Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation
Author
Summary, in English
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 protein 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 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.
Department/s
Publishing year
1986
Language
English
Pages
20-6716
Publication/Series
Proc Natl Acad Sci U S A
Volume
83
Issue
18
Links
Document type
Journal article
Topic
- Medicinal Chemistry
Keywords
- Protein S
- Humans
- Glycoproteins/analysis/*genetics
- Epidermal Growth Factor/analysis
- DNA/*analysis/isolation & purification
- Amino Acid Sequence
- Base Sequence
- RNA
- Messenger/analysis
- Research Support
- Non-U.S. Gov't
Status
Published
Research group
- Clinical Chemistry, Malmö