Coutu M D, Craig S W
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Proc Natl Acad Sci U S A. 1988 Nov;85(22):8535-9. doi: 10.1073/pnas.85.22.8535.
We report the complete primary structure of chicken embryo vinculin. The amino acid sequence was derived from the nucleotide sequence of five overlapping cDNA clones isolated from a lambda gt11 phage library. Chicken embryo vinculin contains 1066 amino acids, has a calculated Mr of 116,990, a calculated pI of 5.9, and a hydropathy index of -4.22. A search of the National Biomedical Research Foundation protein sequence data base found no proteins with significant homology to vinculin. A striking feature of the linear sequence is a proline-rich region extending between residues 837 and 879. This region contains 45% proline and 19% aspartic plus glutamic acids; it is also the longest hydrophilic stretch in the molecule. The proline-rich region separates an amino-terminal domain with a calculated pI of 5.4 from a carboxyl-terminal domain with a calculated pI of 9.7. This feature suggests a structural basis for the specific interaction of vinculin with acidic phospholipids and a mechanism for the shuttling of vinculin between cytoplasm and membrane-associated junctional plaque.
我们报道了鸡胚纽蛋白的完整一级结构。氨基酸序列源自从λgt11噬菌体文库中分离出的五个重叠cDNA克隆的核苷酸序列。鸡胚纽蛋白含有1066个氨基酸，计算所得的分子量为116,990，计算所得的等电点为5.9，亲水性指数为-4.22。在国家生物医学研究基金会蛋白质序列数据库中搜索发现，没有与纽蛋白具有显著同源性的蛋白质。线性序列的一个显著特征是在837至879位残基之间延伸的富含脯氨酸的区域。该区域含有45%的脯氨酸以及19%的天冬氨酸和谷氨酸；它也是分子中最长的亲水区段。富含脯氨酸的区域将计算所得等电点为5.4的氨基末端结构域与计算所得等电点为9.7的羧基末端结构域分隔开来。这一特征为纽蛋白与酸性磷脂的特异性相互作用提供了结构基础，并为纽蛋白在细胞质与膜相关连接斑之间穿梭提供了一种机制。
