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Protein

Glucagon

Gene

Gcg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.1 Publication
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. Inhibits beta cell apoptosis.1 Publication
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.1 Publication
Oxyntomodulin significantly reduces food intake.1 Publication
Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity.1 Publication

GO - Molecular functioni

  • glucagon receptor binding Source: RGD
  • hormone activity Source: RGD

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RGD
  • negative regulation of apoptotic process Source: GO_Central
  • negative regulation of appetite Source: RGD
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: GO_Central
  • protein kinase A signaling Source: GO_Central
  • protein metabolic process Source: RGD
  • regulation of carbohydrate metabolic process Source: RGD
  • regulation of insulin secretion Source: Reactome
  • regulation of lipid metabolic process Source: RGD
  • response to L-arginine Source: RGD
  • response to starvation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiR-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2668. Gcg.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: RGD
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
PeptideiPRO_000001130321 – 89GlicentinBy similarityAdd BLAST69
PeptideiPRO_000001130421 – 50Glicentin-related polypeptideBy similarityAdd BLAST30
PeptideiPRO_000001130553 – 89OxyntomodulinAdd BLAST37
PeptideiPRO_000001130653 – 81GlucagonBy similarityAdd BLAST29
PropeptideiPRO_000001130784 – 89By similarity6
PeptideiPRO_000001130892 – 128Glucagon-like peptide 1By similarityAdd BLAST37
PeptideiPRO_000001130998 – 128Glucagon-like peptide 1(7-37)By similarityAdd BLAST31
PeptideiPRO_000001131098 – 127Glucagon-like peptide 1(7-36)By similarityAdd BLAST30
PropeptideiPRO_0000011311131 – 145By similarityAdd BLAST15
PeptideiPRO_0000011312146 – 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 residuei152PhosphoserineCombined sources1

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.1 Publication

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

PaxDbiP06883.
PRIDEiP06883.

PTM databases

iPTMnetiP06883.
PhosphoSitePlusiP06883.

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.1 Publication

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.

Interactioni

GO - Molecular functioni

  • glucagon receptor binding Source: RGD
  • hormone activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007356.

Structurei

3D structure databases

ProteinModelPortaliP06883.
SMRiP06883.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glucagon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IKZ8. Eukaryota.
ENOG4111VKC. LUCA.
HOGENOMiHOG000231876.
HOVERGENiHBG003010.
InParanoidiP06883.
PhylomeDBiP06883.

Family and domain databases

InterProiIPR015550. Glucagon.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERiPTHR11418:SF0. PTHR11418:SF0. 1 hit.
PfamiPF00123. Hormone_2. 3 hits.
[Graphical view]
PRINTSiPR00275. GLUCAGON.
SMARTiSM00070. GLUCA. 3 hits.
[Graphical view]
PROSITEiPS00260. GLUCAGON. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTVYIVAGL FVMLVQGSWQ HAPQDTEENA RSFPASQTEP LEDPDQINED
60 70 80 90 100
KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE
110 120 130 140 150
GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVAIAE ELGRRHADGS
160 170 180
FSDEMNTILD NLATRDFINW LIQTKITDKK
Length:180
Mass (Da):20,846
Last modified:January 1, 1988 - v1
Checksum:i76931409D03C7978
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02813
, K02809, K02810, K02811, K02812 Genomic DNA. Translation: AAA41235.1.
PIRiA22655. GCRT.
UniGeneiRn.54383.

Genome annotation databases

UCSCiRGD:2668. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02813
, K02809, K02810, K02811, K02812 Genomic DNA. Translation: AAA41235.1.
PIRiA22655. GCRT.
UniGeneiRn.54383.

3D structure databases

ProteinModelPortaliP06883.
SMRiP06883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007356.

PTM databases

iPTMnetiP06883.
PhosphoSitePlusiP06883.

Proteomic databases

PaxDbiP06883.
PRIDEiP06883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2668. rat.

Organism-specific databases

RGDi2668. Gcg.

Phylogenomic databases

eggNOGiENOG410IKZ8. Eukaryota.
ENOG4111VKC. LUCA.
HOGENOMiHOG000231876.
HOVERGENiHBG003010.
InParanoidiP06883.
PhylomeDBiP06883.

Enzyme and pathway databases

ReactomeiR-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Miscellaneous databases

PROiP06883.

Family and domain databases

InterProiIPR015550. Glucagon.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERiPTHR11418:SF0. PTHR11418:SF0. 1 hit.
PfamiPF00123. Hormone_2. 3 hits.
[Graphical view]
PRINTSiPR00275. GLUCAGON.
SMARTiSM00070. GLUCA. 3 hits.
[Graphical view]
PROSITEiPS00260. GLUCAGON. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLUC_RAT
AccessioniPrimary (citable) accession number: P06883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 2, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.