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Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]

 ENOX2_HUMAN             Reviewed;         610 AA.
Q16206; A8K197; A8K1C2; Q5VTJ1; Q5VTJ2; Q8WUX0; Q9NTP6; Q9UH82;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 2.
08-MAY-2019, entry version 160.
RecName: Full=Ecto-NOX disulfide-thiol exchanger 2;
AltName: Full=APK1 antigen;
AltName: Full=Cytosolic ovarian carcinoma antigen 1;
AltName: Full=Tumor-associated hydroquinone oxidase;
Short=tNOX;
Includes:
RecName: Full=Hydroquinone [NADH] oxidase;
EC=1.-.-.-;
Includes:
RecName: Full=Protein disulfide-thiol oxidoreductase;
EC=1.-.-.-;
Name=ENOX2; Synonyms=COVA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ACTIVITY REGULATION,
MUTAGENESIS OF MET-396; CYS-505; CYS-510; HIS-546; CYS-558; HIS-562;
CYS-569; CYS-575; GLY-592 AND CYS-602, AND COFACTOR.
PubMed=11888291; DOI=10.1021/bi012041t;
Chueh P.-J., Kim C., Cho N., Morre D.M., Morre D.J.;
"Molecular cloning and characterization of a tumor-associated, growth-
related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the
HeLa cell surface.";
Biochemistry 41:3732-3741(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-405.
Rhodes S., Huckle E.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 86-90; 249-266 AND 318-333.
TISSUE=Cervix carcinoma;
PubMed=11437345; DOI=10.1006/abbi.2001.2404;
Yantiri F., Morre D.J.;
"Isolation and characterization of a tumor-associated NADH oxidase
(tNOX) from the HeLa cell surface.";
Arch. Biochem. Biophys. 391:149-159(2001).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 275-610, SUBCELLULAR LOCATION, AND
GLYCOSYLATION.
TISSUE=Ovarian carcinoma;
PubMed=8150545; DOI=10.1002/ijc.2910570117;
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 57:90-97(1994).
[9]
ACTIVITY REGULATION.
PubMed=9046026; DOI=10.1023/A:1006866726050;
Dai S., Morre D.J., Geilen C.C., Almond-Roesler B., Orfanos C.E.,
Morre D.M.;
"Inhibition of plasma membrane NADH oxidase activity and growth of
HeLa cells by natural and synthetic retinoids.";
Mol. Cell. Biochem. 166:101-109(1997).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
PubMed=9932650; DOI=10.1023/A:1020594214379;
Morre D.J., Chueh P.-J., Lawler J., Morre D.M.;
"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. 30:477-487(1998).
[11]
HYDROQUINONE OXIDASE ACTIVITY.
PubMed=10354495; DOI=10.1016/S0005-2728(99)00049-3;
Kishi T., Morre D.M., Morre D.J.;
"The plasma membrane NADH oxidase of HeLa cells has hydroquinone
oxidase activity.";
Biochim. Biophys. Acta 1412:66-77(1999).
[12]
PRION-LIKE PROPERTIES.
PubMed=11412089; DOI=10.1021/bi010596i;
Kelker M., Kim C., Chueh P.-J., Guimont R., Morre D.M., Morre D.J.;
"Cancer isoform of a tumor-associated cell surface NADH oxidase (tNOX)
has properties of a prion.";
Biochemistry 40:7351-7354(2001).
[13]
SUBCELLULAR LOCATION.
PubMed=11488599; DOI=10.1006/abbi.2001.2436;
Morre D.J., Sedlak D., Tang X., Chueh P.-J., Geng T., Morre D.M.;
"Surface NADH oxidase of HeLa cells lacks intrinsic membrane binding
motifs.";
Arch. Biochem. Biophys. 392:251-256(2001).
[14]
DISEASE.
PubMed=11941450; DOI=10.1007/s00262-001-0262-2;
Cho N., Chueh P.-J., Kim C., Caldwell S., Morre D.M., Morre D.J.;
"Monoclonal antibody to a cancer-specific and drug-responsive
hydroquinone (NADH) oxidase from the sera of cancer patients.";
Cancer Immunol. Immunother. 51:121-129(2002).
[15]
FUNCTION IN BIOLOGICAL CLOCK CONTROL.
