Cathepsin L2

Protein-coding gene in the species Homo sapiens

CTSV
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1FH0, 3H6S, 3KFQ

Identifiers
AliasesCTSV, cathepsin V, CATL2, CTSL2, CTSU
External IDsOMIM: 603308; MGI: 88564; HomoloGene: 76699; GeneCards: CTSV; OMA:CTSV - orthologs
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for CTSV
Genomic location for CTSV
Band9q22.33Start97,029,677 bp[1]
End97,156,556 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for CTSV
Genomic location for CTSV
Band13 B3|13 33.26 cMStart64,507,151 bp[2]
End64,518,704 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 13: 64.51 – 64.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5][6][7][8]

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.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000136943 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021477 – 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. ^ "Entrez Gene: CTSL2 cathepsin L2".
  6. ^ Brömme D, Li Z, Barnes M, Mehler E (February 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.
  7. ^ Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K (September 1998). "Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium". Investigative Ophthalmology & Visual Science. 39 (10): 1789–96. PMID 9727401.
  8. ^ Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C (April 1998). "Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas". Cancer Research. 58 (8): 1624–30. PMID 9563472.
  9. ^ Kenney MC, Chwa M, Atilano SR, Tran A, Carballo M, Saghizadeh M, Vasiliou V, Adachi W, Brown DJ (2005). "Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder". Invest. Ophthalmol. Vis. Sci. 46 (3): 823–832. doi:10.1167/iovs.04-0549. PMID 15728537.

External links

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". 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.
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  • 1fh0: CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR
    1fh0: CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR
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