Strasser P, Gimona M, Moessler H, Herzog M, Small J V
Institute of Molecular Biology, Austrian Academy of Sciences, Salzburg.
FEBS Lett. 1993 Sep 6;330(1):13-8. doi: 10.1016/0014-5793(93)80909-e.
Calponin is a smooth muscle specific, actin-, tropomyosin- and calmodulin-binding protein thought to be involved in some way in the regulation or modulation of contraction. Here we describe the cloning and bacterial expression of two calponin species from murine and porcine smooth muscle tissues. Primary and secondary structural analyses of the deduced amino acid sequences revealed a high degree of homology to avian calponin with the exception of a short and variable C-terminal segment. The sequence data demonstrate that the two mammalian calponin variants do not arise via alternative splicing but are encoded by different genes.
钙调蛋白是一种平滑肌特异性、与肌动蛋白、原肌球蛋白和钙调蛋白结合的蛋白质,被认为在某种程度上参与收缩的调节或调控。在此,我们描述了从小鼠和猪平滑肌组织中克隆和细菌表达两种钙调蛋白的过程。对推导的氨基酸序列进行的一级和二级结构分析表明,除了一个短的可变C末端片段外,与禽类钙调蛋白具有高度同源性。序列数据表明,这两种哺乳动物钙调蛋白变体并非通过可变剪接产生,而是由不同基因编码。