MOLECULAR-CLONING, EXPRESSION AND CHROMOSOMAL LOCALIZATION OF A HUMANGENE ENCODING A 33 KDA PUTATIVE METALLOPEPTIDASE (PRSM1)

The zincins are a superfamily of structurally-related Zn2+-binding met allopeptidases which play a major role in a wide range of biological p rocesses including pattern formation, growth factor activation and ext racellular matrix synthesis and degradation. In this paper we report t he identification and complete primary structure of a novel 33 kDa pro tein which contains the zinc-binding HEXXH motif found in the zincin s uperfamily. We have named this novel protein PRSM1 (PRoteaSe, Metallo, number 1). The gene was identified by the immunoscreening of a human placental cDNA library using polyclonal antibodies raised to the 70 kD a human matrix metalloendopeptidase, type III procollagen N-proteinase [Halila, R. and Peltonen, L. (1986) Purification of human procollagen type III N-proteinase from placenta and preparation of antiserum. Bio chem. J. 239, 47-52]. The protein is found in placenta and cultured os teosarcoma cells. PRSM1 could share sequence homology with the type II I procollagen N-proteinase. The prsm1 gene is represented once in the human genome and is localized on chromosome 16 (q24.3).