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PROSITE documentation PDOC51647
Kininogen-type cystatin domain profile


Description

The cystatin superfamily consists of a large group of cystatin domain-containing proteins, most of which are reversible and tight-binding inhibitors of the papain (C1) and legumain (C13) families of cysteine proteases [1,E1]. Kininogens are multifunctional and multidomain glycoproteins related to cystatins. Kininogens ubiquitously exist in vertebrates, including mammals, birds, amphibians, and fishes. They vary extremely in both structure and function among different taxa of animals, in particular between mammals and amphibians. Kininogens contain a bradykinin domain and one (in lampreys), two (in fishes) or three (in mammals, birds, and amphibians) cystatin domain(s). Although mammalian kininogens harbor three cystatin domains only two of them are tight-binding inhibitors of cysteine cathepsins, which belong to the papain-like cysteine proteases. A Q-x-V-x-G motif is the canonical binding site for cysteine proteinases in mammals [2,3,4].

The profile we developed cover the entire kininogen-type cystatin domain.

Last update:

June 2012 / First entry.

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Technical section

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

CYSTATIN_KININOGEN, PS51647; Kininogen-type cystatin domain profile  (MATRIX)


References

1AuthorsKordis D. Turk V.
TitlePhylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes.
SourceBMC Evol. Biol. 9:266-266(2009).
PubMed ID19919722
DOI10.1186/1471-2148-9-266

2AuthorsZhou L. Li-Ling J. Huang H. Ma F. Li Q.
TitlePhylogenetic analysis of vertebrate kininogen genes.
SourceGenomics 91:129-141(2008).
PubMed ID18096361
DOI10.1016/j.ygeno.2007.10.007

3AuthorsZhou L. Liu X. Jin P. Li Q.
TitleCloning of the kininogen gene from Lampetra japonica provides insights into its phylogeny in vertebrates.
SourceJ. Genet. Genomics 36:109-115(2009).
PubMed ID19232309
DOI10.1016/S1673-8527(08)60097-1

4AuthorsLalmanach G. Naudin C. Lecaille F. Fritz H.
TitleKininogens: More than cysteine protease inhibitors and kinin precursors.
SourceBiochimie 92:1568-1579(2010).
PubMed ID20346387
DOI10.1016/j.biochi.2010.03.011

E1Titlehttps://www.ebi.ac.uk/merops/cgi-bin/pepsum?id=LI25-002;type=I



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