Gnai3
entrez
25643
canonical
uniprot
P08753
canonical
ensembl
ENSRNOG00055020855
resolver
ensembl
ENSRNOG00060026328
resolver
ensembl
ENSRNOG00065023751
resolver
ensp
ENSRNOP00055028915
resolver
ensp
ENSRNOP00060038070
resolver
ensp
ENSRNOP00065033305
resolver
enst
ENSRNOT00055035657
resolver
enst
ENSRNOT00060045874
resolver
enst
ENSRNOT00065040819
resolver
genesymbol
Gnai3
resolver
genesymbol_syn
Gnai-3
resolver
uniprot_entry
GNAI3_RAT
resolver
amino_acid_sequence
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTSELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQTNYIPTQQDVLRTRVKTTGIVETHFTFKELYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEVYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY
uniprot
proteins
function
FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:2159473). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). Stimulates the activity of receptor-regulated K(+) channels (By similarity). The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division (By similarity). The active GTP-bound form activates the calcium permeant TRPC5 ion channels (By similarity). {ECO:0000250|UniProtKB:P08754, ECO:0000269|PubMed:2159473}.
uniprot
proteins
mass_dalton
40522
uniprot
proteins
mutagenesis
MUTAGEN 40; /note="G->R: Fails to bind GTP. Prevents endothelin-mediated activation of GNAQ. Results in increased frequency of developmental defects compared to wild-type when ectopically expressed in Xenopus laevis embryos."; /evidence="ECO:0000269|PubMed:27072656"; MUTAGEN 45; /note="G->V: Fails to bind GTP. Prevents endothelin-mediated activation of GNAQ. Results in increased frequency of developmental defects compared to wild-type when ectopically expressed in Xenopus laevis embryos."; /evidence="ECO:0000269|PubMed:27072656"; MUTAGEN 47; /note="S->R: Fails to bind GTP. Prevents endothelin-mediated activation of GNAQ. Results in increased frequency of developmental defects compared to wild-type when ectopically expressed in Xenopus laevis embryos."; /evidence="ECO:0000269|PubMed:27072656"; MUTAGEN 48; /note="T->N: Fails to bind GTP. Prevents endothelin-mediated activation of GNAQ. Results in increased frequency of developmental defects compared to wild-type when ectopically expressed in Xenopus laevis embryos."; /evidence="ECO:0000269|PubMed:27072656"; MUTAGEN 203; /note="G->A: Reduces cell migration by 50% and increases mitosis six-fold."; /evidence="ECO:0000269|PubMed:20462955"; MUTAGEN 204; /note="Q->L: No effect on promotion of cell migration or GTP-binding activity. Increases sensitivity to activation by CCDC88A."; /evidence="ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:31363053"; MUTAGEN 208; /note="R->A: Dramatically decreases binding to CCDC88A."; /evidence="ECO:0000269|PubMed:19211784"; MUTAGEN 211; /note="W->A: Abolishes binding to NUCB1. Dramatically decreases binding to CCDC88A. Does not affect GTP-binding activity but increases the basal exchange rate."; /evidence="ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:21653697, ECO:0000269|PubMed:31363053"; MUTAGEN 215; /note="F->A: Abolishes binding to NUCB1. Dramatically decreases binding to CCDC88A. Does not affect GTP-binding activity but increases the basal exchange rate."; /evidence="ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:21653697, ECO:0000269|PubMed:31363053"; MUTAGEN 248; /note="K->E: Abolishes binding to NUCB1."; /evidence="ECO:0000269|PubMed:21653697"; MUTAGEN 248; /note="K->M: Dramatically decreases interaction with NUCB1."; /evidence="ECO:0000269|PubMed:21653697"; MUTAGEN 258; /note="W->F: No effect on interaction with NUCB1."; /evidence="ECO:0000269|PubMed:21653697"; MUTAGEN 269; /note="N->Y: Fails to bind GTP. Prevents endothelin-mediated activation of GNAQ. Results in increased frequency of developmental defects compared to wild-type when ectopically expressed in Xenopus laevis embryos."; /evidence="ECO:0000269|PubMed:27072656
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
19211784
uniprot
proteins
pubmed
20462955
uniprot
proteins
pubmed
2159473
uniprot
proteins
pubmed
21653697
uniprot
proteins
pubmed
25187647
uniprot
proteins
pubmed
27072656
uniprot
proteins
pubmed
2820999
uniprot
proteins
pubmed
2834384
uniprot
proteins
pubmed
31363053
uniprot
proteins
pubmed
31570568
uniprot
proteins
sequence_length
354
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. {ECO:0000250|UniProtKB:P08754}.
uniprot
proteins