Yorifuji T, Lemna W K, Ballard C F, Rosenbloom C L, Rozmahel R, Plavsic N, Tsui L C, Beaudet A L
Institute for Molecular Genetics, Baylor College of Medicine, Houston, Texas 77030.
Genomics. 1991 Jul;10(3):547-50. doi: 10.1016/0888-7543(91)90434-g.
We have cloned the mouse homolog of the human cystic fibrosis transmembrane conductance regulator (CFTR) using clones isolated from a mouse lung cDNA library and using amplification of cDNA to isolate specific regions. The cDNA was 6304 bp in length and encoded a polypeptide of 1476 amino acids. Comparison of the deduced amino acid sequence showed that the mouse protein has high homology to the human protein; overall identity was 78.3%. The amino acid identity was high for both transmembrane domains (first transmembrane domain, 86.7%; second transmembrane domain, 81.1%) and for both ATP-binding folds (first ATP-binding fold, 80.5%; second ATP-binding fold, 83.9%), suggesting the functional importance of these regions. On the other hand, the R domain was less well conserved (68.9% identity). All of the published missense mutation sites and the site of the common delta F508 mutation were conserved between human and mouse.
我们利用从小鼠肺cDNA文库中分离得到的克隆，并通过cDNA扩增来分离特定区域，克隆出了人类囊性纤维化跨膜传导调节因子（CFTR）的小鼠同源物。该cDNA长度为6304 bp，编码一个由1476个氨基酸组成的多肽。推导的氨基酸序列比较显示，小鼠蛋白与人类蛋白具有高度同源性；总体一致性为78.3%。跨膜结构域（第一个跨膜结构域，86.7%；第二个跨膜结构域，81.1%）和两个ATP结合结构域（第一个ATP结合结构域，80.5%；第二个ATP结合结构域，83.9%）的氨基酸一致性都很高，表明这些区域具有功能重要性。另一方面，R结构域的保守性较差（一致性为68.9%）。所有已发表的错义突变位点以及常见的ΔF508突变位点在人和小鼠之间都是保守的。
