Cathepsin O

"CTSO" redirects here. For other uses, see Career and technical student organization.

Cathepsin O is an enzyme encoded by the CTSO gene in humans.

CTSO
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ATK, 1AU0, 1AU2, 1AU3, 1AU4, 1AYU, 1AYV, 1AYW, 1BGO, 1BY8, 1MEM, 1NL6, 1NLJ, 1Q6K, 1SNK, 1TU6, 1U9V, 1U9W, 1U9X, 1VSN, 1YK7, 1YK8, 1YT7, 2ATO, 2AUX, 2AUZ, 2BDL, 2R6N, 3C9E, 3H7D, 3KW9, 3KWB, 3KWZ, 3KX1, 3O0U, 3O1G, 3OVZ, 4DMX, 4DMY, 7PCK, 4LEG, 4N79, 4N8W
Identifiers
Aliases	CTSO, CTSO1, cathepsin O
External IDs	OMIM: 600550; MGI: 2139628; HomoloGene: 1020; GeneCards: CTSO; OMA:CTSO - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q32.1 Start 155,921,580 bp End 155,953,912 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 E3 Start 81,839,908 bp End 81,864,032 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon gallbladder endometrium right coronary artery smooth muscle tissue placenta gastric mucosa liver duodenum monocyte Top expressed in gastrula mesenteric lymph nodes otolith organ utricle median eminence carotid body Epithelium of choroid plexus left lobe of liver decidua white adipose tissue More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity cysteine-type endopeptidase activity cysteine-type peptidase activity hydrolase activity Cellular component lysosome extracellular space Biological process proteolysis involved in cellular protein catabolic process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1519 229445 Ensembl ENSG00000256043 ENSMUSG00000028015 UniProt P43234 Q8BM88 RefSeq (mRNA) NM_001334 NM_177662 RefSeq (protein) NP_001325 NP_808330 Location (UCSC) Chr 4: 155.92 – 155.95 Mb Chr 3: 81.84 – 81.86 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

Cathepsin O is a cysteine cathepsin, a cysteine protease and a member of the cathepsin family. This proteolytic enzyme is involved in cellular protein degradation and turnover. The recombinant form of this enzyme was shown to degrade synthetic peptides typically used as substrates for cysteine proteinases, and its proteolytic activity was abolished by an inhibitor of cysteine proteinase.

Further reading

• Shi GP, Chapman HA, Bhairi SM, et al. (1995). "Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2" (PDF). FEBS Lett. 357 (2): 129–34. doi:10.1016/0014-5793(94)01349-6. PMID 7805878. S2CID 28099876.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
• Velasco G, Ferrando AA, Puente XS, et al. (1994). "Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues". J. Biol. Chem. 269 (43): 27136–42. doi:10.1016/S0021-9258(18)47135-9. PMID 7929457.
• 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.
• Barbe L, Lundberg E, Oksvold P, et al. (2008). "Toward a confocal subcellular atlas of the human proteome". Mol. Cell. Proteomics. 7 (3): 499–508. doi:10.1074/mcp.M700325-MCP200. PMID 18029348.

External links

• The MEROPS online database for peptidases and their inhibitors: C01.035

This article incorporates text from the United States National Library of Medicine, which is in the public domain.