Morgan R O, Fernandez M P
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Oviedo, Spain.
FEBS Lett. 1998 Sep 4;434(3):300-4. doi: 10.1016/s0014-5793(98)00997-1.
Systematic analysis of expressed sequence tags in dbEST yielded an expression profile of the ten known human annexins and led to the discovery of a novel subfamily expressed mainly in differentiating tissues. Full-length cDNAs encoded a 338-amino acid protein with less than 40% identity to other annexins, an atypical amino acid composition, and an insertion and deletion in internal repeat 3. The most striking feature was a complete ablation of all four type II calcium-binding sites in the conserved tetrad core. Annexin 31 thus constitutes a unique, natural probe for investigating the role of membrane binding in annexin function.
对dbEST中表达序列标签的系统分析得出了10种已知人类膜联蛋白的表达谱,并促成了一个主要在分化组织中表达的新亚家族的发现。全长cDNA编码一种338个氨基酸的蛋白质,与其他膜联蛋白的同源性低于40%,具有非典型的氨基酸组成,并且在内部重复序列3中有插入和缺失。最显著的特征是在保守的四重核心中所有四个II型钙结合位点完全缺失。因此,膜联蛋白31构成了一种独特的天然探针,用于研究膜结合在膜联蛋白功能中的作用。