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人类红细胞阴离子转运蛋白。与鼠类蛋白同源的整合膜结构域的进一步氨基酸序列。

The human erythrocyte anion-transport protein. Further amino acid sequence from the integral membrane domain homologous with the murine protein.

作者信息

Brock C J, Tanner M J

出版信息

Biochem J. 1986 May 1;235(3):899-901. doi: 10.1042/bj2350899.

Abstract

Sequences from the human erythrocyte anion-transport protein homologous with residues 417-449 and 794-813 of the murine erythrocyte anion-transport protein have been determined. The former sequence includes the putative transmembrane helix closest to the N-terminus of the protein. The latter sequence traverses almost all of the lipid bilayer and is located towards the C-terminus of the protein. Sites have been identified by alignment with the murine sequence in the integral membrane domain that are accessible to proteolytic enzymes. Sequences from the integral membrane domain of the erythrocyte anion-transport protein are highly conserved.

摘要

已确定了与小鼠红细胞阴离子转运蛋白417 - 449位残基和794 - 813位残基同源的人类红细胞阴离子转运蛋白序列。前一个序列包括最靠近该蛋白N端的假定跨膜螺旋。后一个序列几乎贯穿整个脂质双层,位于该蛋白的C端附近。通过与小鼠序列比对,在整合膜结构域中已确定了可被蛋白水解酶作用的位点。红细胞阴离子转运蛋白整合膜结构域的序列高度保守。

相似文献

10
Structure of the murine anion exchange protein.
J Cell Biochem. 1985;29(1):1-17. doi: 10.1002/jcb.240290102.

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