Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation.
- 1 September 1986
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 83 (18), 6716-6720
- https://doi.org/10.1073/pnas.83.18.6716
Abstract
Protein S is a cofactor of activated protein C; together they function as a regulator of blood coagulation. A human liver cDNA library constructed in bacteriophage .lambda.gt11 was screened with DNA fragments from a full-length bovine cDNA clone encoding protein S. Several cDNA clones were isolated and sequenced. The combined cDNA sequences encoded the mature protein and 15 residues of the leader sequence when compared to bovine protein S. Human protein S is a single-chain consisting of 635 amino acids with 82% homology to bovine protein S. After an NH2-terminal .gamma.-carboxyglutamic acid-containing region, there is a short region with thrombin-sensitive bond(s), followed by a region with four repeat sequences with that are homologous to the precursor of mouse epidermal growth factor. In contrast to the other vitamin K-dependent plasma proteins, the COOH-terminal portion of human protein S does not show any resemblance to serine proteases.Keywords
This publication has 34 references indexed in Scilit:
- Proteolytic inactivation of human factor VIII procoagulant protein by activated human protein C and its analogy with factor V.1984
- erythro -β-hydroxyaspartic acid in bovine factor IX and factor XFEBS Letters, 1984
- A simple and very efficient method for generating cDNA librariesGene, 1983
- Beta-hydroxyaspartic acid in vitamin K-dependent proteins.Journal of Biological Chemistry, 1983
- The occurrence of β-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogensBiochemical and Biophysical Research Communications, 1983
- Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as .beta.-hydroxyaspartic acidBiochemistry, 1983
- Purification of human vitamin K-dependent protein S and its limited proteolysis by thrombinBiochemical Journal, 1983
- Purification of human C4b-binding protein and formation of its complex with vitamin K-dependent protein SBiochemical Journal, 1983
- The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primersGene, 1982
- Regulation of bovine activated protein C by protein S: The role of the cofactor protein in species specificityThrombosis Research, 1981