PROSITE documentation PDOC00292HCP 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.
Last update:April 1990 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Hofmann S.L. Goldstein J.L. Orth K. Moomaw C.R. Slaughter C.A. Brown M.S. |
| Title | Molecular cloning of a histidine-rich Ca2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements. | |
| Source | J. Biol. Chem. 264:18083-18090(1989). | |
| PubMed ID | 2808365 |
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