The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2.[7]
Meinhardt C, Peitz U, Treiber G, et al. (2004). "Identification of a novel isoform predominantly expressed in gastric tissue and a triple-base pair polymorphism of the cathepsin W gene". Biochem. Biophys. Res. Commun. 321 (4): 975–80. doi:10.1016/j.bbrc.2004.07.056. PMID15358123.
Buhling F, Kellner U, Guenther D, et al. (2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal tract". Biol. Chem. 383 (7–8): 1285–9. doi:10.1515/BC.2002.144. PMID12437118.
Wex T, Levy B, Wex H, Brömme D (2000). "Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like cysteine proteases". Adv. Exp. Med. Biol. 477: 271–80. doi:10.1007/0-306-46826-3_29. PMID10849754.
Brinkworth RI, Tort JF, Brindley PJ, Dalton JP (2000). "Phylogenetic relationships and theoretical model of human cathepsin W (lymphopain), a cysteine proteinase from cytotoxic T lymphocytes". Int. J. Biochem. Cell Biol. 32 (3): 373–84. doi:10.1016/S1357-2725(99)00129-6. PMID10716634.
Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun. 259 (2): 401–7. doi:10.1006/bbrc.1999.0700. PMID10362521.