GCGR

The protein encoded by this gene is a glucagon receptor that is important in controlling blood glucose levels. Defects in this gene are a cause of non-insulin-dependent diabetes mellitus (NIDDM).

glucagon receptor

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. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system.

Adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: UniProtKB
Adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: UniProtKB
Cell surface receptor signaling pathway Source: InterPro
Cellular response to glucagon stimulus Source: UniProtKB
Cellular response to starvation Source: ARUK-UCL
Exocytosis Source: Ensembl
Generation of precursor metabolites and energy Source: ProtInc
Glucose homeostasis Source: UniProtKB
Hormone-mediated signaling pathway Source: Ensembl
Positive regulation of gene expression Source: ARUK-UCL
Regulation of blood pressure Source: ProtInc
Regulation of glycogen metabolic process Source: UniProtKB
Response to nutrient Source: ProtInc
Response to starvation Source: UniProtKB

Cell membrane. Is rapidly internalized after ligand-binding.

Extracellular: 26-136
Helical: 137-161
Cytoplasmic: 162-173
Helical: 174-198
Extracellular: 199-225
Helical: 226-249
Cytoplasmic: 250-263
Helical: 264-285
Extracellular: 286-303
Helical: 304-326
Cytoplasmic: 327-350
Helical: 351-369
Extracellular: 370-381
Helical: 382-402
Cytoplasmic: 403-477

Ligand-binding promotes phosphorylation of serine residues in the C-terminal cytoplasmic domain. Phosphorylation is important for receptor endocytosis after ligand-binding.