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

Research output: Contribution to journalArticlepeer-review

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).
Original languageEnglish
Pages (from-to)368-72
JournalProc Natl Acad Sci U S A
Volume84
Issue number2
Publication statusPublished - 1987

Bibliographical note

2

Subject classification (UKÄ)

  • Medicinal Chemistry

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

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