SCUBA

GPR4 — G protein-coupled receptor 4

GPR4 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

GPR4's module in each cell type

Cell typeModuleShares the module with
EndothelialInflammatory EC Activation
Inflammation
FJX1, FNDC3B, HK1, ITGA5, MAP1S, MCAM, MSN, P2RY6 +3 moreView in SCUBA
Smooth muscle cellsCapillary Pericyte
Development
ADAP2, ADRA2A, ANKRD29, CCL8, CNGA1, ENPEP, EPHA2, EPS8L1 +10 moreView in SCUBA

About the gene

Chromosome19: 45589764-45602212
Predicted locationMembrane
Essential geneNo
Protein classG-protein coupled receptors, Predicted membrane proteins
Molecular functionG-protein coupled receptor, Receptor, Transducer

Function

Proton-sensing G-protein coupled receptor activated by extracellular pH, which is required to monitor pH changes and generate adaptive reactions. Activated by an optimal pH of 6.8-7.2. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. GPR4 is mainly coupled to G(s) G proteins and mediates activation of adenylate cyclase activity. May also couple with G(q) and G(12)/G(13) G proteins. Acts as a key regulator of respiratory sensitivity to CO2/H(+) in brain retrotrapezoid nucleus neurons: acts by mediating detection of protons generated by the formation of carbonic acid in the blood, an important mechanism to impulse to breathe (By similarity). Also acts as a regulator of acid secretion in the kidney collecting duct by maintaining acid-base homeostasis in the kidney (By similarity). Acidosis-induced GPR4 activation increases paracellular gap formation and permeability of vascular endothelial cells, possibly through the G(12)/G(13)/Rho GTPase signaling pathway.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.