Ojima T, Tanaka H, Nishita K
Department of Chemistry, Faculty of Fisheries, Hokkaido University, Japan.
Arch Biochem Biophys. 1994 Jun;311(2):272-6. doi: 10.1006/abbi.1994.1237.
A cDNA clone encoding troponin C of Akazara scallop (Chlamys nipponensis akazara) striated adductor muscle was isolated and sequenced. The cDNA is composed of 1987 bp and has an open reading frame of 462 bp at nucleotide positions 12-473. The amino acid sequence deduced from the cDNA showed 89% homology with that of Ezo-giant scallop (Patinopecten yessoensis) troponin C (K. Nishita, H. Tanaka, and T. Ojima, 1994, J. Biol. Chem. 269, 3464-3468). However, it showed lower homology with those of troponin Cs from the other invertebrates (35-40%) and vertebrates (30%). A single functional Ca(2+)-binding site was found in site IV of the four potential Ca(2+)-binding sites as in the case of Ezo-giant scallop troponin C. Three amino acid deletions in the central D/E helix were required to align the scallop sequences with those of other troponin Cs.
分离并测序了编码赤坂扇贝（Chlamys nipponensis akazara）横纹肌内收肌肌钙蛋白C的cDNA克隆。该cDNA由1987个碱基对组成，在核苷酸位置12 - 473处有一个462个碱基对的开放阅读框。从该cDNA推导的氨基酸序列与虾夷扇贝（Patinopecten yessoensis）肌钙蛋白C的氨基酸序列显示出89%的同源性（K. Nishita、H. Tanaka和T. Ojima，1994年，《生物化学杂志》269卷，3464 - 3468页）。然而，它与其他无脊椎动物（35 - 40%）和脊椎动物（30%）的肌钙蛋白C的同源性较低。与虾夷扇贝肌钙蛋白C的情况一样，在四个潜在的Ca(2+)结合位点的位点IV中发现了一个单一的功能性Ca(2+)结合位点。为了使扇贝序列与其他肌钙蛋白C的序列对齐，需要在中央D/E螺旋中进行三个氨基酸的缺失。
