K. Tisljar et al., Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression, FEBS LETTER, 459(3), 1999, pp. 299-304
A novel mouse cysteine protease of the papain family was identified by sear
ching the dbEST database. A 1.28 kb full-length cDNA was obtained which con
tains an open reading frame of 999 nucleotides and encodes a predicted poly
peptide of 333 amino acids, The deduced polypeptide exhibits features chara
cteristic of cysteine proteases of the papain type including the highly con
served residues of the catalytic triad, and was hence named cathepsin J, Ca
thepsin J represents the murine homologue of a previously described rat cat
hepsin L-related protein. Mature cathepsin J shows 59.3% identity to mouse
cathepsin L and contains the characteristic ER(F/W)NIN motif within the pro
peptide indicating that this protease belongs to the subgroup of cathepsin
L-like cysteine proteases, Northern blot analysis of various tissues reveal
ed a placenta-restricted expression. This expression pattern may suggest a
role of cathepsin J in embryo implantation and/or placental function. Ctsj
was mapped to mouse chromosome 13 in the vicinity of cathepsin L suggesting
that cathepsin J may have arisen by gene duplication from cathepsin L or a
common ancestral gene. (C) 1999 Federation of European Biochemical Societi
es.