Cathepsin W

Cathepsin W is a protein that in humans is encoded by the CTSW gene.[4][5][6]

CTSW
Identifiers
Aliases	CTSW, LYPN, cathepsin W
External IDs	OMIM: 602364 MGI: 1338045 HomoloGene: 37471 GeneCards: CTSW
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.1 Start 65,879,837 bp[1] End 65,883,741 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • peptidase activity • cysteine-type endopeptidase activity • cysteine-type peptidase activity • hydrolase activity Cellular component • lysosome • membrane • platelet dense granule lumen • extracellular region • extracellular • endoplasmic reticulum Biological process • proteolysis involved in cellular protein catabolic process • immune response • proteolysis • platelet degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1521	13041
Ensembl	ENSG00000172543	ENSMUSG00000024910
UniProt	P56202	P56203
RefSeq (mRNA)	NM_001335	NM_009985
RefSeq (protein)	NP_001326	NP_034115
Location (UCSC)	Chr 11: 65.88 – 65.88 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000172543 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Linnevers C, Smeekens SP, Bromme D (May 1997). "Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes". FEBS Lett. 405 (3): 253–9. doi:10.1016/S0014-5793(97)00118-X. PMID 9108299. S2CID 45420314.
5. Wex T, Levy B, Smeekens SP, Ansorge S, Desnick RJ, Bromme D (Aug 1998). "Genomic structure, chromosomal localization, and expression of human cathepsin W". Biochem Biophys Res Commun. 248 (2): 255–61. doi:10.1006/bbrc.1998.8954. PMID 9675123.
6. "Entrez Gene: CTSW cathepsin W".

Further reading

• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• 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. PMID 15358123.
• Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMC 2286551. PMID 15340161.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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. PMID 12437118. S2CID 23389714.
• Wex T, Bühling F, Wex H, et al. (2001). "Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum". J. Immunol. 167 (4): 2172–8. doi:10.4049/jimmunol.167.4.2172. PMID 11490002.
• 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. Advances in Experimental Medicine and Biology. 477: 271–80. doi:10.1007/0-306-46826-3_29. ISBN 0-306-46383-0. PMID 10849754.
• 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. PMID 10716634.
• 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. PMID 10362521.
• Brown J, Matutes E, Singleton A, et al. (1998). "Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase". Leukemia. 12 (11): 1771–81. doi:10.1038/sj.leu.2401164. PMID 9823953.

External links

• The MEROPS online database for peptidases and their inhibitors: C01.037