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.
Pungercar
J
J
Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia. joze.pungercar@ijs.si
Ivanovski
G
G
D000595:Amino Acid Sequence / Q000235:genetics; D056657:Cathepsin K; D002403:Cathepsins / Q000235:genetics*; D003001:Cloning, Molecular; D017124:Conserved Sequence / Q000235:genetics; D003546:Cysteine Endopeptidases / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D010206:Papain / Q000235:genetics; D011498:Protein Precursors / Q000235:genetics
D011498:Protein Precursors; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D010206:Papain; C534130:CTSK protein, human; D056657:Cathepsin K