{PDOC00292}
{PS00328; HCP}
{BEGIN}
*************************
* HCP repeats signature *
*************************

The histidine-rich calcium-binding protein (HCP) of sarcoplasmic reticulum [1]
may play a role in the  regulation of  calcium sequestration or release in the
SR of skeletal and cardiac muscle. This protein is very acidic (31% of Asp and
Glu) and rich in histidine (13%).  The sequence  of  HCP  contains  10  tandem
repeats of  a 26 to 29 amino acid residues domain.  This domain starts with an
invariant hexapeptide (HRHRGH),  followed by a stretch of acidic residues. The
end of the domain consist of an almost invariant nonapeptide (STESDRHQA).  The
highly acidic  central  cores of each repeat  are  likely  to  constitute  the
calcium-binding sites of HCP.

The pattern we have developed comprises  the beginning  of the domain and part
of the central acidic stretch.

-Consensus pattern: H-R-H-R-G-H-x(2)-[DE](7)
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 1990 / First entry.

[ 1] Hofmann S.L., Goldstein J.L., Orth K., Moomaw C.R., Slaughter C.A.,
     Brown M.S.
     "Molecular cloning of a histidine-rich Ca2+-binding protein of
     sarcoplasmic reticulum that contains highly conserved repeated
     elements."
     J. Biol. Chem. 264:18083-18090(1989).
     PubMed=2808365

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}