Cathepsin L2

"CTSV" redirects here. For the car, see Cadillac CTS-V.

Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in humans by the CTSV gene.

CTSV
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FH0, 3H6S, 3KFQ
Identifiers
Aliases	CTSV, cathepsin V, CATL2, CTSL2, CTSU
External IDs	OMIM: 603308; MGI: 88564; HomoloGene: 76699; GeneCards: CTSV; OMA:CTSV - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9q22.33 Start 97,029,677 bp End 97,156,556 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 B3|13 33.26 cM Start 64,507,151 bp End 64,518,704 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in thymus skin of arm skin of thigh oocyte retinal pigment epithelium amniotic fluid secondary oocyte hair follicle vulva gonad Top expressed in stroma of bone marrow iris epithelium of lens decidua endothelial cell of lymphatic vessel gastrula corneal stroma ciliary body efferent ductule cumulus cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type peptidase activity peptide binding peptidase activity protein binding aminopeptidase activity hydrolase activity serine-type endopeptidase activity cysteine-type endopeptidase activity cysteine-type carboxypeptidase activity histone binding kininogen binding protein-containing complex binding Cellular component cytoplasm perikaryon apical part of cell secretory granule extracellular region microvillus vacuole lysosomal lumen neuron projection lysosome external side of plasma membrane extracellular space nucleus nucleolus cytoplasmic vesicle Biological process male gonad development response to organic cyclic compound antigen processing and presentation of exogenous peptide antigen via MHC class II cellular response to starvation extracellular matrix disassembly response to glucocorticoid response to glucose Sertoli cell differentiation response to gonadotropin proteolysis cell communication decidualization spermatogenesis multicellular organism aging proteolysis involved in cellular protein catabolic process nerve development autophagic cell death response to odorant regulation of keratinocyte differentiation negative regulation of keratinocyte proliferation protein processing protein autoprocessing hair follicle morphogenesis regulation of actin cytoskeleton reorganization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1515 13039 Ensembl ENSG00000136943 ENSMUSG00000021477 UniProt O60911 P06797 RefSeq (mRNA) NM_001333 NM_001201575 NM_009984 RefSeq (protein) NP_001188504 NP_001324 NP_034114 Location (UCSC) Chr 9: 97.03 – 97.16 Mb Chr 13: 64.51 – 64.52 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

The protein is a human cysteine cathepsin, a lysosomal cysteine protease with endopeptidase activity.

The protein is a member of the papain-like protease family (MEROPS family C1), a lysosomal cysteine protease with endopeptidase activity. It may play an important role in corneal physiology. This gene is expressed in colorectal and breast carcinomas but not in normal colon, mammary gland, or peritumoral tissues, suggesting a possible role for this gene in tumor processes.

Clinical significance

Cathepsin L2 may play a role in the pathogenesis of keratoconus.

External links

• The MEROPS online database for peptidases and their inhibitors: C01.009 Archived 22 February 2021 at the Wayback Machine
• Cathepsin+V at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Further reading

• Santamaría I, Velasco G, Cazorla M, et al. (1998). "Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas". Cancer Res. 58 (8): 1624–30. PMID 9563472.
• Adachi W, Kawamoto S, Ohno I, et al. (1998). "Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium". Invest. Ophthalmol. Vis. Sci. 39 (10): 1789–96. PMID 9727401.
• Brömme D, Li Z, Barnes M, Mehler E (1999). "Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization". Biochemistry. 38 (8): 2377–85. doi:10.1021/bi982175f. PMID 10029531.
• Itoh R, Kawamoto S, Adachi W, et al. (1999). "Genomic organization and chromosomal localization of the human cathepsin L2 gene" (PDF). DNA Res. 6 (2): 137–40. doi:10.1093/dnares/6.2.137. PMID 10382972.
• Somoza JR, Zhan H, Bowman KK, et al. (2000). "Crystal structure of human cathepsin V.". Biochemistry. 39 (41): 12543–51. doi:10.1021/bi000951p. PMID 11027133.
• 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.
• Bernard D, Méhul B, Thomas-Collignon A, et al. (2003). "Analysis of proteins with caseinolytic activity in a human stratum corneum extract revealed a yet unidentified cysteine protease and identified the so-called "stratum corneum thiol protease" as cathepsin l2". J. Invest. Dermatol. 120 (4): 592–600. doi:10.1046/j.1523-1747.2003.12086.x. PMID 12648222.
• Tolosa E, Li W, Yasuda Y, et al. (2003). "Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis". J. Clin. Invest. 112 (4): 517–26. doi:10.1172/JCI18028. PMC 171390. PMID 12925692.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Yasuda Y, Li Z, Greenbaum D, et al. (2004). "Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages". J. Biol. Chem. 279 (35): 36761–70. doi:10.1074/jbc.M403986200. PMID 15192101.
• 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.
• Hagemann S, Günther T, Dennemärker J, et al. (2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles". Eur. J. Cell Biol. 83 (11–12): 775–80. doi:10.1078/0171-9335-00404. PMID 15679121.
• Cheng T, Hitomi K, van Vlijmen-Willems IM, et al. (2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification". J. Biol. Chem. 281 (23): 15893–9. doi:10.1074/jbc.M600694200. hdl:2066/50224. PMID 16565075.
• Burden RE, Snoddy P, Jefferies CA, et al. (2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide". Biol. Chem. 388 (5): 541–5. doi:10.1515/BC.2007.053. PMID 17516850. S2CID 6680659.
• Viken MK, Sollid HD, Joner G, et al. (2007). "Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis". Hum. Immunol. 68 (9): 748–55. doi:10.1016/j.humimm.2007.05.009. PMID 17869649.