Ishioka N, Takahashi N, Putnam F W
Proc Natl Acad Sci U S A. 1986 Apr;83(8):2363-7. doi: 10.1073/pnas.83.8.2363.
The complete amino acid sequence has been determined for alpha 1B-glycoprotein (alpha 1B), a protein of unknown function present in human plasma. This protein (Mr approximately equal to 63,000) consists of a single polypeptide chain N-linked to four glucosamine oligosaccharides. The polypeptide has five intrachain disulfide bonds and contains 474 amino acid residues. Analysis of the amino acid sequence by several computer programs shows that alpha 1B exhibits internal duplication and consists of five repeating structural domains, each containing about 95 amino acids and one disulfide bond. alpha 1B has a unique amino acid sequence. However, several domains of alpha 1B, especially the third, show statistically significant homology to variable regions of certain immunoglobulin light and heavy chains. alpha 1B also exhibits sequence similarity to other members of the immunoglobulin supergene family such as the receptor for transepithelial transport of IgA and IgM and the secretory component of human IgA. Because of its internal duplication and its sequence homology to immunoglobulin-like proteins, alpha 1B appears to have evolved from an ancestral gene similar to that of the immunoglobulin supergene family.
已确定人血浆中存在的一种功能未知的蛋白质α1B-糖蛋白(α1B)的完整氨基酸序列。该蛋白质(分子量约为63,000)由一条与四个氨基葡萄糖寡糖N-连接的单多肽链组成。该多肽有五个链内二硫键,包含474个氨基酸残基。通过几个计算机程序对氨基酸序列进行分析表明,α1B呈现内部重复,由五个重复的结构域组成,每个结构域包含约95个氨基酸和一个二硫键。α1B具有独特的氨基酸序列。然而,α1B的几个结构域,尤其是第三个结构域,与某些免疫球蛋白轻链和重链的可变区具有统计学上显著的同源性。α1B还与免疫球蛋白超基因家族的其他成员表现出序列相似性,如IgA和IgM跨上皮转运受体以及人IgA的分泌成分。由于其内部重复以及与免疫球蛋白样蛋白的序列同源性,α1B似乎是从与免疫球蛋白超基因家族类似的祖先基因进化而来的。