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
| Autor: | Robert John Beckmann, Robert J. Schmidt, Jorge Plutzky, Robert Frank Santerre, George L. Long, Gerald R. Crabtree |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Biology
Factor IX Complementary DNA Genetics Humans Amino Acid Sequence RNA Messenger Protein Precursors Deoxyribonucleases Type II Site-Specific Protein precursor Peptide sequence Glycoproteins chemistry.chemical_classification Messenger RNA Base Sequence Deoxyribonuclease BamHI Protein primary structure Nucleic Acid Hybridization DNA DNA Restriction Enzymes Molecular biology Stop codon Amino acid Biochemistry chemistry Factor X Prothrombin EF-Tu Protein C |
| Zdroj: | Nucleic Acids Research. 13:5233-5247 |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/13.14.5233 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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