Amino acid sequence of a sarcoplasmic calcium-binding protein from the sandworm Nereis diversicolor.
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 263, Issue: 30, Page: 15378-15385
1988
- 3Citations
- 6Captures
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Metrics Details
- Citations3
- Citation Indexes3
- CrossRef3
- Captures6
- Readers6
Abstract Description
Muscles of invertebrate species contain abundant quantities of soluble, sarcoplasmic, high affinity Ca2+-binding proteins (SCBPs). The SCBPs belong to the calmodulin superfamily and contain four homologous domains (I-IV) which arose by reduplication of a gene for a small ancestral protein. We have determined the amino acid sequence of the SCBP from the sandworm Nereis diversicolor. This protein is the only SCBP which has been crystallized in a form suitable for three-dimensional structure determination by high-resolution x-ray analysis (Babu, Y. S., Cox, J. A., and Cook, W. J. (1987) J. Biol. Chem. 262, 11184-11185). N. diversicolor SCBP is a single polypeptide chain of 174 amino acids, including single residues of glutamine and histidine, 2 tyrosines, and 3 tryptophans. It is devoid of cysteine and has an acetylated amino terminus, a calculated Mr of 19,485, and a net charge of -13 at neutral pH. There was no evidence for heterogeneity in the sequence. Probable Ca2+-binding sites were recognized in domains I, III, and IV. Comparison with other available invertebrate SCBP sequences shows an unusually high degree of variability among these proteins, with only 9 residues common to all species.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819375994; http://dx.doi.org/10.1016/s0021-9258(19)37599-4; https://linkinghub.elsevier.com/retrieve/pii/S0021925819375994; https://api.elsevier.com/content/article/PII:S0021925819375994?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:S0021925819375994?httpAccept=text/plain; https://dul.usage.elsevier.com/doi/; http://dx.doi.org/10.1016/s0021-9258%2819%2937599-4; https://dx.doi.org/10.1016/s0021-9258%2819%2937599-4
Elsevier BV
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