| Identification |
|---|
| HMDB Protein ID
| HMDBP13584 |
| Secondary Accession Numbers
| None |
| Name
| Pro-glucagon |
| Synonyms
|
Not Available
|
| Gene Name
| GCG |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.Potent stimulator of glucose-dependent insulin release. Also stimulates insulin release in response to IL6. Plays important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Has growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis.Stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability.Significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness.May modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. |
| Pathways
|
- cAMP signaling pathway
- Glucagon signaling pathway
- Insulin secretion
- Neuroactive ligand-receptor interaction
- Thermogenesis
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| positive regulation of protein binding |
| protein kinase A signaling |
| positive regulation of bicellular tight junction assembly |
| negative regulation of execution phase of apoptosis |
| adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
| positive regulation of gluconeogenesis |
| positive regulation of calcium ion import |
| positive regulation of insulin secretion involved in cellular response to glucose stimulus |
| positive regulation of protein kinase activity |
| positive regulation of peptidyl-serine phosphorylation |
| positive regulation of histone H3-K4 methylation |
| response to activity |
| regulation of insulin secretion |
| positive regulation of peptidyl-threonine phosphorylation |
| positive regulation of ERK1 and ERK2 cascade |
| negative regulation of apoptotic process |
| adenylate cyclase-activating G-protein coupled receptor signaling pathway |
| glucose homeostasis |
| Cellular Component |
| cytoplasm |
| extracellular space |
| Molecular Function |
| hormone activity |
| glucagon receptor binding |
| identical protein binding |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 180 |
| Molecular Weight
| 21029.235 |
| Theoretical pI
| 6.136 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P01274 |
| UniProtKB/Swiss-Prot Entry Name
| GLUC_PIG |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Orskov C, Bersani M, Johnsen AH, Hojrup P, Holst JJ: Complete sequences of glucagon-like peptide-1 from human and pig small intestine. J Biol Chem. 1989 Aug 5;264(22):12826-9. [PubMed:2753890 ]
- Drucker DJ: Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis. Mol Endocrinol. 2003 Feb;17(2):161-71. [PubMed:12554744 ]
- Jiang G, Zhang BB: Glucagon and regulation of glucose metabolism. Am J Physiol Endocrinol Metab. 2003 Apr;284(4):E671-8. [PubMed:12626323 ]
- Kieffer TJ, Habener JF: The glucagon-like peptides. Endocr Rev. 1999 Dec;20(6):876-913. [PubMed:10605628 ]
- Thim L, Moody AJ: The primary structure of porcine glicentin (proglucagon). Regul Pept. 1981 May;2(2):139-50. doi: 10.1016/0167-0115(81)90007-0. [PubMed:6894800 ]
- Thim L, Moody AJ: The amino acid sequence of porcine glicentin. Peptides. 1981;2 Suppl 2:37-9. doi: 10.1016/0196-9781(81)90007-3. [PubMed:7045833 ]
- Buhl T, Thim L, Kofod H, Orskov C, Harling H, Holst JJ: Naturally occurring products of proglucagon 111-160 in the porcine and human small intestine. J Biol Chem. 1988 Jun 25;263(18):8621-4. [PubMed:3379036 ]
- Drucker DJ: Glucagon-like Peptide 2. Trends Endocrinol Metab. 1999 May;10(4):153-156. doi: 10.1016/s1043-2760(98)00136-2. [PubMed:10322410 ]
- Sasaki K, Dockerill S, Adamiak DA, Tickle IJ, Blundell T: X-ray analysis of glucagon and its relationship to receptor binding. Nature. 1975 Oct 30;257(5529):751-7. doi: 10.1038/257751a0. [PubMed:171582 ]
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