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CTSW
Identifiers
Aliases	CTSW, LYPN, cathepsin W
External IDs	OMIM: 602364; MGI: 1338045; HomoloGene: 37471; GeneCards: CTSW; OMA:CTSW - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.1 Start 65,879,809 bp End 65,883,741 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 A Start 5,515,071 bp End 5,518,535 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte blood bone marrow cells spleen decidua mononuclear cell monocyte lymph node upper lobe of left lung right lung Top expressed in mesenteric lymph nodes blood thymus spleen embryo subcutaneous adipose tissue pharynx duodenum embryo granulocyte More reference expression data BioGPS 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 space 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 Chr 19: 5.52 – 5.52 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Cathepsin W is a protein that in humans is encoded by the CTSW gene.

The protein encoded by this gene, a member of the peptidase C1 family of cysteine cathepsins, is a cysteine protease cathepsin that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the cell membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000172543 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000024910 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Linnevers C, Smeekens SP, Brömme D (May 1997). "Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes". FEBS Lett. 405 (3): 253–9. Bibcode:1997FEBSL.405..253L. doi:10.1016/S0014-5793(97)00118-X. PMID 9108299. S2CID 45420314.
6. 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.
7. ^ "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. Bibcode:2002PNAS...9916899M. 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". Cellular Peptidases in Immune Functions and Diseases 2. Advances in Experimental Medicine and Biology. Vol. 477. pp. 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. S2CID 31373986.

External links

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

• Biology

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• Genes on human chromosome 11
• Proteases
• EC 3.4.22
• Cathepsins
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