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Comparative Study
. 1985 Jul 25;13(14):5233-47.
doi: 10.1093/nar/13.14.5233.

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

Free PMC article
Comparative Study

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

R J Beckmann et al. Nucleic Acids Res. .
Free PMC article

Abstract

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 gamma-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", gamma-carboxyglutamate and serine protease domains, but lacks the two "kringle" domains found in prothrombin.

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