Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00292HCP repeats signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00292
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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