ENOX2
| Ecto-NOX disulfide-thiol exchanger 2 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | ENOX2 ; APK1; COVA1; tNOX | ||||||||||||
| External IDs | OMIM: 300282 MGI: 2384799 HomoloGene: 17120 GeneCards: ENOX2 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 10495 | 209224 | |||||||||||
| Ensembl | ENSG00000165675 | ENSMUSG00000031109 | |||||||||||
| UniProt | Q16206 | Q8R0Z2 | |||||||||||
| RefSeq (mRNA) | NM_001281736 | NM_001271447 | |||||||||||
| RefSeq (protein) | NP_001268665 | NP_001258376 | |||||||||||
| Location (UCSC) |
Chr X: 130.62 – 130.9 Mb |
Chr X: 49.01 – 49.29 Mb | |||||||||||
| PubMed search | |||||||||||||
Ecto-NOX disulfide-thiol exchanger 2 is a protein that in humans is encoded by the ENOX2 gene.[1][2][3]
The protein encoded by this gene is a growth-related cell surface protein. It was identified because it reacts with the monoclonal antibody KI in cells, such as the ovarian carcinoma line OVCAR-3, also expressing the CAKI surface glycoprotein. The encoded protein has two enzymatic activities: catalysis of hydroquinone or NADH oxidation, and protein disulfide interchange. The two activities alternate with a period length of about 24 minutes. The encoded protein also displays prion-like properties. Two transcript variants encoding different isoforms have been found for this gene.[3]
References
- ↑ Chang K, Pastan I (May 1994). "Molecular cloning and expression of a cDNA encoding a protein detected by the K1 antibody from an ovarian carcinoma (OVCAR-3) cell line". Int J Cancer 57 (1): 90–7. doi:10.1002/ijc.2910570117. PMID 8150545.
- ↑ Chueh PJ, Kim C, Cho N, Morre DM, Morre DJ (Mar 2002). "Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface". Biochemistry 41 (11): 3732–41. doi:10.1021/bi012041t. PMID 11888291.
- 1 2 "Entrez Gene: COVA1 cytosolic ovarian carcinoma antigen 1".
Further reading
- Tarasoutchi F, Grinberg M, de Figueiredo Neto JA; et al. (1991). "[Mitral valve aneurysm associated with mitral insufficiency in absence of aortic insufficiency]". Arq. Bras. Cardiol. 56 (3): 231–4. PMID 1888291.
- Dai S, Morré DJ, Geilen CC; et al. (1997). "Inhibition of plasma membrane NADH oxidase activity and growth of HeLa cells by natural and synthetic retinoids.". Mol. Cell. Biochem. 166 (1-2): 101–9. doi:10.1023/A:1006866726050. PMID 9046026.
- Morré DJ, Chueh PJ, Lawler J, Morré DM (1999). "The sulfonylurea-inhibited NADH oxidase activity of HeLa cell plasma membranes has properties of a protein disulfide-thiol oxidoreductase with protein disulfide-thiol interchange activity.". J. Bioenerg. Biomembr. 30 (5): 477–87. doi:10.1023/A:1020594214379. PMID 9932650.
- Kishi T, Morré DM, Morré DJ (1999). "The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity.". Biochim. Biophys. Acta 1412 (1): 66–77. doi:10.1016/S0005-2728(99)00049-3. PMID 10354495.
- Kelker M, Kim C, Chueh PJ; et al. (2001). "Cancer isoform of a tumor-associated cell surface NADH oxidase (tNOX) has properties of a prion.". Biochemistry 40 (25): 7351–4. doi:10.1021/bi010596i. PMID 11412089.
- Yantiri F, Morré DJ (2001). "Isolation and characterization of a tumor-associated NADH oxidase (tNOX) from the HeLa cell surface.". Arch. Biochem. Biophys. 391 (2): 149–59. doi:10.1006/abbi.2001.2404. PMID 11437345.
- Morré DJ, Sedlak D, Tang X; et al. (2001). "Surface NADH oxidase of HeLa cells lacks intrinsic membrane binding motifs.". Arch. Biochem. Biophys. 392 (2): 251–6. doi:10.1006/abbi.2001.2436. PMID 11488599.
- Chueh PJ, Morré DM, Morré DJ (2002). "A site-directed mutagenesis analysis of tNOX functional domains.". Biochim. Biophys. Acta 1594 (1): 74–83. doi:10.1016/s0167-4838(01)00286-2. PMID 11825610.
- Cho N, Chueh PJ, Kim C; et al. (2002). "Monoclonal antibody to a cancer-specific and drug-responsive hydroquinone (NADH) oxidase from the sera of cancer patients.". Cancer Immunol. Immunother. 51 (3): 121–9. doi:10.1007/s00262-001-0262-2. PMID 11941450.
- Morré DJ, Chueh PJ, Pletcher J; et al. (2002). "Biochemical basis for the biological clock.". Biochemistry 41 (40): 11941–5. doi:10.1021/bi020392h. PMID 12356293.
- 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.
- 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.
- Chueh PJ, Wu LY, Morré DM, Morré DJ (2005). "tNOX is both necessary and sufficient as a cellular target for the anticancer actions of capsaicin and the green tea catechin (-)-epigallocatechin-3-gallate.". BioFactors 20 (4): 235–49. PMID 15706060.
- Ross MT, Grafham DV, Coffey AJ; et al. (2005). "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
- 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.
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