Amino acid sequence of bovine protein Z: a vitamin K-dependent serine protease homolog

P Højrup, M S Jensen, T E Petersen

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The amino acid sequence of protein Z has been determined from sequence analysis performed on fragments obtained by chemical and enzymatic degradations. The polypeptide consists of a single chain containing 396 amino acid residues (Mr 43 677). Comparison with the vitamin K-dependent plasma proteins reveals an extensive homology. The N-terminal part, containing 13 gamma-carboxyglutamic acid and one beta-hydroxyaspartic acid residue, is extensively homologous to and of similar length to the light chain of factor X. The remainder of protein Z is homologous to the serine proteases and of similar size to the heavy chain of factor Xa, but of the active site residues only aspartic acid-102 is present. Histidine-57 and serine-195 are replaced in protein Z by threonine and alanine, respectively. The physiological function of protein Z is still uncertain.

Original languageEnglish
JournalFEBS Letters
Volume184
Issue number2
Pages (from-to)333-8
Number of pages6
ISSN1873-3468
DOIs
Publication statusPublished - 20. May 1985

Keywords

  • Amino Acid Sequence
  • Amino Acids/analysis
  • Animals
  • Blood Proteins/genetics
  • Cattle
  • Endopeptidases/genetics
  • Mutation
  • Protein Processing, Post-Translational
  • Serine Endopeptidases

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