ENOX2

From Wikipedia, the free encyclopedia

Cytosolic ovarian carcinoma antigen 1

Identifiers

COVA1; APK1; tNOX

External IDs

OMIM: 300282 MGI: 2384799 HomoloGene: 17120

Gene ontology
Molecular Function:	• nucleotide binding • nucleic acid binding • copper ion binding • protein disulfide oxidoreductase activity • oxidoreductase activity
Cellular Component:	• cytosol • external side of plasma membrane • membrane
Biological Process:	• regulation of cell growth • electron transport • transport • ultradian rhythm

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006375 (mRNA)
NP_006366 (protein)

NM_145951 (mRNA)
NP_666063 (protein)

Location

Chr X: 129.59 - 129.86 Mb

Chr X: 45.26 - 45.53 Mb

Pubmed search

[1]

[2]

Cytosolic ovarian carcinoma antigen 1, also known as COVA1, is a human gene.^[1]

The protein encoded by this gene is a growth-related cell surface protein. It was identifed 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: COVA1 cytosolic ovarian carcinoma antigen 1.

[edit] 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.
Chang K, Pastan I (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. PMID 8150545.
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. 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. 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. 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. 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. PMID 11825610.
Chueh PJ, Kim C, Cho N, et al. (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. PMID 11888291.
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. 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. 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. 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. 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.