Wasenius V M, Saraste M, Lehto V P
Department of Medical Chemistry, University of Helsinki, Finland.
Int J Dev Biol. 1989 Mar;33(1):49-54.
The complete nucleotide sequence coding for the chicken brain alpha-spectrin was determined. It comprises the entire coding frame, 5'- and 3'-untranslated sequences terminating in a poly(A)-tail. The deduced amino acid sequence shows that the alpha-chain contains 22 segments, 20 of which correspond to the typical 106 residue repeat of the human erythrocyte spectrin. Some segments non-homologous to the repeat structure reside in the middle and COOH-terminal regions. Sequence comparisons with other proteins show that these segments evidently harbour some structural and functional features such as: homology to alpha-actinin and dystrophin, two typical EF-hand structures (calcium-binding) and a putative calmodulin-binding site in the COOH-terminus and a sequence homologous to various src-tyrosine kinases and to phospholipase C in the middle of the molecule. Comparison of our sequence with other partial alpha-spectrin sequences shows that alpha-spectrin is well conserved in different species and that the human erythrocyte alpha-spectrin is divergent.
测定了编码鸡脑α-血影蛋白的完整核苷酸序列。它包括整个编码框架、以聚腺苷酸尾结尾的5'-和3'-非翻译序列。推导的氨基酸序列表明，α链包含22个区段，其中20个对应于人红细胞血影蛋白典型的106个残基重复序列。一些与重复结构无同源性的区段位于中间和COOH末端区域。与其他蛋白质的序列比较表明，这些区段明显具有一些结构和功能特征，如：与α-辅肌动蛋白和肌营养不良蛋白同源，两个典型的EF-手结构（钙结合）以及COOH末端的一个假定钙调蛋白结合位点，以及分子中间与各种src-酪氨酸激酶和磷脂酶C同源的序列。将我们的序列与其他部分α-血影蛋白序列进行比较表明，α-血影蛋白在不同物种中保守性良好，而人红细胞α-血影蛋白则有差异。
