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Guanine nucleotide-binding protein G(i) subunit alpha-3

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 (By similarity). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins^1,2,3. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels⁴. Stimulates the activity of receptor-regulated K(+) channels⁵. 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 division⁶. The active GTP-bound form activates the calcium permeant TRPC5 ion channels⁷.

AlphaFold DB , UniProt , Accession P08754, Species HUMAN (Homo sapiens, Human), Gene GNAI3, Length 354 aa.