| Literature DB >> 3691815 |
K Ishidoh1, S Imajoh, Y Emori, S Ohno, H Kawasaki, Y Minami, E Kominami, N Katunuma, K Suzuki.
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.Entities:
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Year: 1987 PMID: 3691815 DOI: 10.1016/0014-5793(87)80545-8
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124