Primary structure of bovine vitamin K-dependent protein S
(1986) In Proc Natl Acad Sci U S A 83(12). p.203-4199- Abstract
- Protein S is a vitamin K-dependent plasma protein that functions as a cofactor to activated protein C in the inactivation of coagulation factors Va and VIIIa. The nucleotide sequence of a full-length cDNA clone, obtained from a bovine liver library, was determined and the amino acid sequence was deduced. In addition, 95% of the structure was determined by protein sequencing. Protein S consists of 634 amino acids in a single polypeptide chain and has one asparagine-linked carbohydrate side chain. The cDNA sequence showed that the protein has a leader sequence, 41 amino acid residues long. The amino-terminal part of the molecule containing gamma-carboxyglutamic acid is followed by a region, residues 42-75, with two peptide bonds that are... (More)
- Protein S is a vitamin K-dependent plasma protein that functions as a cofactor to activated protein C in the inactivation of coagulation factors Va and VIIIa. The nucleotide sequence of a full-length cDNA clone, obtained from a bovine liver library, was determined and the amino acid sequence was deduced. In addition, 95% of the structure was determined by protein sequencing. Protein S consists of 634 amino acids in a single polypeptide chain and has one asparagine-linked carbohydrate side chain. The cDNA sequence showed that the protein has a leader sequence, 41 amino acid residues long. The amino-terminal part of the molecule containing gamma-carboxyglutamic acid is followed by a region, residues 42-75, with two peptide bonds that are very sensitive to cleavage by thrombin. Residues 76-244 have four cysteinerich repeat sequences, each about 40 residues long, that are homologous to the precursor of mouse epidermal growth factor. In contrast to the other vitamin K-dependent plasma proteins, the carboxyl-terminal part of protein S is not homologous to the serine proteases. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965125
- author
- Dahlbäck, Björn LU ; Lundwall, Åke LU and Stenflo, Johan LU
- organization
- publishing date
- 1986
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- *Glycoproteins/genetics, Disulfides, DNA/genetics, Molecular, Cloning, Cattle, *Blood Coagulation Factors/genetics, Amino Acid Sequence, Animals, Protein Conformation, Protein S, Research Support, Non-U.S. Gov't, Vitamin K
- in
- Proc Natl Acad Sci U S A
- volume
- 83
- issue
- 12
- pages
- 203 - 4199
- external identifiers
-
- scopus:0010662163
- language
- English
- LU publication?
- yes
- additional info
- 12
- id
- 2f81c12d-49e2-44c6-b069-816921e235b1 (old id 3965125)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2940598
- date added to LUP
- 2016-04-04 14:03:02
- date last changed
- 2021-01-10 05:48:29
@article{2f81c12d-49e2-44c6-b069-816921e235b1, abstract = {{Protein S is a vitamin K-dependent plasma protein that functions as a cofactor to activated protein C in the inactivation of coagulation factors Va and VIIIa. The nucleotide sequence of a full-length cDNA clone, obtained from a bovine liver library, was determined and the amino acid sequence was deduced. In addition, 95% of the structure was determined by protein sequencing. Protein S consists of 634 amino acids in a single polypeptide chain and has one asparagine-linked carbohydrate side chain. The cDNA sequence showed that the protein has a leader sequence, 41 amino acid residues long. The amino-terminal part of the molecule containing gamma-carboxyglutamic acid is followed by a region, residues 42-75, with two peptide bonds that are very sensitive to cleavage by thrombin. Residues 76-244 have four cysteinerich repeat sequences, each about 40 residues long, that are homologous to the precursor of mouse epidermal growth factor. In contrast to the other vitamin K-dependent plasma proteins, the carboxyl-terminal part of protein S is not homologous to the serine proteases.}}, author = {{Dahlbäck, Björn and Lundwall, Åke and Stenflo, Johan}}, keywords = {{*Glycoproteins/genetics; Disulfides; DNA/genetics; Molecular; Cloning; Cattle; *Blood Coagulation Factors/genetics; Amino Acid Sequence; Animals; Protein Conformation; Protein S; Research Support; Non-U.S. Gov't; Vitamin K}}, language = {{eng}}, number = {{12}}, pages = {{203--4199}}, series = {{Proc Natl Acad Sci U S A}}, title = {{Primary structure of bovine vitamin K-dependent protein S}}, url = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2940598}}, volume = {{83}}, year = {{1986}}, }