Cloning and characterization of human liver cDNA encoding a protein S precursor.
- 1 January 1987
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 84 (2), 349-353
- https://doi.org/10.1073/pnas.84.2.349
Abstract
Human liver cDNA encoding a protein S precursor was isolated from two cDNA libraries by two different techniques. Based upon the frequency of positive clones, the abundance of mRNA for protein S is .apprxeq. 0.01%. Blot hybridization of electrophoretically fractionated poly(A)+RNA revealed a major mRNA .apprxeq. 4 kilobases long and two minor forms of .apprxeq. 3.1 and .apprxeq. 2.6 kilobases. One of the cDNA clones contains a segment encoding a 676 amino acid protein S precursor, as well as 108 and 1132 nucleotides of 5'' and 3'' noncoding sequence, respectively, plus a poly(A) region at the 3'' end. The cDNAs are adenosine plus thymidine-rich (60%) except for the 5'' noncoding region, where 78% of the nucleotides are guanosine or cytosine. The protein precursor consists of a 41 amino acid "leader" peptide followed by 635 amino acids corresponding to mature protein S. Comparison of the mature protein region with homologous vitamin K-dependent plasma proteins shows that it is composed of the following domains: an amino-terminal .gamma.-carboxyglutamic acid-rich region of 37 amino acids; a 36 amino acid linker region rich in hydroxy amino acids; four epidermal growth factor-like segments, each .apprxeq. 45 amino acids long; and a 387 amino acid carboxyl-terminal domain of unrecognized structure and unknown function.Keywords
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