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COX17
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2L0Y, 2LGQ, 2RN9, 2RNB
Identifiers
Aliases	COX17, cytochrome c oxidase copper chaperone, cytochrome c oxidase copper chaperone COX17
External IDs	OMIM: 604813; MGI: 1333806; HomoloGene: 38089; GeneCards: COX17; OMA:COX17 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q13.33 Start 119,654,513 bp End 119,677,454 bp
Gene location (Mouse) Chr. Chromosome 16 (mouse) Band 16|16 B3 Start 38,167,353 bp End 38,173,125 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Pituitary Gland anterior pituitary left ventricle apex of heart right auricle left adrenal cortex right adrenal gland gastrocnemius muscle right adrenal cortex skeletal muscle tissue Top expressed in yolk sac aortic valve ascending aorta facial motor nucleus seminal vesicula supraoptic nucleus Ileal epithelium epithelium of stomach intercostal muscle atrioventricular valve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function copper ion binding protein binding metal ion binding cuprous ion binding copper chaperone activity Cellular component mitochondrion mitochondrial intermembrane space cytoplasm Biological process heart development brain development generation of precursor metabolites and energy copper ion transport positive regulation of cell population proliferation mitochondrial cytochrome c oxidase assembly positive regulation of cytochrome-c oxidase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10063 12856 Ensembl ENSG00000138495 ENSMUSG00000046516 UniProt Q14061 P56394 RefSeq (mRNA) NM_005694 NM_001017429 RefSeq (protein) NP_005685 NP_001368931 NP_001368932 NP_001017429 Location (UCSC) Chr 3: 119.65 – 119.68 Mb Chr 16: 38.17 – 38.17 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Cytochrome c oxidase copper chaperone is a protein that in humans is encoded by the COX17 gene.

Function

Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000138495 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000046516 – 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. Amaravadi R, Glerum DM, Tzagoloff A (Mar 1997). "Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment". Hum Genet. 99 (3): 329–33. doi:10.1007/s004390050367. PMID 9050918. S2CID 30340147.
6. ^ "Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)".

Further reading

• Punter FA, Adams DL, Glerum DM (2000). "Characterization and localization of human COX17, a gene involved in mitochondrial copper transport". Hum. Genet. 107 (1): 69–74. doi:10.1007/s004390050013. PMID 10982038.
• Horvath R, Lochmüller H, Stucka R, et al. (2000). "Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency". Biochem. Biophys. Res. Commun. 276 (2): 530–3. doi:10.1006/bbrc.2000.3495. PMID 11027508.
• Kako K, Tsumori K, Ohmasa Y, et al. (2000). "The expression of Cox17p in rodent tissues and cells". Eur. J. Biochem. 267 (22): 6699–707. doi:10.1046/j.1432-1327.2000.01771.x. PMID 11054125.
• Heaton DN, George GN, Garrison G, Winge DR (2001). "The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex". Biochemistry. 40 (3): 743–51. doi:10.1021/bi002315x. PMID 11170391.
• 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.
• Suzuki C, Daigo Y, Kikuchi T, et al. (2004). "Identification of COX17 as a therapeutic target for non-small cell lung cancer". Cancer Res. 63 (21): 7038–41. PMID 14612491.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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.
• Kako K, Takehara A, Arai H, et al. (2005). "A selective requirement for copper-dependent activation of cytochrome c oxidase by Cox17p". Biochem. Biophys. Res. Commun. 324 (4): 1379–85. doi:10.1016/j.bbrc.2004.09.211. PMID 15504366.
• Arnesano F, Balatri E, Banci L, et al. (2005). "Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding". Structure. 13 (5): 713–22. doi:10.1016/j.str.2005.02.015. PMID 15893662.
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Cobine PA, Pierrel F, Leary SC, et al. (2006). "The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding" (PDF). J. Biol. Chem. 281 (18): 12270–6. doi:10.1074/jbc.M600496200. PMID 16520371. S2CID 12826240.
• Ma J, Dempsey AA, Stamatiou D, et al. (2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.
• Voronova A, Kazantseva J, Tuuling M, et al. (2007). "Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents". Protein Expr. Purif. 53 (1): 138–44. doi:10.1016/j.pep.2006.11.014. PMID 17208454.
• Voronova A, Meyer-Klaucke W, Meyer T, et al. (2007). "Oxidative switches in functioning of mammalian copper chaperone Cox17". Biochem. J. 408 (1): 139–48. doi:10.1042/BJ20070804. PMC 2049083. PMID 17672825.

External links

• COX17 human gene location in the UCSC Genome Browser.
• COX17 human gene details in the UCSC Genome Browser.

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