COX7A2L

From Wikipedia, the free encyclopedia


Cytochrome c oxidase subunit VIIa polypeptide 2 like
Identifiers
Symbol(s) COX7A2L; COX7AR; COX7RP; EB1; SIG81
External IDs OMIM: 605771 MGI106015 HomoloGene3463
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 9167 20463
Ensembl ENSG00000115944 ENSMUSG00000024248
Uniprot O14548 Q3U7R2
Refseq NM_004718 (mRNA)
NP_004709 (protein)
NM_009187 (mRNA)
NP_033213 (protein)
Location Chr 2: 42.43 - 42.45 Mb Chr 17: 83.41 - 83.42 Mb
Pubmed search [1] [2]

Cytochrome c oxidase subunit VIIa polypeptide 2 like, also known as COX7A2L, 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 a protein similar to polypeptides 1 and 2 of subunit VIIa in the C-terminal region, and also highly similar to the mouse Sig81 protein sequence. This gene is expressed in all tissues, and upregulated in a breast cancer cell line after estrogen treatment. It is possible that this gene represents a regulatory subunit of COX and mediates the higher level of energy production in target cells by estrogen.[1]

[edit] References

[edit] Further reading

  • Segade F, Hurlé B, Claudio E, et al. (1996). "Identification of an additional member of the cytochrome c oxidase subunit VIIa family of proteins.". J. Biol. Chem. 271 (21): 12343–9. PMID 8647836. 
  • Watanabe T, Inoue S, Hiroi H, et al. (1998). "Isolation of estrogen-responsive genes with a CpG island library.". Mol. Cell. Biol. 18 (1): 442–9. PMID 9418891. 
  • Schmidt TR, Goodman M, Grossman LI (1999). "Molecular evolution of the COX7A gene family in primates.". Mol. Biol. Evol. 16 (5): 619–26. PMID 10335655. 
  • Lee N, Daly MJ, Delmonte T, et al. (2001). "A genomewide linkage-disequilibrium scan localizes the Saguenay-Lac-Saint-Jean cytochrome oxidase deficiency to 2p16.". Am. J. Hum. Genet. 68 (2): 397–409. PMID 11156535. 
  • 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. 
  • Schmidt TR, Doan JW, Goodman M, Grossman LI (2004). "Retention of a duplicate gene through changes in subcellular targeting: an electron transport protein homologue localizes to the golgi.". J. Mol. Evol. 57 (2): 222–8. doi:10.1007/s00239-003-2468-8. PMID 14562965. 
  • 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. PMID 15489334. 
  • 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.