Adcy7
entrez
11513
canonical
uniprot
P51829
canonical
ensembl
ENSMUSG00000031659
resolver
ensp
ENSMUSP00000096122
resolver
ensp
ENSMUSP00000129252
resolver
ensp
ENSMUSP00000130594
resolver
ensp
ENSMUSP00000132528
resolver
enst
ENSMUST00000098521
resolver
enst
ENSMUST00000168545
resolver
enst
ENSMUST00000169037
resolver
enst
ENSMUST00000171456
resolver
genesymbol
Adcy7
resolver
uniprot
Q3U1P1
resolver
uniprot
Q3U1X9
resolver
uniprot
Q3U3P2
resolver
uniprot
Q3UU15
resolver
uniprot_entry
ADCY7_MOUSE
resolver
uniprot_entry
Q3U1P1_MOUSE
resolver
uniprot_entry
Q3U1X9_MOUSE
resolver
uniprot_entry
Q3UU15_MOUSE
resolver
uniprot_sec
Q3U3P2
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). Activated by GNA13 and GNA12 (By similarity). 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 (By similarity). Inhibited by lithium (PubMed:18205980). Activated by TLR9, promoting synthesis of cyclic di-AMP (c-di-AMP) (PubMed:40419769). {ECO:0000250|UniProtKB:P51828, ECO:0000269|PubMed:18205980, ECO:0000269|PubMed:40419769}.
uniprot
proteins
amino_acid_sequence
MPAKGRYFLNEGDEGPDQAALYEKYRLTSLHGPLLLLLLLVAAATCIALISIAFSHEDLRRHQVVLGTAFLMLTLFVALYVLVYVECLVQRWLRALALLTWACLMVLGSVLMWDSLENEAHAWEQVPFFLFVVFVVYALLPLSRRAAIVAGVTSTVSHLLVFGAVTRAFQTSMSSTQLGLQLLANAVILLGGNFTGAFHKHQLQDASRDLFIYTVKCIQIRRKLRVEKRQQENLLLSVLPAHISMGMKLAIIERLKEGGDRHYMPDNNFHSLYVKRHQNVSILYADIVGFTRLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDICEAIKQVREATGVDISMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLNHLDKAYEVEDGHGEQRDPYLKEMNIRTYLVIDPRSQQPPPPSHHLSKPKGDATLKMRASVRVTRYLESWGAARPFAHLNHRESVSSSETPISNGRRQKAIPLRRHRAPDRSASPKGRLEDDCDDEMLSAIEGLSSTRPCCSKSDDFHTFGPIFLEKGFEREYRLVPIPRARYDFACASLVFVCILLVHLLVMPRMATLGVSFGLVACLLGLVLSFCFATEFSRCFPSRSTLQAISESVETQPLVRLVLVVLTVGSLLTVAIINMPLTLNPGPEQPGDNKTSPLAAQNRVGTPCELLPYYTCSCILGFIACSVFLRMSLELKAMLLTVALVAYLLLFNLSPCWHVSGNSTETNGTQRTRLLLSDAQSMPSHTLAPGARETAPSPSYLERDLKIMVNFYLILFYATLILLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKAAEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSAPSGHENQDLERKHVHIGVLVEFSMALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
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:18205980, PubMed:23229509, PubMed:40419769). Acts as a key mediator of G protein-coupled receptor signaling by catalyzing the formation of cAMP downstream of G protein-coupled receptors (By similarity). Functions in G protein-coupled receptor signaling cascades activated by thrombin, sphingosine 1-phosphate, dopamine and anaphylatoxin C5a (By similarity). Mediates regulation of cAMP synthesis through synergistic action of the G alpha protein G(s) (GNAS) with G(13) (GNA13) (PubMed:18541530, PubMed:23178822). Also involved in inflammation by acting as a diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into c-di-AMP (PubMed:40419769). Following activation by TLR9, mediates formation of c-di-AMP, which directly activates NLRP3, thereby promoting assembly and maturation of the NLRP3 inflammasome (PubMed:40419769). 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 (PubMed:20505140). {ECO:0000250|UniProtKB:P51828, ECO:0000269|PubMed:18205980, ECO:0000269|PubMed:18541530, ECO:0000269|PubMed:20505140, ECO:0000269|PubMed:23178822, ECO:0000269|PubMed:23229509, ECO:0000269|PubMed:40419769}.
uniprot
proteins
mass_dalton
122708
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PRKCD. {ECO:0000250|UniProtKB:P51828}.
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18205980
uniprot
proteins
pubmed
18541530
uniprot
proteins
pubmed
20505140
uniprot
proteins
pubmed
23178822
uniprot
proteins
pubmed
23229509
uniprot
proteins
pubmed
40419769
uniprot
proteins
pubmed
7961850
uniprot
proteins
sequence_length
1099
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 178..198; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 596..616; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 621..641; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 670..689; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 719..738; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 747..766; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 813..833; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins