PROSITE documentation PDOC00233
Glucagon / GIP / secretin / VIP family signature


A number of polypeptidic hormones, mainly expressed in the intestine or the pancreas, belong to a group of structurally related peptides [1,2]. Members of this family are:

  • Glucagon, which promotes hydrolysis of glycogen and lipids, and raises the blood sugar level.
  • Glucagon-like peptide 1 (GLP-1), a peptide of unknown function processed from the same precursor protein as that of glucagon.
  • Glucagon-like peptide 2 (GLP-2), a peptide of unknown function also processed from the glucagon precursor protein but which, in contrast to GLP-1, is only found in mammals.
  • Gastric inhibitory polypeptide (GIP), which is a potent stimulator of insulin secretion and a relatively poor inhibitor of gastric acid secretion.
  • Secretin, which stimulates formation of NaHCO(3)-rich pancreatic juice and secretion of NaHCO(3)-rich bile as well as inhibiting HCl production by the stomach.
  • Vasoactive intestinal peptide (VIP), which causes vasodilatation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes some smooth muscles.
  • Peptide PHI-27, a vasodilator peptide which is coded by the same precursor protein as that of VIP.
  • Growth hormone-releasing factor (GRF) (also known as somatoliberin), which is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.
  • Pituitary adenylate cyclase activating polypeptide (PACAP) [3].
  • Helospectin (exendin-1), helodermin (exendin-2), exendin-3, and exendin-4 from the venom of gila monsters. The exendins are peptides with a VIP/ secretin biological activity [4].
  • A peptide produced by the X-cells of the islets of ratfish pancreas [5].

As a pattern for this family of peptides (which are from 30 to 45 amino acid residues long), we used the more or less conserved first ten positions of the N-terminal as well as a conserved hydrophobic residue in position 23.

Last update:

December 2004 / Pattern and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

GLUCAGON, PS00260; Glucagon / GIP / secretin / VIP family signature  (PATTERN)


1AuthorsMutt V.
TitleVasoactive intestinal polypeptide and related peptides. Isolation and chemistry.
SourceAnn. N.Y. Acad. Sci. 527:1-19(1988).
PubMed ID3133967

2AuthorsBataille D. Blache P. Mercier F. Jarrousse C. Kervran A. Dufour M. Mangeat P. Dubrasquet M. Mallat A. Lotersztajn S. Pavoine C. Pecker F.
SourceAnn. N.Y. Acad. Sci. 527:169-185(1988).

3AuthorsMiyata A. Arimura A. Dahl R.R. Minamino N. Uehara A. Jiang L. Culler M.D. Coy D.H.
TitleIsolation of a novel 38 residue-hypothalamic polypeptide which stimulates adenylate cyclase in pituitary cells.
SourceBiochem. Biophys. Res. Commun. 164:567-574(1989).
PubMed ID2803320

4AuthorsEng J. Kleinman W.A. Singh L. Singh G. Raufman J.-P.
TitleIsolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas.
SourceJ. Biol. Chem. 267:7402-7405(1992).
PubMed ID1313797

5AuthorsConlon J.M. Dafgard E. Falkmer S. Thim L.
TitleA glucagon-like peptide, structurally related to mammalian oxyntomodulin, from the pancreas of a holocephalan fish, Hydrolagus colliei.
SourceBiochem. J. 245:851-855(1987).
PubMed ID3311036

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