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Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases. 1987
K Ishidoh, and
S Imajoh, and
Y Emori, and
S Ohno, and
H Kawasaki, and
Y Minami, and
E Kominami, and
N Katunuma, and
K Suzuki
Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
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.
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