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beta-Hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein S

Stenflo, Johan LU ; Lundwall, Åke LU and Dahlbäck, Björn LU (1987) In Proc Natl Acad Sci U S A 84(2). p.72-368
Abstract
Vitamin K-dependent protein S is involved in the regulation of blood coagulation. It is a 75-kDa single chain protein with an NH2-terminal gamma-carboxyglutamic acid-containing domain followed by a thrombin-sensitive region and four domains arranged in tandem, each of which is homologous to the epidermal growth factor (EGF) precursor. The NH2-terminal EGF-like domain contains beta-hydroxyaspartic acid, which has been identified in vitamin K-dependent proteins. The following EGF-like repeat has a very pronounced sequence homology (10 consecutive residues identical) to one of the EGF-like units in the EGF precursor. We now show that, in protein S, this EGF-like repeat has one beta-hydroxyasparagine residue formed by hydroxylation of... (More)
Vitamin K-dependent protein S is involved in the regulation of blood coagulation. It is a 75-kDa single chain protein with an NH2-terminal gamma-carboxyglutamic acid-containing domain followed by a thrombin-sensitive region and four domains arranged in tandem, each of which is homologous to the epidermal growth factor (EGF) precursor. The NH2-terminal EGF-like domain contains beta-hydroxyaspartic acid, which has been identified in vitamin K-dependent proteins. The following EGF-like repeat has a very pronounced sequence homology (10 consecutive residues identical) to one of the EGF-like units in the EGF precursor. We now show that, in protein S, this EGF-like repeat has one beta-hydroxyasparagine residue formed by hydroxylation of asparagine. The two COOH-terminal EGF-like repeats also contain beta-hydroxyasparagine, an amino acid not previously found in proteins. Sequence comparisons have enabled us to identify a consensus sequence that seems to be required by the hydroxylase(s). (Less)
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keywords
Hydroxylation, *Glycoproteins/genetics, *Epidermal Growth Factor/genetics, DNA/analysis, Comparative Study, High Pressure Liquid, Chromatography, Cattle, Asparagine/*analogs & derivatives/analysis, Amino Acid Sequence, Animals, Peptide Fragments/analysis, Protein Conformation, *Protein Precursors/genetics, Protein S, Research Support, Non-U.S. Gov't, Sequence Homology, Nucleic Acid
in
Proc Natl Acad Sci U S A
volume
84
issue
2
pages
72 - 368
language
English
LU publication?
yes
additional info
2
id
72d30d3a-5cfb-4c6f-b99c-1235d9e58de2 (old id 3965154)
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http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2948188
date added to LUP
2016-04-04 13:58:25
date last changed
2018-11-21 21:17:30
@article{72d30d3a-5cfb-4c6f-b99c-1235d9e58de2,
  abstract     = {{Vitamin K-dependent protein S is involved in the regulation of blood coagulation. It is a 75-kDa single chain protein with an NH2-terminal gamma-carboxyglutamic acid-containing domain followed by a thrombin-sensitive region and four domains arranged in tandem, each of which is homologous to the epidermal growth factor (EGF) precursor. The NH2-terminal EGF-like domain contains beta-hydroxyaspartic acid, which has been identified in vitamin K-dependent proteins. The following EGF-like repeat has a very pronounced sequence homology (10 consecutive residues identical) to one of the EGF-like units in the EGF precursor. We now show that, in protein S, this EGF-like repeat has one beta-hydroxyasparagine residue formed by hydroxylation of asparagine. The two COOH-terminal EGF-like repeats also contain beta-hydroxyasparagine, an amino acid not previously found in proteins. Sequence comparisons have enabled us to identify a consensus sequence that seems to be required by the hydroxylase(s).}},
  author       = {{Stenflo, Johan and Lundwall, Åke and Dahlbäck, Björn}},
  keywords     = {{Hydroxylation; *Glycoproteins/genetics; *Epidermal Growth Factor/genetics; DNA/analysis; Comparative Study; High Pressure Liquid; Chromatography; Cattle; Asparagine/*analogs & derivatives/analysis; Amino Acid Sequence; Animals; Peptide Fragments/analysis; Protein Conformation; *Protein Precursors/genetics; Protein S; Research Support; Non-U.S. Gov't; Sequence Homology; Nucleic Acid}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{72--368}},
  series       = {{Proc Natl Acad Sci U S A}},
  title        = {{beta-Hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein S}},
  url          = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2948188}},
  volume       = {{84}},
  year         = {{1987}},
}