Proglucagon

GCG
Identifiers
Aliases	GCG, GLP1, glucagon, GRPP, GLP-1, GLP2
External IDs	OMIM: 138030; MGI: 95674; HomoloGene: 136497; GeneCards: GCG; OMA:GCG - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BH0, 1NAU, 2G49, 2M5P, 2M5Q,%%s4ZGM, 4APD, 3IOL, 1D0R,%%s2L64, 2L63
Gene location (Human) Chr. Chromosome 2 (human) Band 2q24.2 Start 162,142,882 bp End 162,152,404 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 C1.3|2 35.85 cM Start 62,304,874 bp End 62,313,994 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in beta cell body of pancreas rectum mucosa of sigmoid colon mucosa of ileum testicle mucosa of transverse colon epithelium of colon jejunal mucosa appendix Top expressed in islet of Langerhans crypt of lieberkuhn of small intestine ileum large intestine colon lens Paneth cell left colon jejunum epithelium of small intestine More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding identical protein binding hormone activity glucagon receptor binding signaling receptor binding Cellular component cytoplasm endoplasmic reticulum lumen extracellular region secretory granule lumen extracellular space Biological process negative regulation of execution phase of apoptosis G protein-coupled receptor signaling pathway regulation of insulin secretion cellular response to glucagon stimulus positive regulation of peptidyl-serine phosphorylation positive regulation of calcium ion import positive regulation of histone H3-K4 methylation positive regulation of peptidyl-threonine phosphorylation feeding behavior positive regulation of ERK1 and ERK2 cascade positive regulation of protein binding cell population proliferation signal transduction positive regulation of protein kinase activity adenylate cyclase-modulating G protein-coupled receptor signaling pathway protein kinase A signaling positive regulation of insulin secretion involved in cellular response to glucose stimulus response to starvation negative regulation of apoptotic process regulation of signaling receptor activity adenylate cyclase-activating G protein-coupled receptor signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2641 14526 Ensembl ENSG00000115263 ENSMUSG00000000394 UniProt P01275 P55095 RefSeq (mRNA) NM_002054 NM_008100 RefSeq (protein) NP_002045 NP_032126 Location (UCSC) Chr 2: 162.14 – 162.15 Mb Chr 2: 62.3 – 62.31 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Proglucagon is a protein that is a precursor of glucagon and several other components. It is cleaved from preproglucagon. Proglucagon is generated in the alpha cells of the pancreas and in the intestinal L cells in the distal ileum and colon.

Preproglucagon in humans is encoded by the GCG gene and is composed of 180 amino-acid residues.

Function and Terminology

The “pre-” prefix of preproglucagon indicates that it is composed of proglucagon together with a signal peptide. The signal peptide is a 20 amino acid fragment that signals that the protein needs to be secreted out of the cell. Proglucagon has the “pro-“ prefix because it is a prohormone, which means it is an inactivate precursor that needs to be further modified in order to produce active hormone(s). In particular, proglucagon is cleaved (cut) into different active hormones depending on the organ. Omitting various inactive fragments, preproglucagon is cleaved into the following:

Pancreas

• Signal peptide (1-20)
• Glicentin-related pancreatic polypeptide (GRPP, 21-50)
• Glucagon (53–81)

Gut and Brain

• Signal peptide (1-20)
• Glicentin (21–89)
• Oxyntomodulin (OXY or OXM, 53–89) – A further cleavage of Glicentin
• Glucagon-like peptide 1 (GLP-1, 92–128) – first seven residues further cleaved
• Glucagon-like peptide 2 (GLP-2, 146–178)

Further reading

• Drucker DJ (November 2005). "Biologic actions and therapeutic potential of the proglucagon-derived peptides". Nature Clinical Practice. Endocrinology & Metabolism. 1 (1): 22–31. doi:10.1038/ncpendmet0017. PMID 16929363. S2CID 18101345.

External links

• Dhanvantari S. "Molecular and Cellular Mechanisms of Glucagon Synthesis and Secretion". lawsonimaging.ca. Archived from the original on 29 September 2007.
• "PC1 Cleavage Sites". phoenixpeptide.com. Archived from the original on 28 December 2005.
• "GLP-1 is Derived From Proglucagon". medscape.com.
• "Pro-glucagon". PDBe-KB Aggregated Views of Proteins. Wellcome Genome Campus, Hinxton, Cambridgeshire: EMBL-EBI.