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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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.
Amos Bairoch

PROSITE documentation PDOC00675
Calsequestrin signatures


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00675

Description

Calsequestrin is a moderate-affinity, high-capacity calcium-binding protein of cardiac and skeletal muscle [1], where it is located in the lumenal space of the sarcoplasmic reticulum terminal cisternae. Calsequestrin acts as a calcium buffer and plays an important role in the muscle excitation-contraction coupling. It is a highly acidic protein of about 400 amino acid residues that binds more than 40 moles of calcium per mole of protein. There are at least two different forms of calsequestrin: one which is expressed in cardiac muscles and another in skeletal muscles. Both forms have highly similar sequences.

We have developed two signature sequences, the first one corresponds to the N-terminus of the mature protein; the second is located just in front of the C-terminus of the protein which is composed of a highly acidic tail of variable length.

Last update:

October 1993 / First entry.

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Technical section

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

CALSEQUESTRIN_1, PS00863; Calsequestrin signature 1  (PATTERN)

CALSEQUESTRIN_2, PS00864; Calsequestrin signature 2  (PATTERN)


Reference

1AuthorsTreves S. Vilsen B. Chiozzi P. Andersen J.P. Zorzato F.
TitleMolecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin.
SourceBiochem. J. 283:767-772(1992).
PubMed ID1375450



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