Kube E, Weber K, Gerke V
Department of Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, F.R.G.
Gene. 1991 Jun 30;102(2):255-9. doi: 10.1016/0378-1119(91)90086-q.
The p11 protein is a member of the S-100 family of Ca(2+)-binding proteins and serves within the cell as a ligand of the tyrosine kinase substrate, annexin II. To obtain more structural information on this molecule, we have isolated and characterized p11 cDNA clones from several different species. A comparison of the deduced amino acid (aa) sequences reveals that mammalian and avian p11 are highly similar (at least 90% identical at the aa level), whereas p11 from Xenopus laevis shows a considerable degree of sequence variation (the aa sequence identity drops to approx. 60% when compared to mammalian or chicken p11). Interestingly, the C-terminal 18 aa, which are unique to p11 within the S-100 family, show a relatively high conservation among species. This high evolutionary conservation is in line with a structurally and/or functionally important role of this C terminus, e.g., in annexin II binding.
p11蛋白是Ca(2+)结合蛋白S-100家族的成员，在细胞内作为酪氨酸激酶底物膜联蛋白II的配体发挥作用。为了获得关于该分子的更多结构信息，我们从几个不同物种中分离并鉴定了p11 cDNA克隆。对推导的氨基酸(aa)序列进行比较发现，哺乳动物和禽类的p11高度相似(在氨基酸水平上至少90%相同)，而非洲爪蟾的p11则表现出相当程度的序列变异(与哺乳动物或鸡的p11相比，氨基酸序列同一性降至约60%)。有趣的是，S-100家族中p11特有的C末端18个氨基酸在物种间表现出相对较高的保守性。这种高度的进化保守性与该C末端在结构和/或功能上的重要作用一致，例如在膜联蛋白II结合中。
