COX10

From Wikipedia, the free encyclopedia

COX10 homolog, cytochrome c oxidase assembly protein, heme A: farnesyltransferase (yeast)

Identifiers

External IDs

OMIM: 602125 MGI: 1917633 HomoloGene: 80170

Gene ontology
Molecular Function:	• cytochrome-c oxidase activity • protoheme IX farnesyltransferase activity • transferase activity
Cellular Component:	• mitochondrion • membrane • integral to membrane
Biological Process:	• mitochondrial fission • mitochondrial electron transport, cytochrome c to oxygen • heme a biosynthetic process • cytochrome c oxidase complex assembly • aerobic respiration • cytochrome complex assembly

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001303 (mRNA)
NP_001294 (protein)

NM_178379 (mRNA)
NP_848466 (protein)

Location

Chr 17: 13.91 - 14.05 Mb

Chr 11: 63.78 - 63.9 Mb

Pubmed search

[1]

[2]

COX10 homolog, cytochrome c oxidase assembly protein, heme A: farnesyltransferase (yeast), also known as COX10, is a human gene.^[1]

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 heme A:farnesyltransferase, which is not a structural subunit but required for the expression of functional COX and functions in the maturation of the heme A prosthetic group of COX. This protein is predicted to contain 7-9 transmembrane domains localized in the mitochondrial inner membrane. A gene mutation, which results in the substitution of a lysine for an asparagine (N204K), is identified to be responsible for cytochrome c oxidase deficiency. 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: COX10 COX10 homolog, cytochrome c oxidase assembly protein, heme A: farnesyltransferase (yeast).

[edit] Further reading

Glerum DM, Tzagoloff A (1994). "Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant.". Proc. Natl. Acad. Sci. U.S.A. 91 (18): 8452-6. PMID 8078902.
Murakami T, Reiter LT, Lupski JR (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.
Reiter LT, Murakami T, Koeuth T, et al. (1998). "The human COX10 gene is disrupted during homologous recombination between the 24 kb proximal and distal CMT1A-REPs.". Hum. Mol. Genet. 6 (9): 1595-603. PMID 9285799.
Kennerson ML, Nassif NT, Dawkins JL, et al. (1998). "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 (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, et al. (2000). "A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency.". Hum. Mol. Genet. 9 (8): 1245-9. PMID 10767350.
Bosetti F, Brizzi F, Barogi S, et al. (2002). "Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease.". Neurobiol. Aging 23 (3): 371-6. PMID 11959398.
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. PMID 12477932.
Antonicka H, Leary SC, Guercin GH, et al. (2004). "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.". Hum. Mol. Genet. 12 (20): 2693-702. doi:10.1093/hmg/ddg284. PMID 12928484.
Williams SL, Valnot I, Rustin P, Taanman JW (2004). "Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1.". J. Biol. Chem. 279 (9): 7462-9. doi:10.1074/jbc.M309232200. PMID 14607829.
Coenen MJ, van den Heuvel LP, Ugalde C, et al. (2004). "Cytochrome c oxidase biogenesis in a patient with a mutation in COX10 gene.". Ann. Neurol. 56 (4): 560-4. doi:10.1002/ana.20229. PMID 15455402.
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. PMID 15489334.
Veluthakal R, Kaur H, Goalstone M, Kowluru A (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.