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P55095 (GLUC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucagon

Cleaved into the following 8 chains:

  1. Glicentin
  2. Glicentin-related polypeptide
    Short name=GRPP
  3. Oxyntomodulin
    Short name=OXM
    Short name=OXY
  4. Glucagon
  5. Glucagon-like peptide 1
    Short name=GLP-1
  6. Glucagon-like peptide 1(7-37)
    Short name=GLP-1(7-37)
  7. Glucagon-like peptide 1(7-36)
    Short name=GLP-1(7-36)
  8. Glucagon-like peptide 2
    Short name=GLP-2
Gene names
Name:Gcg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.5

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. Ref.5

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. Ref.5

Oxyntomodulin significantly reduces food intake By similarity. Ref.5

Glicentin may modulate gastric acid secretion and gastro-pyloro-duodenal activity. Ref.5

Subcellular location

Secreted.

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.

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. Ref.6 Ref.7

Sequence similarities

Belongs to the glucagon family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Cleavage on pair of basic residues
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of apoptotic process

Inferred from direct assay PubMed 19915011. Source: UniProtKB

negative regulation of execution phase of apoptosis

Inferred from direct assay PubMed 19915011. Source: MGI

negative regulation of intrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 19915011. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 19915011PubMed 19915011. Source: UniProtKB

positive regulation of cAMP biosynthetic process

Inferred from direct assay PubMed 19915011. Source: UniProtKB

positive regulation of calcium ion import

Inferred from direct assay PubMed 19915011. Source: UniProtKB

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from direct assay PubMed 19915011. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 19915011PubMed 19915011. Source: UniProtKB

positive regulation of peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 19915011. Source: UniProtKB

positive regulation of protein binding

Inferred from direct assay PubMed 19915011PubMed 19915011. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from direct assay PubMed 19915011. Source: UniProtKB

protein kinase A signaling

Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB

regulation of insulin secretion

Inferred from direct assay PubMed 14736883. Source: MGI

response to starvation

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19915011. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 17693256. Source: MGI

secretory granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionglucagon receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

hormone activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Peptide21 – 8969Glicentin By similarity
PRO_0000011273
Peptide21 – 5030Glicentin-related polypeptide By similarity
PRO_0000011274
Peptide53 – 8937Oxyntomodulin By similarity
PRO_0000011275
Peptide53 – 8129Glucagon By similarity
PRO_0000011276
Propeptide84 – 896 By similarity
PRO_0000011277
Peptide92 – 12837Glucagon-like peptide 1 By similarity
PRO_0000011278
Peptide98 – 12831Glucagon-like peptide 1(7-37) By similarity
PRO_0000011279
Peptide98 – 12730Glucagon-like peptide 1(7-36) By similarity
PRO_0000011280
Propeptide131 – 14515 By similarity
PRO_0000011281
Peptide146 – 17833Glucagon-like peptide 2 By similarity
PRO_0000011282

Sites

Site52 – 532Cleavage; by PCSK2
Site83 – 842Cleavage; by PCSK1 and PCSK2
Site91 – 922Cleavage; by PCSK1
Site97 – 982Cleavage; by PCSK1
Site130 – 1312Cleavage; by PCSK1
Site145 – 1462Cleavage; by PCSK1

Amino acid modifications

Modified residue1271Arginine amide By similarity

Sequences

Sequence LengthMass (Da)Tools
P55095 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 595AA6DD9A589950

FASTA18020,906
        10         20         30         40         50         60 
MKTIYFVAGL LIMLVQGSWQ HALQDTEENP RSFPASQTEA HEDPDEMNED KRHSQGTFTS 

        70         80         90        100        110        120 
DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE GTFTSDVSSY LEGQAAKEFI 

       130        140        150        160        170        180 
AWLVKGRGRR DFPEEVAIAE ELGRRHADGS FSDEMSTILD NLATRDFINW LIQTKITDKK 

« Hide

References

« Hide 'large scale' references
[1]"Processing of mouse proglucagon by recombinant prohormone convertase 1 and immunopurified prohormone convertase 2 in vitro."
Rothenberg M.E., Eilertson C.D., Klein K., Zhou Y., Linberg I., McDonald J.K., Mackin R.B., Noe B.D.
J. Biol. Chem. 270:10136-10146(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreatic islet.
[2]"Mouse glucagon full length cDNA."
Shamsadin R., Knepel W.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
[5]"GLP-1 and GLP-1(7-36) amide: influences on basal and stimulated insulin and glucagon secretion in the mouse."
Fridolf T., Bottcher G., Sundler F., Ahren B.
Pancreas 6:208-215(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF GLP-1 AND GLP-1(7-36) AMIDE.
[6]"Role of the prohormone convertase PC3 in the processing of proglucagon to glucagon-like peptide 1."
Rouille Y., Kantengwa S., Irminger J.C., Halban P.A.
J. Biol. Chem. 272:32810-32816(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING BY PCSK1.
[7]"Severe defect in proglucagon processing in islet A-cells of prohormone convertase 2 null mice."
Furuta M., Zhou A., Webb G., Carroll R., Ravazzola M., Orci L., Steiner D.F.
J. Biol. Chem. 276:27197-27202(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING BY PCSK2.
[8]"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.
[9]"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.
[10]"Glucagon-like peptide 2."
Drucker D.J.
Trends Endocrinol. Metab. 10:153-156(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"The glucagon-like peptides."
Kieffer T.J., Habener J.F.
Endocr. Rev. 20:876-913(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46845 mRNA. Translation: CAA86902.1.
AF276754 mRNA. Translation: AAK96898.1.
AK007911 mRNA. Translation: BAB25344.1.
AK148544 mRNA. Translation: BAE28612.1.
BC012975 mRNA. Translation: AAH12975.1.
PIRA57294.
RefSeqNP_032126.1. NM_008100.3.
UniGeneMm.45494.

3D structure databases

ProteinModelPortalP55095.
SMRP55095. Positions 53-81, 98-127, 146-178.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP55095.

Proteomic databases

PaxDbP55095.
PRIDEP55095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102733; ENSMUSP00000099794; ENSMUSG00000000394.
GeneID14526.
KEGGmmu:14526.
UCSCuc008jvj.1. mouse.

Organism-specific databases

CTD2641.
MGIMGI:95674. Gcg.

Phylogenomic databases

eggNOGNOG42743.
GeneTreeENSGT00390000005372.
HOGENOMHOG000231876.
HOVERGENHBG003010.
InParanoidP55095.
KOK05259.
OMARNKNNIA.
OrthoDBEOG7WMCM1.
PhylomeDBP55095.
TreeFamTF332333.

Enzyme and pathway databases

ReactomeREACT_93132. Metabolism of proteins.

Gene expression databases

BgeeP55095.
CleanExMM_GCG.
GenevestigatorP55095.

Family and domain databases

InterProIPR015550. Glucagon-like.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERPTHR11418. PTHR11418. 1 hit.
PfamPF00123. Hormone_2. 3 hits.
[Graphical view]
PRINTSPR00275. GLUCAGON.
SMARTSM00070. GLUCA. 3 hits.
[Graphical view]
PROSITEPS00260. GLUCAGON. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGCG. mouse.
NextBio286168.
PMAP-CutDBP55095.
PROP55095.
SOURCESearch...

Entry information

Entry nameGLUC_MOUSE
AccessionPrimary (citable) accession number: P55095
Secondary accession number(s): Q3UFE9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot