Takagi T, Nojiri M, Konishi K, Maruyama K, Nonomura Y
FEBS Lett. 1986 May 26;201(1):41-5. doi: 10.1016/0014-5793(86)80567-1.
The amino acid sequence of vitamin D-dependent calcium-binding protein from bovine cerebellum has been determined. It is composed of 260 amino acid residues and its N-terminus is acetylated. The molecular mass is calculated to be 29 851 Da. The presence of six calcium-binding sites (I-VI) has been proposed, two of them (sites II and VI) have lost their calcium-binding function through amino acid replacements, and the other four are able to bind calcium. Six calcium-binding domains are supposed to be derived from two gene duplications of the two ancestral calcium-binding domains. In comparison with the sequence of chick intestinal calcium-binding protein deduced from a cDNA sequence [(1985) Nucleic Acids Res. 13, 8867-8881], the bovine calcium-binding protein is two amino acid residues shorter at the N-terminus and the other parts show 78.5% identity.
已确定来自牛小脑的维生素D依赖性钙结合蛋白的氨基酸序列。它由260个氨基酸残基组成，其N端被乙酰化。计算出的分子量为29851道尔顿。已提出存在六个钙结合位点（I - VI），其中两个（位点II和VI）通过氨基酸替换失去了钙结合功能，另外四个能够结合钙。六个钙结合结构域被认为源自两个祖先钙结合结构域的两次基因复制。与从cDNA序列推导的鸡肠钙结合蛋白的序列相比[（1985年）核酸研究。13, 8867 - 8881]，牛钙结合蛋白在N端短两个氨基酸残基，其他部分显示78.5%的同一性。
