95..117; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 122..142; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 147..167; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 176..196; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 595..615; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 620..640; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 669..688; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 718..737; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 746..773; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 794..814; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins