Cathepsin Z
Cathepsin Z or cathepsin X is a protein that in humans is encoded by the CTSZ gene.[1][2]
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. The encoded protein has also been known as cathepsin X and cathepsin P. This gene is expressed ubiquitously in cancer cell lines and primary tumors and, like other members of this family, may be involved in tumorigenesis. At least two transcript variants of this gene have been found, but the full-length nature of only one of them has been determined.[2]
References
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
PDB gallery |
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| | 1deu: CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN X: A CYSTEINE PROTEASE WITH THE PROREGION COVALENTLY LINKED TO THE ACTIVE SITE CYSTEINE |
| 1ef7: CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X |
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