Adcy2
entrez
81636
canonical
uniprot
P26769
canonical
ensembl
ENSRNOG00000032150
resolver
ensp
ENSRNOP00000038994
resolver
ensp
ENSRNOP00000109970
resolver
enst
ENSRNOT00000047627
resolver
enst
ENSRNOT00000127647
resolver
genesymbol
Adcy2
resolver
uniprot
A0ABK0LGM5
resolver
uniprot
F1LV12
resolver
uniprot_entry
A0ABK0LGM5_RAT
resolver
uniprot_entry
ADCY2_RAT
resolver
uniprot_entry
F1LV12_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated by forskolin (PubMed:1719547, PubMed:22906005, PubMed:24363043). Is not activated by calmodulin (PubMed:1719547). Inhibited by calcium ions, already at micromolar concentration. Activated by the G protein alpha subunit GNAS (PubMed:1719547, PubMed:21596131, PubMed:7761832). Activated by the G protein beta and gamma subunit complex (PubMed:21596131, PubMed:22906005, PubMed:7761832). Phosphorylation by RAF1 results in its activation (By similarity). Phosphorylation by PKC activates the enzyme (PubMed:22906005). {ECO:0000250|UniProtKB:Q08462, ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:22906005, ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:7761832}.
uniprot
proteins
amino_acid_sequence
MRRRRYLRDRAEAAAAAAAGGGEGLQRSRDWLYESYYCMSQQHPLIVFLLLIVMGACLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRVFSLVIWICLVAMGYLFMCFGGTVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHTIVLSVYLSATPGAKEHLFWQILANVIIFICGNLAGAYHKHLMELALQQTYRDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEGDGEIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPRHTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTLRTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKNIEKEYRATALPAFKYYVTCACLIFLCIFIVQILVLPKTSILGFSFGAAFLSLIFILFVCFAGQLLQCSKKASTSLMWLLKSSGIIANRPWPRISLTIVTTAIILTMAVFNMFFLSNSEETTLPTANTSNANVSVPDNQASILHARNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHTHAHVLDAYSQVLFQRPGIWKDLKTMGSVSLSIFFITLLVLGRQSEYYCRLDFLWKNKFKKEREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLILQTLGYTCTCRGIINVKGKGDLKTYFVNTEMSRSLSQSNLAS
uniprot
proteins
ec_number
4.6.1.1
uniprot
proteins
function
FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G protein signaling (PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:1719547, PubMed:19243146, PubMed:21596131, PubMed:22906005, PubMed:24363043, PubMed:7761832). Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production (PubMed:24363043). Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (PubMed:22906005). {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:22906005, ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:7761832}.
uniprot
proteins
mass_dalton
123316
uniprot
proteins
mutagenesis
MUTAGEN 490; /note="S->A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-543."; /evidence="ECO:0000269|PubMed:22906005"; MUTAGEN 490; /note="S->D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-543."; /evidence="ECO:0000269|PubMed:22906005"; MUTAGEN 543; /note="S->A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-490."; /evidence="ECO:0000269|PubMed:22906005"; MUTAGEN 543; /note="S->D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-490."; /evidence="ECO:0000269|PubMed:22906005
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by RAF1 (By similarity). {ECO:0000250|UniProtKB:Q08462}.
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
10427002
uniprot
proteins
pubmed
11087399
uniprot
proteins
pubmed
15591060
uniprot
proteins
pubmed
16766715
uniprot
proteins
pubmed
1719547
uniprot
proteins
pubmed
19243146
uniprot
proteins
pubmed
21596131
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
22906005
uniprot
proteins
pubmed
24363043
uniprot
proteins
pubmed
7761832
uniprot
proteins
pubmed
9069282
uniprot
proteins
pubmed
9417641
uniprot
proteins
sequence_length
1090
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:22906005}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:7761832}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q08462}.
uniprot
proteins
transmembrane_region
TRANSMEM 45..65; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 75..95; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 107..127; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 132..152; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 157..177; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 186..206; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 601..621; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 626..646; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 679..699; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 734..754; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 763..783; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 800..820; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins