Gnai1
entrez
25686
canonical
uniprot
P10824
canonical
ensembl
ENSRNOG00000057096
resolver
ensembl
ENSRNOG00055021986
resolver
ensembl
ENSRNOG00060012765
resolver
ensembl
ENSRNOG00065016882
resolver
ensp
ENSRNOP00000074036
resolver
ensp
ENSRNOP00055030885
resolver
ensp
ENSRNOP00060017197
resolver
ensp
ENSRNOP00065022342
resolver
enst
ENSRNOT00000091004
resolver
enst
ENSRNOT00055037843
resolver
enst
ENSRNOT00060021730
resolver
enst
ENSRNOT00065028267
resolver
genesymbol
Gnai1
resolver
genesymbol_syn
Gnai-1
resolver
uniprot
Q45QN2
resolver
uniprot_entry
GNAI1_RAT
resolver
uniprot_sec
Q45QN2
resolver
amino_acid_sequence
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
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:19703466, PubMed:24596087, PubMed:25037222). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:19703466, PubMed:24596087, PubMed:25037222). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:21158412). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:21158412). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity of ADCY1, ADCY5 and ADCY6, leading to decreased intracellular cAMP levels (PubMed:19703466). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed:16870394). Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity). {ECO:0000250|UniProtKB:P63096, ECO:0000269|PubMed:16870394, ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:21158412, ECO:0000269|PubMed:24596087, ECO:0000269|PubMed:25037222, ECO:0000305}.
uniprot
proteins
mass_dalton
40345
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Abolishes myristoylation and palmitoylation."; /evidence="ECO:0000269|PubMed:26253820"; MUTAGEN 3; /note="C->S: Abolishes palmitoylation."; /evidence="ECO:0000269|PubMed:26253820"; MUTAGEN 43; /note="E->A: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange."; /evidence="ECO:0000269|PubMed:24596087"; MUTAGEN 149; /note="N->I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A."; /evidence="ECO:0000269|PubMed:21158412"; MUTAGEN 189; /note="F->Y: Increases basal GDP exchange rate; no effect on receptor-stimulated GDP exchange."; /evidence="ECO:0000269|PubMed:25037222"; MUTAGEN 191; /note="F->Y: No effect on basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange."; /evidence="ECO:0000269|PubMed:25037222"; MUTAGEN 204; /note="Q->L: Expected to have lost GTPase activity; inhibits the forskolin-mediated increase of cellular cAMP levels. Does not inhibit interaction with RGS14 at centrosomes."; /evidence="ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:19703466"; MUTAGEN 329; /note="T->A: Increases basal GDP exchange rate and inhibits the forskolin-mediated increase of cellular cAMP levels."; /evidence="ECO:0000269|PubMed:19703466"; MUTAGEN 332; /note="V->A: Increases basal GDP exchange rate."; /evidence="ECO:0000269|PubMed:19703466"; MUTAGEN 336; /note="F->A,C: Increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange."; /evidence="ECO:0000269|PubMed:25037222"; MUTAGEN 336; /note="F->Y: Strongly increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange."; /evidence="ECO:0000269|PubMed:25037222"; MUTAGEN 345; /note="K->L: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange."; /evidence="ECO:0000269|PubMed:24596087
uniprot
proteins
post_translational_modification
PTM: Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation. {ECO:0000269|PubMed:26253820}.; PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. {ECO:0000269|PubMed:26253820}.
uniprot
proteins
protein_family
G(i/o/t/z) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
11121039
uniprot
proteins
pubmed
11387333
uniprot
proteins
pubmed
16870394
uniprot
proteins
pubmed
17635935
uniprot
proteins
pubmed
19211784
uniprot
proteins
pubmed
19703466
uniprot
proteins
pubmed
21158412
uniprot
proteins
pubmed
21653697
uniprot
proteins
pubmed
24596087
uniprot
proteins
pubmed
25037222
uniprot
proteins
pubmed
26253820
uniprot
proteins
pubmed
2820999
uniprot
proteins
pubmed
32103024
uniprot
proteins
pubmed
8073283
uniprot
proteins
pubmed
8521505
uniprot
proteins
pubmed
9108480
uniprot
proteins
pubmed
9705312
uniprot
proteins
pubmed
9772163
uniprot
proteins
sequence_length
354
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:21158412}; Peripheral membrane protein {ECO:0000269|PubMed:26253820, ECO:0000305|PubMed:24596087, ECO:0000305|PubMed:25037222}; Cytoplasmic side {ECO:0000269|PubMed:26253820}. Nucleus {ECO:0000269|PubMed:17635935}. Cytoplasm {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Note=Associated to the plasma membrane via lipid-anchor (PubMed:26253820). Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis (By similarity). Detected at the cleavage furrow or the midbody (By similarity). Localized at the plasma membrane throughout mitosis (By similarity). Colocalizes with RIC8A and RGS14 at the plasma membrane (PubMed:21158412). {ECO:0000250|UniProtKB:P63096, ECO:0000269|PubMed:21158412, ECO:0000269|PubMed:26253820}.
uniprot
proteins