Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases

FEBS Lett. 1987 Dec 21;226(1):33-7. doi: 10.1016/0014-5793(87)80545-8.

Abstract

A cDNA for rat cathepsin H was isolated and sequenced. The deduced protein comprising 333 amino acid residues is composed of a typical signal sequence (21 residues), a pro-peptide region (92 residues) and a mature enzyme region (220 residues). The amino acid sequence in the pro-peptide region, in particular, residues Phe-(-41) to Ser-(-29) of cathepsin H, is highly homologous to the pro-peptide regions of other cysteine proteinases. This homologous region may play a role in the processing of cysteine proteinases.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cathepsin H
  • Cathepsins / genetics*
  • Cloning, Molecular*
  • Cysteine Endopeptidases / genetics*
  • DNA / metabolism*
  • Enzyme Precursors / genetics
  • Molecular Sequence Data
  • Rats
  • Sequence Homology, Nucleic Acid

Substances

  • Enzyme Precursors
  • DNA
  • Cathepsins
  • Cysteine Endopeptidases
  • Cathepsin H
  • Ctsh protein, rat