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

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 Nor...

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Bibliographic Details
Published in:Nucleic acids research 1985-07, Vol.13 (14), p.5233-5247
Main Authors: Beckmann, Robert J., Schmidt, Robert J., Santerre, Robert F., Plutzky, Jorge, Crabtree, Gerald R., Long, George L.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Biological and medical sciences
cDNA
Deoxyribonuclease BamHI
Deoxyribonucleases, Type II Site-Specific
DNA - analysis
DNA Restriction Enzymes - metabolism
Factor IX - analysis
Factor X - analysis
Fundamental and applied biological sciences. Psychology
Glycoproteins - biosynthesis
Humans
liver
Miscellaneous
Molecular and cellular biology
Molecular genetics
mRNA
Nucleic Acid Hybridization
nucleotide sequence
Protein C
Protein Precursors - genetics
Prothrombin - analysis
RNA, Messenger - analysis
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Summary: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 γ-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”, γ-carboxyglutamate and serine protease domains, but lacks the two “kringle” domains found in prothrombin.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/13.14.5233