GNAI1

Guanine nucleotide-binding proteins (G proteins) form a large family of signal-transducing molecules. They are found as heterotrimers made up of alpha, beta, and gamma subunits. Members of the G protein family have been characterized most extensively on the basis of the alpha subunit, which binds guanine nucleotide, is capable of hydrolyzing GTP, and interacts with specific receptor and effector molecules. The G protein family includes Gs (MIM 139320) and Gi, the stimulatory and inhibitory GTP-binding regulators of adenylate cyclase; Go, a protein abundant in brain (GNAO1; MIM 139311); and transducin-1 (GNAT1; MIM 139330) and transducin-2 (GNAT2; MIM 139340), proteins involved in phototransduction in retinal rods and cones, respectively (Sullivan et al., 1986 [PubMed 3092218]; Bray et al., 1987 [PubMed 3110783]). Suki et al. (1987) [PubMed 2440724] concluded that the human genome contains at least 3 nonallelic genes for alpha-i-type subunits of G protein; see, e.g, GNAI2 (MIM 139360), GNAI3 (MIM 139370), and GNAIH (MIM 139180).[supplied by OMIM

guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 1

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. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:8774883, PubMed:18434541).

Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity).

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:17635935).

Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed:22327364).

Adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway Source: Reactome
Adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: GO_Central
Cell cycle Source: UniProtKB-KW
Cell division Source: UniProtKB
Cellular response to forskolin Source: UniProtKB
G protein-coupled receptor signaling pathway Source: UniProtKB
Negative regulation of synaptic transmission Source: Ensembl
Positive regulation of protein localization to cell cortex Source: UniProtKB
Regulation of cAMP-mediated signaling Source: UniProtKB
Regulation of mitotic spindle organization Source: UniProtKB
Response to peptide hormone Source: BHF-UCL

Centrosome; Nucleus; Cell membrane; Cytoplasm; Cell cortex; Membrane. Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody (PubMed:17635935). Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane.

Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.By similarity
Palmitoylation at Cys-3 varies with membrane lipid composition.By similarity
(Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA.