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Pflugers Arch. 2000;439(3 Suppl):R116-8.

Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family.

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  • 1Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia.


A cDNA encoding a novel human putative member of the papain family of cysteine peptidases has been cloned. The protease, named cathepsin P, is synthesized as a preproprotein. The presumed propeptide of 38 amino acids is followed by a 242-residue mature protein. The mature protease region is 30% identical to human papain-like cathepsins, with all the residues important for catalysis conserved. No similarity was observed in the propeptide region. On the contrary, the proenzyme shares 51-87% residues with some precursors of cysteine proteases from other species that have not yet been characterized. They all show a nearly completely conserved "CYTRED motif" in the propeptide region, not present in other members of the family, and could therefore constitute a distinct subfamily.

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