Ecto-NOX disulfide-thiol exchanger 2

Details

Name

Ecto-NOX disulfide-thiol exchanger 2

Synonyms

• APK1 antigen
• COVA1
• Cytosolic ovarian carcinoma antigen 1
• tNOX
• Tumor-associated hydroquinone oxidase

Gene Name

ENOX2

Organism

Humans

Amino acid sequence

>lcl|BSEQ0004780|Ecto-NOX disulfide-thiol exchanger 2
MQRDFRWLWVYEIGYAADNSRTLNVDSTAMTLPMSDPTAWATAMNNLGMAPLGIAGQPIL
PDFDPALGMMTGIPPITPMMPGLGIVPPPIPPDMPVVKEIIHCKSCTLFPPNPNLPPPAT
RERPPGCKTVFVGGLPENGTEQIIVEVFEQCGEIIAIRKSKKNFCHIRFAEEYMVDKALY
LSGYRIRLGSSTDKKDTGRLHVDFAQARDDLYEWECKQRMLAREERHRRRMEEERLRPPS
PPPVVHYSDHECSIVAEKLKDDSKFSEAVQTLLTWIERGEVNRRSANNFYSMIQSANSHV
RRLVNEKAAHEKDMEEAKEKFKQALSGILIQFEQIVAVYHSASKQKAWDHFTKAQRKNIS
VWCKQAEEIRNIHNDELMGIRREEEMEMSDDEIEEMTETKETEESALVSQAEALKEENDS
LRWQLDAYRNEVELLKQEQGKVHREDDPNKEQQLKLLQQALQGMQQHLLKVQEEYKKKEA
ELEKLKDDKLQVEKMLENLKEKESCASRLCASNQDSEYPLEKTMNSSPIKSEREALLVGI
ISTFLHVHPFGASIEYICSYLHRLDNKICTSDVECLMGRLQHTFKQEMTGVGASLEKRWK
FCGFEGLKLT

Number of residues

610

Molecular Weight

70081.515

Theoretical pI

5.78

GO Classification

Functions

nucleic acid binding / nucleotide binding / protein disulfide oxidoreductase activity

Processes

cell growth / oxidation-reduction process / regulation of growth / ultradian rhythm

Components

cytosol / external side of plasma membrane / extracellular space

General Function

Protein disulfide oxidoreductase activity

Specific Function

May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock.

Pfam Domain Function

• RRM_1 (PF00076)

