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PMID: 3691815 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 226 ·No. 1 ·1987-12-21 ·Pages 33-7

Ishidoh K, Imajoh S, Emori Y, Ohno S, Kawasaki H, Minami Y, Kominami E, Katunuma N, Suzuki K

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.

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
Chemicals
Enzyme Precursors DNA Cathepsins Cysteine Endopeptidases Cathepsin H Ctsh protein, rat
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Ishidoh K
Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
Imajoh S
Emori Y
Ohno S
Kawasaki H
Minami Y
Kominami E
Katunuma N
Suzuki K
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1987-12-21
Pages
33-7
Language
English
Region
England
NLM ID
0155157
Subset
IM
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