beta-Hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein S
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965154
- author
- Stenflo, Johan LU ; Lundwall, Åke LU and Dahlbäck, Björn LU
- organization
- publishing date
- 1987
- 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
- 72 - 368
- language
- English
- LU publication?
- yes
- additional info
- 2
- 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
- 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}}, }