PRIMARY STRUCTURE OF BOVINE VITAMIN-K-DEPENDENT PROTEIN-S
PRIMARY STRUCTURE OF BOVINE VITAMIN-K-DEPENDENT PROTEIN-S
复制标题
DOI：
10.1073/pnas.83.12.4199
复制
发表时间：
1986-06-01
影响因子：
11.1
通讯作者：
STENFLO, J
中科院分区：
文献类型：
--
作者：
DAHLBACK, B;LUNDWALL, A;STENFLO, J
蛋白S是一种维生素K依赖性血浆蛋白，在凝血因子Va和VIIIa的失活中作为活化蛋白C的辅因子发挥作用。从牛肝脏文库中获得的全长cDNA克隆的核苷酸序列进行了测定，并推导了氨基酸序列。此外，95%的结构通过蛋白质测序确定。蛋白质S由634个氨基酸组成的单一多肽链，并有一个天冬酰胺连接的碳水化合物侧链。cDNA序列分析表明，该蛋白具有一个前导序列，长41个氨基酸残基。含有γ-的分子的氨基末端部分羧基谷氨酸之后是残基42-75的区域，其具有对凝血酶切割非常敏感的两个肽键。残基76-244具有四个富含半胱氨酸的重复序列，每个约40个残基长，其与小鼠表皮生长因子的前体同源。与其他维生素K依赖性血浆蛋白相比，蛋白S的羧基末端部分与丝氨酸蛋白酶不同源。
Protein S is a vitamin K-dependent plasma protein that functions as a cofactor to activated protein C in the inactivation of coagulation factors Va and VIIIa. The nucleotide sequence of a full-length cDNA clone, obtained from a bovine liver library, was determined and the amino acid sequence was deduced. In addition, 95% of the structure was determined by protein sequencing. Protein S consists of 634 amino acids in a single polypeptide chain and has one asparagine-linked carbohydrate side chain. The cDNA sequence showed that the protein has a leader sequence, 41 amino acid residues long. The amino-terminal part of the molecule containing .gamma.-carboxyglutamic acid is followed by a region, residues 42-75, with two peptide bonds that are very sensitive to cleavage by thrombin. Residues 76-244 have four cysteine-rich repeat sequences, each about 40 residues long, that are homologous to the precursor of mouse epidermal growth factor. In contrast to the other vitamin K-dependent plasma proteins, the carboxyl-terminal part of protein S is not homologous to the serine proteases.