Recombinant Human Glucagon receptor (GCGR), partial

Function

G protein-coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:32193322, PubMed:38346960). Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system

Subcellular Location

Cell membrane (Multi-pass membrane protein)

Disease Association

Mahvash disease (MVAH) : An autosomal recessive disorder characterized by alpha-cell hyperplasia of the pancreas, hyperglucagonemia without glucagonoma syndrome, aminoacidemia, and occasional hypoglycemia. The disease may lead to glucagonomas and/or primitive neuroectodermal tumors. [The disease is caused by variants affecting the gene represented in this entry]

Subunit

Interacts with glucagon (PubMed:32193322). Interacts with GNAS (PubMed:32193322, PubMed:38346960). Interacts with GNAI1 (PubMed:32193322, PubMed:38346960)

• Macneil D.J. et al. Cloning and expression of a human glucagon receptor. — Biochem. Biophys. Res. Commun. (1994)
• Lok S. et al. The human glucagon receptor encoding gene: structure, cDNA sequence and chromosomal localization. — Gene (1994)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Menzel S. et al. Localization of the glucagon receptor gene to human chromosome band 17q25. — Genomics (1994)
• Buggy J.J. et al. Role of the glucagon receptor COOH-terminal domain in glucagon-mediated signaling and receptor internalization. — Diabetes (1997)
• Bian Y. et al. An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. — J. Proteomics (2014)
• Ruckert C. et al. Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype. — J. Biol. Chem. (2006)
• Koth C.M. et al. Molecular basis for negative regulation of the glucagon receptor. — Proc. Natl. Acad. Sci. U.S.A. (2012)