Advanced

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.368-72
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)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
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
368 - 72
language
English
LU publication?
yes
id
72d30d3a-5cfb-4c6f-b99c-1235d9e58de2 (old id 3965154)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2948188
date added to LUP
2013-08-11 15:09:33
date last changed
2016-04-16 11:55:33
@misc{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},
  keyword      = {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        = {368--72},
  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},
  volume       = {84},
  year         = {1987},
}