COX17

COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)
Rendering based on PDB 2RN9.
Available structures PDB 2RN9, 2RNB
Identifiers
Symbols	COX17; MGC104397; MGC117386
External IDs	OMIM: 604813 MGI: 1333806 HomoloGene: 38089 GeneCards: COX17 Gene
Gene Ontology Molecular function • copper ion binding • enzyme activator activity • copper chaperone activity • metal ion binding Cellular component • cytoplasm • mitochondrion • mitochondrial intermembrane space Biological process • generation of precursor metabolites and energy • copper ion transport • brain development • heart development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10063	12856
Ensembl	ENSG00000138495	ENSMUSG00000046516
UniProt	Q14061	Q3UJM3
RefSeq (mRNA)	NM_005694	NM_001017429.2
RefSeq (protein)	NP_005685	NP_001017429.1
Location (UCSC)	Chr 3: 119.37 – 119.4 Mb	Chr 16: 38.35 – 38.36 Mb
PubMed search	[1]	[2]

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.

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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. PMID 16169070. 
• 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. doi:10.1038/nature04209. PMID 16189514. 
• 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". J. Biol. Chem. 281 (18): 12270–6. doi:10.1074/jbc.M600496200. PMID 16520371. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2049083.