Data from: Phylogentic analysis of serine proteases from Russell’s viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom

Serine proteases are widely found in snake venoms. They have variety of functions including contributions to hemostasis. In this study, five serine protease were cloned and characterized from two different cDNA libraries. Factor V activator (RVV-V), alpha fibrinogenase (RVAF) and beta fibrinogenase (RVBF) from Russell’s viper (Daboia russelli siamensis), and plasminogen activator (APL-PA) and protein C activator (APL-C) from Agkistrodon piscivorus leucostoma. The snake venom serine proteases were clustered in phylogenetic tree according to their functions. KA/KS values suggested that accelerated evolution has occurred in the mature protein-coding regions in cDNAs of snake venom serine proteases.

丝氨酸蛋白酶（Serine proteases）广泛分布于蛇毒之中，具备多种生物学功能，其中包括参与凝血稳态（hemostasis）过程。本研究从两个不同的互补DNA（cDNA）文库中克隆并鉴定了5种丝氨酸蛋白酶：分别源自罗素蝰（Daboia russelli siamensis）的第五因子激活剂（Factor V activator, RVV-V）、α纤维蛋白原酶（alpha fibrinogenase, RVAF）与β纤维蛋白原酶（beta fibrinogenase, RVBF），以及源自白唇食鱼蝮（Agkistrodon piscivorus leucostoma）的纤溶酶原激活剂（plasminogen activator, APL-PA）与蛋白C激活剂（protein C activator, APL-C）。本研究中的蛇毒丝氨酸蛋白酶依据其功能在系统发育树中完成聚类；KA/KS值分析结果显示，蛇毒丝氨酸蛋白酶的cDNA中编码成熟蛋白的区域发生了加速进化。