Nucleic Acids Research, 1985, Vol. 13, No. 14 5233-5247
© 1985
Articles |
The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAs
Division of Molecular and Cellular Biology, Lilly Research Laboratories Indianapolis, IN 46285 1Department of Pathology, Stanford Medical School Palo Alto, CA 94305, USA
Received May 29, 1985. Accepted June 19, 1985.
Human liver cDNA coding for protein C has been synthesized, cloned and sequenced. The abundance of protein C message is approximately 0.02% of total mRNA. Three overlapping clones contain 1,798 nucleotides of contiguous sequence, which approximates the size of the protein's mRNA, based upon Northern hybridization. The cDNA sequence consists of 73 5'-noncoding bases, coding sequence for a 461 amino acid nascent polypeptide precursor, a TAA termination codon, 296 3'-noncoding bases, and a 38 base polyadenylation segment. The nascent protein consists of a 33 amino acid "signal", a 9 amino acid propeptide, a 155 amino acid "light" chain, a Lys-Arg connecting dipeptide, and a 262 amino acid "heavy" chain. Human protein C and Factor IX and X precursors possess about one third identical amino acids (59% in the 
-carboxyglutamate domain), including two forty-six amino acid segments homologous to epidermal growth factor. Human protein C also has similar homology with prothrombin in the "leader", -carboxyglutamate and serine protease domains, but lacks the two "kringle" domains found in prothrombin.
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