PubMed=12356293; DOI=10.1021/bi020392h;
Morre D.J., Chueh P.-J., Pletcher J., Tang X., Wu L.Y., Morre D.M.;
"Biochemical basis for the biological clock.";
Biochemistry 41:11941-11945(2002).
[16]
VARIANT ILE-202.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- 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. {ECO:0000269|PubMed:12356293,
ECO:0000269|PubMed:9932650}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:11888291};
-!- ACTIVITY REGULATION: Inhibited by the antitumor sulfonylurea
LY181984, the vabilloid capsaicin, and retinoids.
{ECO:0000269|PubMed:11888291, ECO:0000269|PubMed:9046026,
ECO:0000269|PubMed:9932650}.
-!- INTERACTION:
Q96Q77:CIB3; NbExp=3; IntAct=EBI-10179508, EBI-10292696;
Q8TC92:ENOX1; NbExp=3; IntAct=EBI-10179508, EBI-713221;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-10179508, EBI-10178634;
Q6P2C6:MLLT6; NbExp=3; IntAct=EBI-10179508, EBI-5773143;
P09012:SNRPA; NbExp=3; IntAct=EBI-10179508, EBI-607085;
O00463:TRAF5; NbExp=3; IntAct=EBI-10179508, EBI-523498;
-!- SUBCELLULAR LOCATION: Cell membrane. Secreted, extracellular
space. Note=Extracellular and plasma membrane-associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q16206-1; Sequence=Displayed;
Name=2;
IsoId=Q16206-2; Sequence=VSP_015719;
-!- TISSUE SPECIFICITY: Found in the sera of cancer patients with a
wide variety of cancers including breast, prostate, lung and
ovarian cancers, leukemias, and lymphomas. Not found in the serum
of healthy volunteers or patients with disorders other than
cancer. Probably shed into serum by cancer cells. Found on the
cell borders of renal, kidney and ovarian carcinomas but not on
the borders of surrounding non-cancerous stromal cells.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:8150545}.
-!- MISCELLANEOUS: Has several properties associated with prions
including resistance to proteases, resistance to cyanogen bromide
digestion, and the ability to form amyloid filaments resembling
those of spongiform encephalopathies.
-!- SIMILARITY: Belongs to the ENOX family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB30428.1; Type=Frameshift; Positions=302, 357; Evidence={ECO:0000305};
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EMBL; AF207881; AAF20934.2; -; mRNA.
EMBL; AK000353; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK289837; BAF82526.1; -; mRNA.
EMBL; AK289812; BAF82501.1; -; mRNA.
EMBL; AL049733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471107; EAX11796.1; -; Genomic_DNA.
EMBL; CH471107; EAX11797.1; -; Genomic_DNA.
EMBL; BC019254; AAH19254.2; -; mRNA.
EMBL; BC140874; AAI40875.1; -; mRNA.
EMBL; AL133207; CAB61581.2; -; mRNA.
EMBL; S72904; AAB30428.1; ALT_FRAME; mRNA.
CCDS; CCDS14626.1; -. [Q16206-1]
CCDS; CCDS14627.1; -. [Q16206-2]
PIR; I54780; I54780.
RefSeq; NP_001268665.1; NM_001281736.1. [Q16206-2]
RefSeq; NP_006366.2; NM_006375.3. [Q16206-2]
RefSeq; NP_872114.1; NM_182314.2. [Q16206-1]
RefSeq; XP_005262411.1; XM_005262354.3. [Q16206-1]
RefSeq; XP_011529549.1; XM_011531247.2. [Q16206-1]
RefSeq; XP_011529551.1; XM_011531249.2. [Q16206-1]
RefSeq; XP_011529553.1; XM_011531251.2. [Q16206-2]
RefSeq; XP_016884715.1; XM_017029226.1. [Q16206-1]
RefSeq; XP_016884716.1; XM_017029227.1. [Q16206-1]
RefSeq; XP_016884717.1; XM_017029228.1. [Q16206-1]
SMR; Q16206; -.
BioGrid; 115758; 16.
IntAct; Q16206; 12.
MINT; Q16206; -.
STRING; 9606.ENSP00000337146; -.
ChEMBL; CHEMBL3714292; -.
DrugBank; DB04915; Phenoxodiol.
iPTMnet; Q16206; -.
PhosphoSitePlus; Q16206; -.
