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Protein

Glucagon

Gene

GCG

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity
GLP-1 is a potent stimulator of glucose-dependent insulin release. Play 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. Have 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 (By similarity).By similarity
GLP-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 (By similarity).By similarity
Oxyntomodulin significantly reduces food intake.By similarity
Glicentin may modulate gastric acid secretion and gastro-pyloro-duodenal activity.

GO - Molecular functioni

  • glucagon receptor binding Source: GO_Central
  • hormone activity Source: AgBase

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  • lactate biosynthetic process Source: AgBase
  • lipid biosynthetic process Source: AgBase
  • negative regulation of apoptotic process Source: GO_Central
  • positive regulation of gluconeogenesis Source: AgBase
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: GO_Central
  • protein kinase A signaling Source: GO_Central
  • response to starvation Source: GO_Central

Keywordsi

Molecular functionHormone

Enzyme and pathway databases

ReactomeiR-BTA-163359 Glucagon signaling in metabolic regulation
R-BTA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-BTA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-BTA-416476 G alpha (q) signalling events
R-BTA-418555 G alpha (s) signalling events
R-BTA-420092 Glucagon-type ligand receptors
R-BTA-422085 Synthesis, secretion, and deacylation of Ghrelin

Names & Taxonomyi

Protein namesi
Recommended name:
Glucagon
Cleaved into the following 8 chains:
Oxyntomodulin
Short name:
OXM
Short name:
OXY
Glucagon-like peptide 1
Short name:
GLP-1
Glucagon-like peptide 1(7-37)
Short name:
GLP-1(7-37)
Glucagon-like peptide 1(7-36)
Short name:
GLP-1(7-36)
Glucagon-like peptide 2
Short name:
GLP-2
Gene namesi
Name:GCG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Organism-specific databases

VGNCiVGNC:29284 GCG

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
PeptideiPRO_000001122321 – 89GlicentinBy similarityAdd BLAST69
PeptideiPRO_000001122421 – 50Glicentin-related polypeptideBy similarityAdd BLAST30
PeptideiPRO_000001122553 – 89OxyntomodulinBy similarityAdd BLAST37
PeptideiPRO_000001122653 – 81GlucagonAdd BLAST29
PropeptideiPRO_000001122784 – 89By similarity6
PeptideiPRO_000001122892 – 128Glucagon-like peptide 1By similarityAdd BLAST37
PeptideiPRO_000001122998 – 128Glucagon-like peptide 1(7-37)By similarityAdd BLAST31
PeptideiPRO_000001123098 – 127Glucagon-like peptide 1(7-36)By similarityAdd BLAST30
PropeptideiPRO_0000011231131 – 145By similarityAdd BLAST15
PeptideiPRO_0000011232146 – 178Glucagon-like peptide 2By similarityAdd BLAST33

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54PhosphoserineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei127Arginine amideBy similarity1
Modified residuei150PhosphoserineBy similarity1
Modified residuei152PhosphoserineBy similarity1

Post-translational modificationi

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei52 – 53Cleavage; by PCSK2By similarity2
Sitei83 – 84Cleavage; by PCSK1 and PCSK2By similarity2
Sitei91 – 92Cleavage; by PCSK1By similarity2
Sitei97 – 98Cleavage; by PCSK1By similarity2
Sitei130 – 131Cleavage; by PCSK1By similarity2
Sitei145 – 146Cleavage; by PCSK1By similarity2

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Phosphoprotein

Proteomic databases

PaxDbiP01272
PRIDEiP01272

Expressioni

Tissue specificityi

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.

Inductioni

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).By similarity

Gene expression databases

BgeeiENSBTAG00000000730
ExpressionAtlasiP01272 baseline and differential

Interactioni

GO - Molecular functioni

  • glucagon receptor binding Source: GO_Central
  • hormone activity Source: AgBase

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000054709

Structurei

Secondary structure

1180
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni60 – 64Combined sources5
Beta strandi70 – 73Combined sources4
Helixi75 – 78Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KX6NMR-A53-81[»]
ProteinModelPortaliP01272
SMRiP01272
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01272

Family & Domainsi

Sequence similaritiesi

Belongs to the glucagon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IKZ8 Eukaryota
ENOG4111VKC LUCA
GeneTreeiENSGT00390000005372
HOGENOMiHOG000231876
HOVERGENiHBG003010
InParanoidiP01272
KOiK05259

Family and domain databases

InterProiView protein in InterPro
IPR015550 Glucagon
IPR000532 Glucagon_GIP_secretin_VIP
PANTHERiPTHR11418 PTHR11418, 1 hit
PfamiView protein in Pfam
PF00123 Hormone_2, 3 hits
PRINTSiPR00275 GLUCAGON
SMARTiView protein in SMART
SM00070 GLUCA, 3 hits
PROSITEiView protein in PROSITE
PS00260 GLUCAGON, 4 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLYFVAGL FVMLVQGSWQ RSLQNTEEKS SSFPAPQTDP LGDPDQINED
60 70 80 90 100
KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNKNNIAK RHDEFERHAE
110 120 130 140 150
GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVNIVE ELRRRHADGS
160 170 180
FSDEMNTVLD SLATRDFINW LLQTKITDRK
Length:180
Mass (Da):20,944
Last modified:August 13, 1987 - v1
Checksum:i8D9B4FF05B9F15FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00107 mRNA Translation: AAA30538.1
BC102221 mRNA Translation: AAI02222.1
PIRiA93970 GCBO
RefSeqiNP_776341.1, NM_173916.3
UniGeneiBt.410

Genome annotation databases

EnsembliENSBTAT00000000972; ENSBTAP00000000972; ENSBTAG00000000730
GeneIDi280802
KEGGibta:280802

Similar proteinsi

Entry informationi

Entry nameiGLUC_BOVIN
AccessioniPrimary (citable) accession number: P01272
Secondary accession number(s): Q3T0X0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: May 23, 2018
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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