The protein encoded by COX10 is an assembly factor essential to COX synthesis, participating in the first step of the mitochondrial heme A biosynthetic pathway. It catalyzes the farnesylation of the vinyl group at position C2 of protoheme (heme B) and converts it to heme O.[10][11]
In addition, this gene is disrupted in patients with CMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP (hereditary neuropathy with liability to pressure palsies) deletion.[6]
^ abcGRCh38: Ensembl release 89: ENSG00000006695 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000042148 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Murakami T, Reiter LT, Lupski JR (May 1997). "Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene". Genomics. 42 (1): 161–4. doi:10.1006/geno.1997.4711. PMID 9177788.
^ abcde"Entrez Gene: COX10 COX10 homolog, cytochrome c oxidase assembly protein, heme A: farnesyltransferase (yeast)". This article incorporates text from this source, which is in the public domain.
^Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (October 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC4076475. PMID 23965338.
^"COX10 - Protoheme IX farnesyltransferase, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).[permanent dead link]
^ abValnot I, von Kleist-Retzow JC, Barrientos A, Gorbatyuk M, Taanman JW, Mehaye B, Rustin P, Tzagoloff A, Munnich A, Rötig A (May 2000). "A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency". Human Molecular Genetics. 9 (8): 1245–9. doi:10.1093/hmg/9.8.1245. PMID 10767350.
^ abcAntonicka H, Leary SC, Guercin GH, Agar JN, Horvath R, Kennaway NG, Harding CO, Jaksch M, Shoubridge EA (October 2003). "Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency". Human Molecular Genetics. 12 (20): 2693–702. doi:10.1093/hmg/ddg284. PMID 12928484.
^Williams SL, Valnot I, Rustin P, Taanman JW (February 2004). "Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1". The Journal of Biological Chemistry. 279 (9): 7462–9. doi:10.1074/jbc.M309232200. PMID 14607829.
^Tyers M. "COX10 Result Summary | BioGRID". thebiogrid.org n. Retrieved 2018-08-07.
External linksedit
Human COX10 genome location and COX10 gene details page in the UCSC Genome Browser.
Further readingedit
Pitceathly RD, Taanman JW, Rahman S, Meunier B, Sadowski M, Cirak S, et al. (December 2013). "COX10 mutations resulting in complex multisystem mitochondrial disease that remains stable into adulthood". JAMA Neurology. 70 (12): 1556–61. doi:10.1001/jamaneurol.2013.3242. PMID 24100867.
Glerum DM, Tzagoloff A (August 1994). "Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant". Proceedings of the National Academy of Sciences of the United States of America. 91 (18): 8452–6. Bibcode:1994PNAS...91.8452G. doi:10.1073/pnas.91.18.8452. PMC44624. PMID 8078902.
Reiter LT, Murakami T, Koeuth T, Gibbs RA, Lupski JR (September 1997). "The human COX10 gene is disrupted during homologous recombination between the 24 kb proximal and distal CMT1A-REPs". Human Molecular Genetics. 6 (9): 1595–603. doi:10.1093/hmg/6.9.1595. PMID 9285799.
Kennerson ML, Nassif NT, Dawkins JL, DeKroon RM, Yang JG, Nicholson GA (November 1997). "The Charcot-Marie-Tooth binary repeat contains a gene transcribed from the opposite strand of a partially duplicated region of the COX10 gene". Genomics. 46 (1): 61–9. doi:10.1006/geno.1997.5012. PMID 9403059.
Kennerson ML, Nassif NT, Nicholson GA (October 1998). "Genomic structure and physical mapping of C17orf1: a gene associated with the proximal element of the CMT1A-REP binary repeat". Genomics. 53 (1): 110–2. doi:10.1006/geno.1998.5453. PMID 9787083.
Valnot I, von Kleist-Retzow JC, Barrientos A, Gorbatyuk M, Taanman JW, Mehaye B, Rustin P, Tzagoloff A, Munnich A, Rötig A (May 2000). "A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency". Human Molecular Genetics. 9 (8): 1245–9. doi:10.1093/hmg/9.8.1245. PMID 10767350.
Bosetti F, Brizzi F, Barogi S, Mancuso M, Siciliano G, Tendi EA, Murri L, Rapoport SI, Solaini G (2002). "Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease". Neurobiology of Aging. 23 (3): 371–6. doi:10.1016/S0197-4580(01)00314-1. PMID 11959398. S2CID 5621542.
Antonicka H, Leary SC, Guercin GH, Agar JN, Horvath R, Kennaway NG, Harding CO, Jaksch M, Shoubridge EA (October 2003). "Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency". Human Molecular Genetics. 12 (20): 2693–702. doi:10.1093/hmg/ddg284. PMID 12928484.
Williams SL, Valnot I, Rustin P, Taanman JW (February 2004). "Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1". The Journal of Biological Chemistry. 279 (9): 7462–9. doi:10.1074/jbc.M309232200. PMID 14607829.
Coenen MJ, van den Heuvel LP, Ugalde C, Ten Brinke M, Nijtmans LG, Trijbels FJ, Beblo S, Maier EM, Muntau AC, Smeitink JA (October 2004). "Cytochrome c oxidase biogenesis in a patient with a mutation in COX10 gene". Annals of Neurology. 56 (4): 560–4. doi:10.1002/ana.20229. PMID 15455402. S2CID 2348661.
Veluthakal R, Kaur H, Goalstone M, Kowluru A (January 2007). "Dominant-negative alpha-subunit of farnesyl- and geranyltransferase inhibits glucose-stimulated, but not KCl-stimulated, insulin secretion in INS 832/13 cells". Diabetes. 56 (1): 204–10. doi:10.2337/db06-0668. PMID 17192483. S2CID 25460768.