BioMuta; ENOX2; -.
DMDM; 34978371; -.
jPOST; Q16206; -.
MaxQB; Q16206; -.
PaxDb; Q16206; -.
PeptideAtlas; Q16206; -.
PRIDE; Q16206; -.
ProteomicsDB; 60838; -.
ProteomicsDB; 60839; -. [Q16206-2]
Ensembl; ENST00000338144; ENSP00000337146; ENSG00000165675. [Q16206-1]
Ensembl; ENST00000370927; ENSP00000359965; ENSG00000165675. [Q16206-1]
Ensembl; ENST00000370935; ENSP00000359973; ENSG00000165675. [Q16206-2]
Ensembl; ENST00000394363; ENSP00000377890; ENSG00000165675. [Q16206-2]
GeneID; 10495; -.
KEGG; hsa:10495; -.
UCSC; uc004evw.5; human. [Q16206-1]
CTD; 10495; -.
DisGeNET; 10495; -.
GeneCards; ENOX2; -.
HGNC; HGNC:2259; ENOX2.
HPA; HPA000514; -.
MIM; 300282; gene.
neXtProt; NX_Q16206; -.
OpenTargets; ENSG00000165675; -.
PharmGKB; PA162385106; -.
eggNOG; ENOG410ITYH; Eukaryota.
eggNOG; ENOG4110UUI; LUCA.
GeneTree; ENSGT00390000006788; -.
InParanoid; Q16206; -.
OMA; FDPNLGM; -.
OrthoDB; 357901at2759; -.
PhylomeDB; Q16206; -.
TreeFam; TF323802; -.
SIGNOR; Q16206; -.
ChiTaRS; ENOX2; human.
GeneWiki; ENOX2; -.
GenomeRNAi; 10495; -.
PRO; PR:Q16206; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000165675; Expressed in 217 organ(s), highest expression level in tendon.
ExpressionAtlas; Q16206; baseline and differential.
Genevisible; Q16206; HS.
GO; GO:0005829; C:cytosol; TAS:ProtInc.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0007624; P:ultradian rhythm; IDA:UniProtKB.
CDD; cd12228; RRM_ENOX; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR038876; ENOX.
InterPro; IPR034140; ENOX_RRM.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR16001; PTHR16001; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Alternative splicing; Biological rhythms; Cell membrane; Coiled coil;
Complete proteome; Copper; Direct protein sequencing;
Electron transport; Glycoprotein; Growth regulation; Membrane; NAD;
Oxidoreductase; Polymorphism; Reference proteome; Secreted; Transport.
CHAIN 1 610 Ecto-NOX disulfide-thiol exchanger 2.
/FTId=PRO_0000079275.
DOMAIN 128 207 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COILED 293 328 {ECO:0000255}.
COILED 381 505 {ECO:0000255}.
COMPBIAS 58 125 Pro-rich.
VAR_SEQ 1 29 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015719.
VARIANT 202 202 V -> I (in dbSNP:rs754363472).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069427.
MUTAGEN 396 396 M->A: No effect on activity but response
to capsaicin is lost.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 505 505 C->A: No effect on activity.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 510 510 C->A: Loss of activity.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 546 546 H->A: Loss of activity.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 558 558 C->A: Period length of activity extended
to 42 minutes.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 562 562 H->A: Loss of activity.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 569 569 C->A: Loss of activity.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 575 575 C->A: Period length of activity extended
to 36 minutes.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 592 592 G->V: Loss of activity.
{ECO:0000269|PubMed:11888291}.
MUTAGEN 602 602 C->A: Period length of activity extended
to 36 minutes.
{ECO:0000269|PubMed:11888291}.
CONFLICT 123 123 R -> G (in Ref. 2; AK000353).
{ECO:0000305}.
CONFLICT 311 311 E -> G (in Ref. 2; AK000353).
{ECO:0000305}.
CONFLICT 326 326 S -> V (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 328 328 I -> V (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 332 332 F -> A (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 406 407 Missing (in Ref. 5; AAH19254).
{ECO:0000305}.
