Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family.
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.
Department of Biochemistry and Molecular Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia, , , , , , SI.
Jože
J
Pungerčar
Department of Biochemistry and Molecular Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia, , , , , , SI.
Gabriela
G
Ivanovski
Cathepsin P; Human; Key words cDNA; Propeptide