P01274 · GLUC_PIG

  • Protein
    Pro-glucagon
  • Gene
    GCG
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Glucagon

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.

Glucagon-like peptide 1

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.

Glucagon-like peptide 2

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.

Oxyntomodulin

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.

Glicentin

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.

Miscellaneous

GLP-2 does not have cleavage on a pair of basic residues at C-terminus as in other mammals.

Features

Showing features for site.

TypeIDPosition(s)Description
Site52-53Cleavage; by PCSK2
Site83-84Cleavage; by PCSK1 and PCSK2
Site91-92Cleavage; by PCSK1
Site97-98Cleavage; by PCSK1
Site130-131Cleavage; by PCSK1
Site145-146Cleavage; by PCSK1

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionglucagon receptor binding
Molecular Functionhormone activity
Biological Processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
Biological Processglucose homeostasis
Biological Processnegative regulation of apoptotic process
Biological Processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
Biological Processprotein kinase A signaling
Biological Processregulation of insulin secretion
Biological Processresponse to activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      GCG

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    P01274
  • Secondary accessions
    • Q864V8

Proteomes

Organism-specific databases

Subcellular Location

Secreted

Glucagon-like peptide 1

Secreted

Keywords

PTM/Processing

Features

Showing features for signal, peptide, modified residue, propeptide.

TypeIDPosition(s)Description
Signal1-20
PeptidePRO_000001129421-50
PeptidePRO_000001129321-89Glicentin
PeptidePRO_000001129653-81Glucagon
PeptidePRO_000001129553-89Oxyntomodulin
Modified residue54Phosphoserine
PropeptidePRO_000001129784-89
PeptidePRO_000001129892-128Glucagon-like peptide 1
PeptidePRO_000001130098-127Glucagon-like peptide 1(7-36)
PeptidePRO_000001129998-128Glucagon-like peptide 1(7-37)
Modified residue105Phosphoserine
Modified residue108Phosphoserine
Modified residue127Arginine amide
PropeptidePRO_0000011301131-145
PeptidePRO_0000011302146-180Glucagon-like peptide 2
Modified residue150Phosphoserine
Modified residue152Phosphoserine

Post-translational modification

Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity).

Keywords

Proteomic databases

Expression

Tissue specificity

Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP-1 and GLP-2 are also secreted in selected neurons in the brain.

Induction

Glucagon release is stimulated by hypoglycemia and inhibited by hyperglycemia, insulin, and somatostatin. GLP-1 and GLP-2 are induced in response to nutrient ingestion (By similarity).

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region25-59Disordered

Sequence similarities

Belongs to the glucagon family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    180
  • Mass (Da)
    21,029
  • Last updated
    2004-03-29 v4
  • Checksum
    362997AB72197EE6
MKTIYFVAGLFVMLVQGSWQRSLQNTEEKSRSFPAPQTDPLDDPDQMTEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVTIVEELRRRHADGSFSDEMNTVLDNLATRDFINWLLHTKITDSL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict143in Ref. 6; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY242124
EMBL· GenBank· DDBJ
AAO88211.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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