Proglucagon

GCG
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BH0, 1NAU, 2G49, 2M5P, 2M5Q,%%s4ZGM, 4APD, 3IOL, 1D0R,%%s2L64, 2L63
Identifiers
Aliases	GCG, GLP1, glucagon, GRPP, GLP-1, GLP2
External IDs	OMIM: 138030; MGI: 95674; HomoloGene: 136497; GeneCards: GCG; OMA:GCG - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	162,152,404 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	62,313,994 bp
RNA expression pattern
	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
	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
	2641
	14526
	ENSG00000115263
	ENSMUSG00000000394
	P01275
	P55095
	NM_002054
	NM_008100
	NP_002045
	NP_032126
	Wikidata
View/Edit Human	View/Edit Mouse

Proglucagon is a protein that is cleaved from preproglucagon. Preproglucagon in humans is encoded by the GCG gene and is composed of 180 amino-acid residues.^[5]^[6]

Proglucagon is a precursor of glucagon, and several other components. It is generated in the alpha cells of the pancreas and in the intestinal L cells in the distal ileum and colon.

More specifically, preproglucagon is cleaved into the following components in different organs:

Signal peptide (1-20) – removed from preproglucagon to form proglucagon (21-180)
Glicentin (21–89)
Glicentin-related pancreatic polypeptide (GRPP, 21-50)
Oxyntomodulin (OXY or OXM, 53–89)
Glucagon (53–81)
Glucagon-like peptide 1 (GLP-1, 92–128) – first seven residues further cleaved
Glucagon-like peptide 2 (GLP-2, 146–178)

Proglucagon itself is a protein with three repeats of slightly different secretin family hormones to be cleaved to form mature hormones.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000115263 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000000394 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Schroeder WT, Lopez LC, Harper ME, Saunders GF (1984). "Localization of the human glucagon gene (GCG) to chromosome segment 2q36–37". Cytogenetics and Cell Genetics. 38 (1): 76–79. doi:10.1159/000132034. PMID 6546710.
^ White JW, Saunders GF (June 1986). "Structure of the human glucagon gene". Nucleic Acids Research. 14 (12): 4719–4730. doi:10.1093/nar/14.12.4719. PMC 311486. PMID 3725587.
^ Pollock HG, Hamilton JW, Rouse JB, Ebner KE, Rawitch AB (July 1988). "Isolation of peptide hormones from the pancreas of the bullfrog (Rana catesbeiana). Amino acid sequences of pancreatic polypeptide, oxyntomodulin, and two glucagon-like peptides". The Journal of Biological Chemistry. 263 (20): 9746–9751. doi:10.1016/S0021-9258(19)81581-8. PMID 3260236.

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000115263 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000000394 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid6546710-5] Schroeder WT, Lopez LC, Harper ME, Saunders GF (1984). "Localization of the human glucagon gene (GCG) to chromosome segment 2q36–37". Cytogenetics and Cell Genetics. 38 (1): 76–79. doi:10.1159/000132034. PMID 6546710.

[pmid3725587-6] White JW, Saunders GF (June 1986). "Structure of the human glucagon gene". Nucleic Acids Research. 14 (12): 4719–4730. doi:10.1093/nar/14.12.4719. PMC 311486. PMID 3725587.

[PUB00002491-7] Pollock HG, Hamilton JW, Rouse JB, Ebner KE, Rawitch AB (July 1988). "Isolation of peptide hormones from the pancreas of the bullfrog (Rana catesbeiana). Amino acid sequences of pancreatic polypeptide, oxyntomodulin, and two glucagon-like peptides". The Journal of Biological Chemistry. 263 (20): 9746–9751. doi:10.1016/S0021-9258(19)81581-8. PMID 3260236.

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References

Further reading

External links