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.
Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones
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C F Catterall, A Lyons, R B Sim, A J Day, T J R Harris; Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones. Biochem J 15 March 1987; 242 (3): 849–856. doi: https://doi.org/10.1042/bj2420849
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