Kobayashi T, Takasaki Y, Takagi T, Konishi K
Eur J Biochem. 1984 Oct 15;144(2):401-8. doi: 10.1111/j.1432-1033.1984.tb08478.x.
The amino acid sequence of sarcoplasmic calcium-binding protein obtained from sandworm (Perinereis vancaurica tetradentata) has been determined. It is composed of 174 amino acid residues, its N-terminus is blocked by an acetyl group and the relative molecular mass is calculated to be 19556. From the results of amino acid sequence, it has three EF-hand-type calcium-binding sites. The positions of calcium-binding sites could be easily predicted by its hydropathy profile. Amino acid sequence homology between sarcoplasmic calcium-binding protein from different species is between 14-20%, thus it is not such a conservative protein.
已确定从沙蚕（Perinereis vancaurica tetradentata）获得的肌浆钙结合蛋白的氨基酸序列。它由174个氨基酸残基组成，其N端被乙酰基封闭，计算相对分子质量为19556。根据氨基酸序列结果，它有三个EF手型钙结合位点。通过其亲水性图谱可以很容易地预测钙结合位点的位置。不同物种的肌浆钙结合蛋白之间的氨基酸序列同源性在14%-20%之间，因此它不是一种非常保守的蛋白质。
