The Primary Structure and Tissue Distribution of Cathepsin
- 1 January 1992
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 373 (2) , 367-374
- https://doi.org/10.1515/bchm3.1992.373.2.367
Abstract
A cDNA for rat cathepsin C (dipeptidylaminopeptidase I) was isolated. The encoded protein is composed of the signal peptide of 28 residues, the propeptide of 201 residues and the mature enzyme region of 233 residues. The amino acid sequence of the mature enzyme region has 39.5 to 30.5% identity to other papain family proteinases. Cathepsin C is, therefore, belongs to papain family, although its propeptide region is much longer than those of other cysteine proteinases and show no significant sequence similarity to any other cysteine proteinase. The mRNA and protein for cathepsin C are broadly distributed in rat tissues, but the relative proportions of cathepsin C and other cysteine proteinases are found to vary from tissue to tissue.Keywords
This publication has 3 references indexed in Scilit:
- Primary structures of Sm31/32 diagnostic proteins of Schistosoma mansoni and their identification as proteasesMolecular and Biochemical Parasitology, 1989
- Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.Proceedings of the National Academy of Sciences, 1986
- Homology of amino acid sequences of rat liver cathepsins B and H with that of papain.Proceedings of the National Academy of Sciences, 1983