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Identification
HMDB Protein ID HMDBP01690
Secondary Accession Numbers
  • 7027
Name Ecto-NOX disulfide-thiol exchanger 2
Synonyms
  1. APK1 antigen
  2. Cytosolic ovarian carcinoma antigen 1
  3. Hydroquinone [NADH] oxidase
  4. Protein disulfide-thiol oxidoreductase
  5. Tumor-associated hydroquinone oxidase
  6. tNOX
Gene Name ENOX2
Protein Type Unknown
Biological Properties
General Function Involved in nucleotide binding
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
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
nucleotide binding
nucleic acid binding
Cellular Location
  1. Cell membrane
  2. Secreted
  3. extracellular space
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs ENOX2
Gene Sequence
>1833 bp
ATGCAAAGAGATTTTAGATGGCTGTGGGTCTACGAAATAGGCTATGCAGCCGATAACAGT
AGAACTCTGAACGTGGATTCCACTGCAATGACACTACCTATGTCTGATCCAACTGCATGG
GCCACAGCAATGAATAATCTTGGAATGGCACCGCTGGGAATTGCCGGACAACCAATTTTA
CCTGACTTTGATCCTGCTCTTGGAATGATGACTGGAATTCCACCAATAACTCCAATGATG
CCTGGTTTGGGAATAGTACCTCCACCAATTCCTCCAGATATGCCAGTAGTAAAAGAGATC
ATACACTGTAAAAGCTGCACGCTCTTCCCTCCAAATCCAAATCTCCCACCTCCTGCAACC
CGAGAAAGACCACCAGGATGCAAAACAGTATTTGTGGGTGGTCTGCCTGAAAATGGGACA
GAGCAAATCATTGTGGAAGTTTTCGAGCAGTGTGGAGAGATCATTGCCATTCGCAAGAGC
AAGAAGAACTTCTGCCACATTCGCTTTGCTGAGGAGTACATGGTGGACAAAGCCCTGTAT
CTGTCTGGTTACCGCATTCGCCTGGGCTCTAGTACTGACAAGAAGGACACAGGCAGACTC
CACGTTGATTTCGCACAGGCTCGAGATGACCTGTATGAGTGGGAGTGTAAACAGCGTATG
CTAGCCAGAGAGGAGCGCCATCGTAGAAGAATGGAAGAAGAAAGATTGCGTCCACCATCT
CCACCCCCAGTGGTCCACTATTCAGATCATGAATGCAGCATTGTTGCTGAAAAATTAAAA
GATGATTCCAAATTCTCAGAAGCTGTACAGACCTTGCTTACCTGGATAGAGCGAGGAGAG
GTCAACCGTCGTAGCGCCAATAACTTCTACTCCATGATCCAGTCGGCCAACAGCCATGTC
CGCCGCCTGGTGAACGAGAAAGCTGCCCATGAGAAAGATATGGAAGAAGCAAAGGAGAAG
TTCAAGCAGGCCCTTTCTGGAATTCTCATTCAATTTGAGCAGATAGTGGCTGTGTACCAT
TCCGCCTCCAAGCAGAAGGCATGGGACCACTTCACAAAAGCCCAGCGGAAGAACATCAGC
GTGTGGTGCAAACAAGCTGAGGAAATTCGCAACATTCATAATGATGAATTAATGGGAATC
AGGCGAGAAGAAGAAATGGAAATGTCTGATGATGAAATAGAAGAAATGACAGAAACAAAA
GAAACTGAGGAATCAGCCTTAGTATCACAGGCAGAAGCTCTGAAGGAAGAAAATGACAGC
CTCCGTTGGCAGCTCGATGCCTACCGGAATGAAGTAGAACTGCTCAAGCAAGAACAAGGC
AAAGTCCACAGAGAAGATGACCCTAACAAAGAACAGCAGCTGAAACTCCTGCAACAAGCC
CTGCAAGGAATGCAACAGCATCTACTCAAAGTCCAAGAGGAATACAAAAAGAAAGAAGCT
GAACTTGAAAAACTCAAAGATGACAAGTTACAGGTGGAAAAAATGTTGGAAAATCTTAAA
GAAAAGGAAAGCTGTGCTTCTAGGCTGTGTGCCTCAAACCAGGATAGCGAATACCCTCTT
GAGAAGACCATGAACAGCAGTCCTATCAAATCTGAACGTGAAGCACTGCTAGTGGGGATT
ATCTCCACATTCCTTCATGTTCACCCATTTGGAGCAAGCATTGAATACATCTGTTCCTAC
TTGCACCGTCTTGATAATAAGATCTGCACCAGCGATGTGGAGTGTCTCATGGGTAGACTC
CAGCATACCTTCAAGCAGGAAATGACTGGAGTTGGAGCCAGCCTGGAAAAGAGATGGAAA
TTCTGTGGCTTCGAGGGCTTGAAGCTGACCTAA
Protein Properties
Number of Residues 610
Molecular Weight 70081.5
Theoretical pI 5.78
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ecto-NOX disulfide-thiol exchanger 2
MQRDFRWLWVYEIGYAADNSRTLNVDSTAMTLPMSDPTAWATAMNNLGMAPLGIAGQPIL
PDFDPALGMMTGIPPITPMMPGLGIVPPPIPPDMPVVKEIIHCKSCTLFPPNPNLPPPAT
RERPPGCKTVFVGGLPENGTEQIIVEVFEQCGEIIAIRKSKKNFCHIRFAEEYMVDKALY
LSGYRIRLGSSTDKKDTGRLHVDFAQARDDLYEWECKQRMLAREERHRRRMEEERLRPPS
PPPVVHYSDHECSIVAEKLKDDSKFSEAVQTLLTWIERGEVNRRSANNFYSMIQSANSHV
RRLVNEKAAHEKDMEEAKEKFKQALSGILIQFEQIVAVYHSASKQKAWDHFTKAQRKNIS
VWCKQAEEIRNIHNDELMGIRREEEMEMSDDEIEEMTETKETEESALVSQAEALKEENDS
LRWQLDAYRNEVELLKQEQGKVHREDDPNKEQQLKLLQQALQGMQQHLLKVQEEYKKKEA
ELEKLKDDKLQVEKMLENLKEKESCASRLCASNQDSEYPLEKTMNSSPIKSEREALLVGI
ISTFLHVHPFGASIEYICSYLHRLDNKICTSDVECLMGRLQHTFKQEMTGVGASLEKRWK
FCGFEGLKLT
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q16206
UniProtKB/Swiss-Prot Entry Name ENOX2_HUMAN
PDB IDs Not Available
GenBank Gene ID AF207881
GeneCard ID ENOX2
GenAtlas ID ENOX2
HGNC ID HGNC:2259
References
General References
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  4. 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 ]
  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 ]