Gnao1
entrez
14681
canonical
uniprot
P18872
canonical
ensembl
ENSMUSG00000031748
resolver
ensp
ENSMUSP00000034198
resolver
ensp
ENSMUSP00000114144
resolver
ensp
ENSMUSP00000148550
resolver
genesymbol
Gnao1
resolver
genesymbol_syn
Gna0
resolver
genesymbol_syn
Gnao
resolver
uniprot
P18873
resolver
uniprot
Q543S2
resolver
uniprot_entry
GNAO_MOUSE
resolver
uniprot_entry
Q543S2_MOUSE
resolver
uniprot_sec
P18873
resolver
activity_regulation
ACTIVITY REGULATION: The GTPase activity is promoted by GTPAse activators, such as RGS14, RGS16 and RGS19. {ECO:0000269|PubMed:10926822}.
uniprot
proteins
amino_acid_sequence
MGCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGVEYGDKERKTDSKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAGDYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDAAAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY
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, such as regulation of postsynaptic neurotransmitter release (PubMed:10926822, PubMed:11248120). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:10926822, PubMed:11248120). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:10926822, PubMed:11248120). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:10926822). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:10926822, PubMed:11248120). Signaling is mediated via effector proteins, such as adenylate cyclase: GNAO1 acts by inhibiting the activity of adenylate cyclases, leading to decreased intracellular cAMP levels (PubMed:10926822, PubMed:11248120). Plays a key role in postsynaptic inhibition of neurotransmitter release (By similarity). {ECO:0000250|UniProtKB:P59215, ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:11248120}.
uniprot
proteins
mass_dalton
40085
uniprot
proteins
mutagenesis
MUTAGEN 184; /note="G->S: Heterozygous knockin mice display neurologic disorders characterized by onset of seizures, a markedly increased frequency of interictal epileptiform discharges, leading to sudden death."; /evidence="ECO:0000269|PubMed:24700286
uniprot
proteins
post_translational_modification
PTM: Histaminylated at Gln-205 residues by TGM2. {ECO:0000269|PubMed:23022564}.
uniprot
proteins
protein_family
G(i/o/t/z) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
10926822
uniprot
proteins
pubmed
11248120
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15585744
uniprot
proteins
pubmed
1697681
uniprot
proteins
pubmed
18434540
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23022564
uniprot
proteins
pubmed
24700286
uniprot
proteins
pubmed
9050846
uniprot
proteins
pubmed
9501252
uniprot
proteins
sequence_length
354
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585744}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09471}; Cytoplasmic side {ECO:0000250|UniProtKB:P09471}. Note=Associated to the cell membrane via lipid-anchor. {ECO:0000250|UniProtKB:P09471}.
uniprot
proteins