{PDOC51647}
{PS51647; CYSTATIN_KININOGEN}
{BEGIN}
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* Kininogen-type cystatin domain profile *
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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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2012 / First entry.

[ 1] Kordis D., Turk V.
     "Phylogenomic analysis of the cystatin superfamily in eukaryotes and
     prokaryotes."
     BMC Evol. Biol. 9:266-266(2009).
     PubMed=19919722; DOI=10.1186/1471-2148-9-266
[ 2] Zhou L., Li-Ling J., Huang H., Ma F., Li Q.
     "Phylogenetic analysis of vertebrate kininogen genes."
     Genomics 91:129-141(2008).
     PubMed=18096361; DOI=10.1016/j.ygeno.2007.10.007
[ 3] Zhou L., Liu X., Jin P., Li Q.
     "Cloning of the kininogen gene from Lampetra japonica provides
     insights into its phylogeny in vertebrates."
     J. Genet. Genomics 36:109-115(2009).
     PubMed=19232309; DOI=10.1016/S1673-8527(08)60097-1
[ 4] Lalmanach G., Naudin C., Lecaille F., Fritz H.
     "Kininogens: More than cysteine protease inhibitors and kinin
     precursors."
     Biochimie 92:1568-1579(2010).
     PubMed=20346387; DOI=10.1016/j.biochi.2010.03.011
[E1] https://www.ebi.ac.uk/merops/cgi-bin/pepsum?id=LI25-002;type=I

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