GIPR

This gene encodes a G-protein coupled receptor for gastric inhibitory polypeptide (GIP), which was originally identified as an activity in gut extracts that inhibited gastric acid secretion and gastrin release, but subsequently was demonstrated to stimulate insulin release in the presence of elevated glucose. Mice lacking this gene exhibit higher blood glucose levels with impaired initial insulin response after oral glucose load. Defect in this gene thus may contribute to the pathogenesis of diabetes.

Full Name

Gastric Inhibitory Polypeptide Receptor

Function

This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Biological Process

Activation of adenylate cyclase activity Source: ProtInc
Adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: BHF-UCL
Adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: GO_Central
Cell surface receptor signaling pathway Source: ProtInc
Desensitization of G protein-coupled receptor signaling pathway Source: Ensembl
Endocrine pancreas development Source: Ensembl
Gastric inhibitory peptide signaling pathway Source: BHF-UCL
Generation of precursor metabolites and energy Source: ProtInc
Positive regulation of cAMP-mediated signaling Source: Ensembl
Positive regulation of cytosolic calcium ion concentration Source: Ensembl
Positive regulation of insulin secretion Source: Ensembl
Regulation of insulin secretion Source: ParkinsonsUK-UCL
Response to axon injury Source: Ensembl
Response to calcium ion Source: Ensembl
Response to fatty acid Source: Ensembl
Response to glucose Source: Ensembl
Response to nutrient Source: ProtInc

Cellular Location

Cell membrane

Topology

Extracellular: 22-138
Helical: 139-161
Cytoplasmic: 162-169
Helical: 170-189
Extracellular: 190-217
Helical: 218-242
Cytoplasmic: 243-254
Helical: 255-278
Extracellular: 279-293
Helical: 294-319
Cytoplasmic: 320-341
Helical: 342-362
Extracellular: 363-377
Helical: 378-398
Cytoplasmic: 399-466

PTM

N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER.