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PROSITE documentation PDOC00232 [for PROSITE entry PS00259]

Gastrin / cholecystokinin family signature





Description

Gastrin and cholecystokinin (CCK) [1,2] are structurally and functionally related peptide hormones that function as hormonal regulators of various digestive processes and feeding behaviors . They are known to induce gastric secretion, stimulate pancreatic secretion, increase blood circulation and water secretion in the stomach and intestine, and stimulate smooth muscle contraction. Originally found in the gut, these hormones have since been shown to be present in various parts of the nervous system. Like many other active peptides they are synthesized as larger protein precursors that are enzymatically converted to their mature forms. They are found in several molecular forms due to tissue-specific post-translational processing. A number of other peptides are known to belong to the same family:

  • Caerulein [3], an amphibian skin peptide, with a biological activity similar to that of CCK or gastrin. There are different types of caerulein precursors [4] in which a single or up to four copies of the peptide are present.
  • Leukosulfakinin I and II (LSK) [5,6] are peptides, isolated from cockroach, that change the frequency and amplitude of contractions of the hindgut.
  • Drosulfakinins I and II [7] are putative CCK-homologs from Drosophila. Those two peptides are part of a precursor sequence that was isolated using a probe based on the sequence of CCK and LSK.
  • A chicken antrum peptide [8] which is a potent stimulus of avian gastric acid but not of pancreatic secretion.
  • Cionin [9], a neuropeptide from the protochordate Ciona intestinalis.

The biological activity of gastrin and CCK is associated with the last five C-terminal residues. One or two positions downstream, there is a conserved sulfated tyrosine residue. The signature pattern developed for this family of peptides includes the biologically active C-terminal sequence as well as the sulfated tyrosine.

Note:

The residues in positions 4 and 6 of the pattern are respectively Trp and Asp in vertebrate peptides, and His and Arg in insect peptides.

Last update:

April 1990 / Text revised.

Technical section

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

GASTRIN, PS00259; Gastrin / cholecystokinin family signature  (PATTERN)


References

1SourceConcise Encyclopedia Biochemistry, Second Edition, Walter de Gruyter, Berlin New-York (1988).

2TitleCholecystokinin. Ann. N.Y. Acad. Sci. 448(1985).

3AuthorsErspamer V. Falconieri Erspamer G. Mazzanti G. Endean R.
SourceComp. Biochem. Physiol. 77C:99-108(1984).

4AuthorsRichter K. Egger R. Kreil G.
TitleSequence of preprocaerulein cDNAs cloned from skin of Xenopus laevis. A small family of precursors containing one, three, or four copies of the final product.
SourceJ. Biol. Chem. 261:3676-3680(1986).
PubMed ID3753978

5AuthorsNachman R.J. Holman G.M. Haddon W.F. Ling N.
TitleLeucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin.
SourceScience 234:71-73(1986).
PubMed ID3749893

6AuthorsNachman R.J. Holman G.M. Cook B.J. Haddon W.F. Ling N.
TitleLeucosulfakinin-II, a blocked sulfated insect neuropeptide with homology to cholecystokinin and gastrin.
SourceBiochem. Biophys. Res. Commun. 140:357-364(1986).
PubMed ID3778455

7AuthorsNichols R. Schneuwly S.A. Dixon J.E.
TitleIdentification and characterization of a Drosophila homologue to the vertebrate neuropeptide cholecystokinin.
SourceJ. Biol. Chem. 263:12167-12170(1988).
PubMed ID2842322

8AuthorsDimaline R. Young J. Gregory H.
TitleIsolation from chicken antrum, and primary amino acid sequence of a novel 36-residue peptide of the gastrin/CCK family.
SourceFEBS Lett. 205:318-322(1986).
PubMed ID3743781

9AuthorsJohnsen A.H. Rehfeld J.F.
TitleCionin: a disulfotyrosyl hybrid of cholecystokinin and gastrin from the neural ganglion of the protochordate Ciona intestinalis.
SourceJ. Biol. Chem. 265:3054-3058(1990).
PubMed ID2303439



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