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P06883

- GLUC_RAT

UniProt

P06883 - GLUC_RAT

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Protein
Glucagon
Gene
Gcg
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei52 – 532Cleavage; by PCSK2 By similarity
Sitei83 – 842Cleavage; by PCSK1 and PCSK2 By similarity
Sitei91 – 922Cleavage; by PCSK1 By similarity
Sitei97 – 982Cleavage; by PCSK1 By similarity
Sitei130 – 1312Cleavage; by PCSK1 By similarity
Sitei145 – 1462Cleavage; by PCSK1 By similarity

GO - Molecular functioni

  1. glucagon receptor binding Source: RGD
  2. hormone activity Source: RGD
Complete GO annotation...

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RGD
  2. negative regulation of apoptotic process Source: RefGenome
  3. negative regulation of appetite Source: RGD
  4. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: RefGenome
  5. protein kinase A signaling Source: RefGenome
  6. protein metabolic process Source: RGD
  7. regulation of carbohydrate metabolic process Source: RGD
  8. regulation of lipid metabolic process Source: RGD
  9. response to starvation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hormone

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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2668. Gcg.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020
Add
BLAST
Peptidei21 – 8969Glicentin By similarity
PRO_0000011303Add
BLAST
Peptidei21 – 5030Glicentin-related polypeptide By similarity
PRO_0000011304Add
BLAST
Peptidei53 – 8937Oxyntomodulin1 Publication
PRO_0000011305Add
BLAST
Peptidei53 – 8129Glucagon By similarity
PRO_0000011306Add
BLAST
Propeptidei84 – 896 By similarity
PRO_0000011307
Peptidei92 – 12837Glucagon-like peptide 1 By similarity
PRO_0000011308Add
BLAST
Peptidei98 – 12831Glucagon-like peptide 1(7-37) By similarity
PRO_0000011309Add
BLAST
Peptidei98 – 12730Glucagon-like peptide 1(7-36) By similarity
PRO_0000011310Add
BLAST
Propeptidei131 – 14515 By similarity
PRO_0000011311Add
BLAST
Peptidei146 – 17833Glucagon-like peptide 2 By similarity
PRO_0000011312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271Arginine amide By similarity

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

Keywords - PTMi

Amidation, Cleavage on pair of basic residues

Proteomic databases

PRIDEiP06883.

PTM databases

PhosphoSiteiP06883.

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.

Gene expression databases

GenevestigatoriP06883.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007356.

Structurei

3D structure databases

ProteinModelPortaliP06883.
SMRiP06883. Positions 53-81, 98-127.

Family & Domainsi

Sequence similaritiesi

Belongs to the glucagon family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42743.
HOGENOMiHOG000231876.
HOVERGENiHBG003010.
InParanoidiP06883.
PhylomeDBiP06883.

Family and domain databases

InterProiIPR015550. Glucagon-like.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERiPTHR11418. PTHR11418. 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

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MKTVYIVAGL FVMLVQGSWQ HAPQDTEENA RSFPASQTEP LEDPDQINED    50
KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE 100
GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVAIAE ELGRRHADGS 150
FSDEMNTILD NLATRDFINW LIQTKITDKK 180
Length:180
Mass (Da):20,846
Last modified:January 1, 1988 - v1
Checksum:i76931409D03C7978
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
K02813
, K02809 , K02810 , K02811 , K02812 Genomic DNA. Translation: AAA41235.1 .
PIRi A22655. GCRT.
UniGenei Rn.54383.

3D structure databases

ProteinModelPortali P06883.
SMRi P06883. Positions 53-81, 98-127.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000007356.

PTM databases

PhosphoSitei P06883.

Proteomic databases

PRIDEi P06883.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:2668. rat.

Organism-specific databases

RGDi 2668. Gcg.

Phylogenomic databases

eggNOGi NOG42743.
HOGENOMi HOG000231876.
HOVERGENi HBG003010.
InParanoidi P06883.
PhylomeDBi P06883.

Miscellaneous databases

NextBioi 13948569.
PROi P06883.

Gene expression databases

Genevestigatori P06883.

Family and domain databases

InterProi IPR015550. Glucagon-like.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view ]
PANTHERi PTHR11418. PTHR11418. 1 hit.
Pfami PF00123. Hormone_2. 3 hits.
[Graphical view ]
PRINTSi PR00275. GLUCAGON.
SMARTi SM00070. GLUCA. 3 hits.
[Graphical view ]
PROSITEi PS00260. GLUCAGON. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Glucagon gene sequence. Four of six exons encode separate functional domains of rat pre-proglucagon."
    Heinrich G., Gros P., Habener J.F.
    J. Biol. Chem. 259:14082-14087(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Pre-proglucagon messenger ribonucleic acid: nucleotide and encoded amino acid sequences of the rat pancreatic complementary deoxyribonucleic acid."
    Heinrich G., Gros P., Lund P.K., Bentley R.C., Habener J.F.
    Endocrinology 115:2176-2181(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing."
    Mojsov S., Heinrich G., Wilson I.B., Ravazzola M., Orci L., Habener J.F.
    J. Biol. Chem. 261:11880-11889(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: PROTEIN SEQUENCE OF 53-89.
  5. Cited for: FUNCTION OF OXYNTOMODULIN.
  6. "Role of prohormone convertases in the tissue-specific processing of proglucagon."
    Dhanvantari S., Seidah N.G., Brubaker P.L.
    Mol. Endocrinol. 10:342-355(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING BY PCSK1 AND PCSK2.
  7. "Both amidated and nonamidated forms of glucagon-like peptide I are synthesized in the rat intestine and the pancreas."
    Mojsov S., Kopczynski M.G., Habener J.F.
    J. Biol. Chem. 265:8001-8008(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Direct and indirect mechanisms regulating secretion of glucagon-like peptide-1 and glucagon-like peptide-2."
    Brubaker P.L., Anini Y.
    Can. J. Physiol. Pharmacol. 81:1005-1012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis."
    Drucker D.J.
    Mol. Endocrinol. 17:161-171(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Glucagon and regulation of glucose metabolism."
    Jiang G., Zhang B.B.
    Am. J. Physiol. 284:E671-E678(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. Cited for: REVIEW.
  12. Cited for: REVIEW.

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: September 3, 2014
This is version 114 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

External Data

Dasty 3

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