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Primary structure of bovine vitamin K-dependent protein S

Dahlbäck, Björn LU ; Lundwall, Åke LU and Stenflo, Johan LU (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)
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Contribution to journal
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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
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
2013-08-11 18:50:40
date last changed
2016-04-16 12:01:44
@misc{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},
  keyword      = {*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},
  volume       = {83},
  year         = {1986},
}