Gnaq
entrez
14682
canonical
uniprot
P21279
canonical
ensembl
ENSMUSG00000024639
resolver
ensp
ENSMUSP00000025541
resolver
enst
ENSMUST00000025541
resolver
genesymbol
Gnaq
resolver
uniprot
Q3UHH5
resolver
uniprot
Q6PFF5
resolver
uniprot_entry
GNAQ_MOUSE
resolver
uniprot_entry
Q3UHH5_MOUSE
resolver
uniprot_sec
Q6PFF5
resolver
amino_acid_sequence
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:20966218, PubMed:9687499). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:20966218). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:20966218). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:20966218). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:20966218). Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNAQ activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:20966218). Required for platelet activation (PubMed:9296496). Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity (PubMed:20624888). Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (PubMed:17938235). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNA11, required for heart development (PubMed:9687499). {ECO:0000250|UniProtKB:P50148, ECO:0000269|PubMed:17938235, ECO:0000269|PubMed:20624888, ECO:0000269|PubMed:20966218, ECO:0000269|PubMed:9296496, ECO:0000269|PubMed:9687499}.
uniprot
proteins
mass_dalton
42158
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="C->S: Abolishes palmitoylation."; /evidence="ECO:0000269|PubMed:8227063"; MUTAGEN 10; /note="C->S: Abolishes palmitoylation."; /evidence="ECO:0000269|PubMed:8227063"; MUTAGEN 218; /note="H->A: Reduced ability to activate phospholipase PLCB3."; /evidence="ECO:0000269|PubMed:20966218
uniprot
proteins
post_translational_modification
PTM: Palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:19001095). Palmitoylation occurs in the Golgi and participates in the localization of GNAQ to the plasma membrane (PubMed:19001095). {ECO:0000269|PubMed:19001095}.; PTM: Histaminylated at Gln-209 residues by TGM2. {ECO:0000269|PubMed:23022564}.
uniprot
proteins
protein_family
G(q) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17938235
uniprot
proteins
pubmed
18802028
uniprot
proteins
pubmed
19001095
uniprot
proteins
pubmed
20624888
uniprot
proteins
pubmed
20966218
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2123549
uniprot
proteins
pubmed
23022564
uniprot
proteins
pubmed
23994616
uniprot
proteins
pubmed
8227063
uniprot
proteins
pubmed
9296496
uniprot
proteins
pubmed
9391157
uniprot
proteins
pubmed
9687499
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19001095}; Peripheral membrane protein {ECO:0000269|PubMed:19001095}; Cytoplasmic side {ECO:0000269|PubMed:19001095}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000269|PubMed:18802028}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Note=Associated to the plasma membrane via lipid-anchor (By similarity). Colocalizes with the adrenergic receptors ADRA1A and ADRA1B at the nuclear membrane of cardiac myocytes (PubMed:18802028). {ECO:0000250|UniProtKB:P50148, ECO:0000269|PubMed:18802028}.
uniprot
proteins