Catterall C F, Lyons A, Sim R B, Day A J, Harris T J
Biochem J. 1987 Mar 15;242(3):849-56. doi: 10.1042/bj2420849.
A cDNA clone of the mRNA coding for the human complement system control protein Factor I has been isolated. The predicted amino acid sequence obtained from the DNA sequence demonstrates a protein consisting of a heavy chain (Mr 35,400) linked to a light chain (Mr 27,600), both of which contain three sites for N-linked glycosylation. The light chain has clear homology with other serine proteinases, most notably in the region of the catalytically active and structurally important amino acids and shares some of the features characteristic of the plasminogen activators. The heavy chain has a clear 'mosaic' nature typical of the plasma serine proteinases; in particular it contains class A and class B LDL (low-density lipoprotein) receptor repeats with conserved cysteine residues similar to those found in other complement proteins.
编码人补体系统调控蛋白I因子的mRNA的cDNA克隆已被分离出来。从DNA序列获得的预测氨基酸序列显示，该蛋白质由一条重链（分子量35400）和一条轻链（分子量27600）相连组成，二者均含有三个N-连接糖基化位点。轻链与其他丝氨酸蛋白酶具有明显的同源性，最显著的是在催化活性和结构重要氨基酸区域，并且具有一些纤溶酶原激活剂的特征。重链具有血浆丝氨酸蛋白酶典型的明显“镶嵌”性质；特别是它含有A类和B类低密度脂蛋白（LDL）受体重复序列，带有与其他补体蛋白中发现的类似的保守半胱氨酸残基。
