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Proteins/UNIPROT:P29992
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. Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNA11 activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs). Together with GNAQ, required for heart development (By similarity). In the respiratory epithelium, transmits OXGR1-dependent signals that lead to downstream intracellular Ca(2+) release and mucocilliary clearance of airborne pathogens..
Function from UniProtKB (P29992), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
4 rows
248 statements
248 statements · 4 reference databases · Subject: GNA11 · Sources: gene ontology, Hetionet, Reactome, WikiPathways
1 reaction
4 names
Resolves to: GNA11
Rhea RHEA:19669CC BY 4.0Reference data