Transmembrane Regions

Not Available

Cellular Location

Cell membrane

Gene sequence

>lcl|BSEQ0016790|Ecto-NOX disulfide-thiol exchanger 2 (ENOX2)
ATGACACTACCTATGTCTGATCCAACTGCATGGGCCACAGCAATGAATAATCTTGGAATG
GCACCGCTGGGAATTGCCGGACAACCAATTTTACCTGACTTTGATCCTGCTCTTGGAATG
ATGACTGGAATTCCACCAATAACTCCAATGATGCCTGGTTTGGGAATAGTACCTCCACCA
ATTCCTCCAGATATGCCAGTAGTAAAAGAGATCATACACTGTAAAAGCTGCACGCTCTTC
CCTCCAAATCCAAATCTCCCACCTCCTGCAACCCGAGAAAGACCACCAGGATGCAAAACA
GTATTTGTGGGTGGTCTGCCTGAAAATGGGACAGAGCAAATCATTGTGGAAGTTTTCGAG
CAGTGTGGAGAGATCATTGCCATTCGCAAGAGCAAGAAGAACTTCTGCCACATTCGCTTT
GCTGAGGAGTACATGGTGGACAAAGCCCTGTATCTGTCTGGTTACCGCATTCGCCTGGGC
TCTAGTACTGACAAGAAGGACACAGGCAGACTCCACGTTGATTTCGCACAGGCTCGAGAT
GACCTGTATGAGTGGGAGTGTAAACAGCGTATGCTAGCCAGAGAGGAGCGCCATCGTAGA
AGAATGGAAGAAGAAAGATTGCGTCCACCATCTCCACCCCCAGTGGTCCACTATTCAGAT
CATGAATGCAGCATTGTTGCTGAAAAATTAAAAGATGATTCCAAATTCTCAGAAGCTGTA
CAGACCTTGCTTACCTGGATAGAGCGAGGAGAGGTCAACCGTCGTAGCGCCAATAACTTC
TACTCCATGATCCAGTCGGCCAACAGCCATGTCCGCCGCCTGGTGAACGAGAAAGCTGCC
CATGAGAAAGATATGGAAGAAGCAAAGGAGAAGTTCAAGCAGGCCCTTTCTGGAATTCTC
ATTCAATTTGAGCAGATAGTGGCTGTGTACCATTCCGCCTCCAAGCAGAAGGCATGGGAC
CACTTCACAAAAGCCCAGCGGAAGAACATCAGCGTGTGGTGCAAACAAGCTGAGGAAATT
CGCAACATTCATAATGATGAATTAATGGGAATCAGGCGAGAAGAAGAAATGGAAATGTCT
GATGATGAAATAGAAGAAATGACAGAAACAAAAGAAACTGAGGAATCAGCCTTAGTATCA
CAGGCAGAAGCTCTGAAGGAAGAAAATGACAGCCTCCGTTGGCAGCTCGATGCCTACCGG
AATGAAGTAGAACTGCTCAAGCAAGAACAAGGCAAAGTCCACAGAGAAGATGACCCTAAC
AAAGAACAGCAGCTGAAACTCCTGCAACAAGCCCTGCAAGGAATGCAACAGCATCTACTC
AAAGTCCAAGAGGAATACAAAAAGAAAGAAGCTGAACTTGAAAAACTCAAAGATGACAAG
TTACAGGTGGAAAAAATGTTGGAAAATCTTAAAGAAAAGGAAAGCTGTGCTTCTAGGCTG
TGTGCCTCAAACCAGGATAGCGAATACCCTCTTGAGAAGACCATGAACAGCAGTCCTATC
AAATCTGAACGTGAAGCACTGCTAGTGGGGATTATCTCCACATTCCTTCATGTTCACCCA
TTTGGAGCAAGCATTGAATACATCTGTTCCTACTTGCACCGTCTTGATAATAAGATCTGC
ACCAGCGATGTGGAGTGTCTCATGGGTAGACTCCAGCATACCTTCAAGCAGGAAATGACT
GGAGTTGGAGCCAGCCTGGAAAAGAGATGGAAATTCTGTGGCTTCGAGGGCTTGAAGCTG
ACCTAA

Chromosome Location

X

Locus

Xq25-q26.2

External Identifiers

Resource	Link
UniProtKB ID	Q16206
UniProtKB Entry Name	ENOX2_HUMAN
GenBank Gene ID	AF207881
GenAtlas ID	ENOX2
HGNC ID	HGNC:2259

General References

1. Chueh PJ, Kim C, Cho N, Morre DM, Morre DJ: Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface. Biochemistry. 2002 Mar 19;41(11):3732-41. [Article]
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4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
5. Yantiri F, Morre DJ: Isolation and characterization of a tumor-associated NADH oxidase (tNOX) from the HeLa cell surface. Arch Biochem Biophys. 2001 Jul 15;391(2):149-59. [Article]
6. Chang K, Pastan I: 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. 1994 Apr 1;57(1):90-7. [Article]
7. Dai S, Morre DJ, Geilen CC, Almond-Roesler B, Orfanos CE, Morre DM: Inhibition of plasma membrane NADH oxidase activity and growth of HeLa cells by natural and synthetic retinoids. Mol Cell Biochem. 1997 Jan;166(1-2):101-9. [Article]
8. Morre DJ, Chueh PJ, Lawler J, Morre DM: 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. 1998 Oct;30(5):477-87. [Article]
9. Kishi T, Morre DM, Morre DJ: The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity. Biochim Biophys Acta. 1999 May 26;1412(1):66-77. [Article]
10. Kelker M, Kim C, Chueh PJ, Guimont R, Morre DM, Morre DJ: Cancer isoform of a tumor-associated cell surface NADH oxidase (tNOX) has properties of a prion. Biochemistry. 2001 Jun 26;40(25):7351-4. [Article]
11. Morre DJ, Sedlak D, Tang X, Chueh PJ, Geng T, Morre DM: Surface NADH oxidase of HeLa cells lacks intrinsic membrane binding motifs. Arch Biochem Biophys. 2001 Aug 15;392(2):251-6. [Article]
12. Cho N, Chueh PJ, Kim C, Caldwell S, Morre DM, Morre DJ: Monoclonal antibody to a cancer-specific and drug-responsive hydroquinone (NADH) oxidase from the sera of cancer patients. Cancer Immunol Immunother. 2002 May;51(3):121-9. Epub 2002 Feb 27. [Article]
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Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB04915	Idronoxil	investigational	unknown		Details