Suzuki T
Department of Biology, Faculty of Science, Kochi University, Japan.
Biochim Biophys Acta. 1989 Oct 19;998(3):292-6. doi: 10.1016/0167-4838(89)90287-2.
The sea cucumber Paracaudina chilensis (Echinodermata) contains three major globins I, II and III in coelomic cells. The complete amino acid sequence of globin I has been determined. It is composed of 157 amino acid residues, is acetylated at the N-terminus, and has a characteristic N-terminal extension of 9-10 residues when compared with vertebrate globins. The sequence of Paracaudina globin I showed slightly higher homology with human alpha globin (25%) rather than with the invertebrate Anadara alpha globin (22%). Paracaudina globin I also showed strong homology (59%) with globin D from another sea cucumber, Molpadia arenicola (Mauri, F.C. (1985) Ph.D. dissertation, University of Texas). The globin sequences from the phylum Echinodermata have an important position in the molecular evolution of the globins, because they are the invertebrate group most closely related to the vertebrates.
海棒槌（棘皮动物门）的体腔细胞中含有三种主要的球蛋白I、II和III。球蛋白I的完整氨基酸序列已被确定。它由157个氨基酸残基组成，N端被乙酰化，与脊椎动物的球蛋白相比，具有9-10个残基的特征性N端延伸。海棒槌球蛋白I的序列与人α球蛋白的同源性略高（25%），而与无脊椎动物泥蚶α球蛋白的同源性较低（22%）。海棒槌球蛋白I与另一种海参——沙海螂的球蛋白D也有很强的同源性（59%）（毛里，F.C.（1985年）博士论文，德克萨斯大学）。棘皮动物门的球蛋白序列在球蛋白的分子进化中具有重要地位，因为它们是与脊椎动物关系最密切的无脊椎动物类群。
