Amino acid sequence of a sarcoplasmic calcium-binding protein from the sandworm Nereis diversicolor.

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.