Cathepsin Z

Cathepsin Z
PDB rendering based on 1deu.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1DEU​, 1EF7​
Identifiers
Symbols	CTSZ ; CTSX
External IDs	OMIM: 603169 MGI: 1891190 HomoloGene: 1022 IUPHAR: 2354 ChEMBL: 4160 GeneCards: CTSZ Gene
EC number	3.4.18.1
Gene ontology Molecular function • cysteine-type endopeptidase activity • protein binding • cysteine-type peptidase activity Cellular component • extracellular space • lysosome • endoplasmic reticulum • plasma membrane • intracellular membrane-bounded organelle • extracellular exosome Biological process • angiotensin maturation • proteolysis • cellular protein metabolic process • proteolysis involved in cellular protein catabolic process • epithelial tube branching involved in lung morphogenesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1522	64138
Ensembl	ENSG00000101160	ENSMUSG00000016256
UniProt	Q9UBR2	Q9WUU7
RefSeq (mRNA)	NM_001336	NM_022325
RefSeq (protein)	NP_001327	NP_071720
Location (UCSC)	Chr 20: 59 – 59.01 Mb	Chr 2: 174.43 – 174.44 Mb
PubMed search

Cathepsin Z or cathepsin X is a protein that in humans is encoded by the CTSZ gene.^[1][2]The encoded protein has also been known as cathepsin X and cathepsin P.

Structure

At least two transcript variants of this gene have been found, but the full-length nature of only one of them has been determined.The gene has 6 exons and locates at chromosome band 20q13.32.^[2]

Function

The protein encoded by this gene is a lysosomal cysteine proteinase and member of the peptidase C1 family. It exhibits both carboxy-monopeptidase and carboxy-dipeptidase activities. Up to date, nine human cysteine proteinases have been identified, including cathepsin B, cathepsin C, cathepsin H, cathepsin K, cathepsin L, cathepsin L2, cathepsin O, cathepsin S, and cathepsin W. These cysteine proteinases belong to the papain family and represent a major component of the lysosomal proteolytic system.In addition to playing a critical role in protein degradation and turnover, these proteinases appear to play an extracellular role in a number of normal and pathological conditions.

Clinical Significance

This gene is expressed ubiquitously in cancer cell lines and primary tumors and, like other members of this family, may be involved in tumorigenesis.

References

1. Santamaria I, Velasco G, Pendas AM, Fueyo A, Lopez-Otin C (Aug 1998). "Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location". J Biol Chem 273 (27): 16816–23. doi:10.1074/jbc.273.27.16816. PMID 9642240.
2. "Entrez Gene: CTSZ cathepsin Z".

Further reading

• Nägler DK, Ménard R (1998). "Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions.". FEBS Lett. 434 (1-2): 135–9. doi:10.1016/S0014-5793(98)00964-8. PMID 9738465.
• Pungercar J, Ivanovski G (2000). "Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family.". Pflugers Arch. 439 (3 Suppl): R116–8. doi:10.1007/s004240000112. PMID 10653162.
• Pungercar J, Viyjak A, Ivanovski G, Krizaj I (2000). "Tissue expression and immunolocalization of a novel human cathepsin P.". Pflugers Arch. 439 (3 Suppl): R119–21. doi:10.1007/s004240000113. PMID 10653163.
• Sivaraman J, Nägler DK, Zhang R; et al. (2000). "Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine.". J. Mol. Biol. 295 (4): 939–51. doi:10.1006/jmbi.1999.3410. PMID 10656802.
• Guncar G, Klemencic I, Turk B; et al. (2000). "Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.". Structure 8 (3): 305–13. doi:10.1016/S0969-2126(00)00108-8. PMID 10745011.
• Deussing J, von Olshausen I, Peters C (2000). "Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization.". Biochim. Biophys. Acta 1491 (1-3): 93–106. doi:10.1016/s0167-4781(00)00021-x. PMID 10760573.
• Bonthron DT, Hayward BE, Moran V, Strain L (2000). "Characterization of TH1 and CTSZ, two non-imprinted genes downstream of GNAS1 in chromosome 20q13.". Hum. Genet. 107 (2): 165–75. doi:10.1007/s004390000344. PMID 11030415.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Simpson JC, Wellenreuther R, Poustka A; et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
• Deloukas P, Matthews LH, Ashurst J; et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• 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.
• 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.
• Wiemann S, Arlt D, Huber W; et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Puzer L, Barros NM, Oliveira V; et al. (2005). "Defining the substrate specificity of mouse cathepsin P.". Arch. Biochem. Biophys. 435 (1): 190–6. doi:10.1016/j.abb.2004.12.007. PMID 15680921.
• Mehrle A, Rosenfelder H, Schupp I; et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
• Lechner AM, Assfalg-Machleidt I, Zahler S; et al. (2007). "RGD-dependent binding of procathepsin X to integrin alphavbeta3 mediates cell-adhesive properties.". J. Biol. Chem. 281 (51): 39588–97. doi:10.1074/jbc.M513439200. PMID 17065156.

External links

• The MEROPS online database for peptidases and their inhibitors: C01.013