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
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
ResourceLink
UniProtKB IDQ16206
UniProtKB Entry NameENOX2_HUMAN
GenBank Gene IDAF207881
GenAtlas IDENOX2
HGNC IDHGNC: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. [PubMed:11888291]
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  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. [PubMed:11437345]
  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. [PubMed:8150545]
  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. [PubMed:9046026]
  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. [PubMed:9932650]
  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. [PubMed:10354495]
  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. [PubMed:11412089]
  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. [PubMed:11488599]
  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. [PubMed:11941450]
  13. Morre DJ, Chueh PJ, Pletcher J, Tang X, Wu LY, Morre DM: Biochemical basis for the biological clock. Biochemistry. 2002 Oct 8;41(40):11941-5. [PubMed:12356293]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04915IdronoxilinvestigationalunknownDetails