Pflügers Archiv

, Volume 439, Supplement 1, pp r116–r118

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

  • Jože Pungerčar
  • Gabriela Ivanovski
Regular article

DOI: 10.1007/s004240000112

Cite this article as:
Pungerčar, J. & Ivanovski, G. Pflügers Arch (2000) 439: r116. doi:10.1007/s004240000112

Abstract

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.

Key words cDNAHumanCathepsin PPropeptide

Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Jože Pungerčar
    • 1
  • Gabriela Ivanovski
    • 1
  1. 1.Department of Biochemistry and Molecular Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, SloveniaSI