SEQUENCE 610 AA; 70082 MW; C30BC45730B62A57 CRC64;
MQRDFRWLWV YEIGYAADNS RTLNVDSTAM TLPMSDPTAW ATAMNNLGMA PLGIAGQPIL
PDFDPALGMM TGIPPITPMM PGLGIVPPPI PPDMPVVKEI IHCKSCTLFP PNPNLPPPAT
RERPPGCKTV FVGGLPENGT EQIIVEVFEQ CGEIIAIRKS KKNFCHIRFA EEYMVDKALY
LSGYRIRLGS STDKKDTGRL HVDFAQARDD LYEWECKQRM LAREERHRRR MEEERLRPPS
PPPVVHYSDH ECSIVAEKLK DDSKFSEAVQ TLLTWIERGE VNRRSANNFY SMIQSANSHV
RRLVNEKAAH EKDMEEAKEK FKQALSGILI QFEQIVAVYH SASKQKAWDH FTKAQRKNIS
VWCKQAEEIR NIHNDELMGI RREEEMEMSD DEIEEMTETK ETEESALVSQ AEALKEENDS
LRWQLDAYRN EVELLKQEQG KVHREDDPNK EQQLKLLQQA LQGMQQHLLK VQEEYKKKEA
ELEKLKDDKL QVEKMLENLK EKESCASRLC ASNQDSEYPL EKTMNSSPIK SEREALLVGI
ISTFLHVHPF GASIEYICSY LHRLDNKICT SDVECLMGRL QHTFKQEMTG VGASLEKRWK
FCGFEGLKLT


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Related Genes :
[ENOX2 COVA1] Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]
[Enox2 Cova1] Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]
[ENOX1 PIG38] Ecto-NOX disulfide-thiol exchanger 1 (Candidate growth-related and time keeping constitutive hydroquinone [NADH] oxidase) (cCNOX) (Cell proliferation-inducing gene 38 protein) (Constitutive Ecto-NOX) (cNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]
[Enox1] Ecto-NOX disulfide-thiol exchanger 1 (Constitutive Ecto-NOX) (cNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[PLAAT3 HRASLS3 HREV107 PLA2G16] Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HRAS-like suppressor 3) (HRSL3) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[FOLR1 FOLR] Folate receptor alpha (FR-alpha) (Adult folate-binding protein) (FBP) (Folate receptor 1) (Folate receptor, adult) (KB cells FBP) (Ovarian tumor-associated antigen MOv18)
[MUC16 CA125] Mucin-16 (MUC-16) (Ovarian cancer-related tumor marker CA125) (CA-125) (Ovarian carcinoma antigen CA125)
[STK11 LKB1 PJS] Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1) (LKB1) (hLKB1) (Renal carcinoma antigen NY-REN-19)
[DUOX2 LNOX2 THOX2] Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase p138-tox) (NADPH oxidase/peroxidase DUOX2) (NADPH thyroid oxidase 2) (Thyroid oxidase 2) (p138 thyroid oxidase)
[TYR] Tyrosinase (EC 1.14.18.1) (LB24-AB) (Monophenol monooxygenase) (SK29-AB) (Tumor rejection antigen AB)
[GCC2 KIAA0336 RANBP2L4] GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (CLL-associated antigen KW-11) (CTCL tumor antigen se1-1) (Ran-binding protein 2-like 4) (RanBP2L4) (Renal carcinoma antigen NY-REN-53)
[EPCAM GA733-2 M1S2 M4S1 MIC18 TACSTD1 TROP1] Epithelial cell adhesion molecule (Ep-CAM) (Adenocarcinoma-associated antigen) (Cell surface glycoprotein Trop-1) (Epithelial cell surface antigen) (Epithelial glycoprotein) (EGP) (Epithelial glycoprotein 314) (EGP314) (hEGP314) (KS 1/4 antigen) (KSA) (Major gastrointestinal tumor-associated protein GA733-2) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)
[EPHB2 DRT EPHT3 EPTH3 ERK HEK5 TYRO5] Ephrin type-B receptor 2 (EC 2.7.10.1) (Developmentally-regulated Eph-related tyrosine kinase) (ELK-related tyrosine kinase) (EPH tyrosine kinase 3) (EPH-like kinase 5) (EK5) (hEK5) (Renal carcinoma antigen NY-REN-47) (Tyrosine-protein kinase TYRO5) (Tyrosine-protein kinase receptor EPH-3) [Cleaved into: EphB2/CTF1; EphB2/CTF2]
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[NOX1 MOX1 NOH1] NADPH oxidase 1 (NOX-1) (EC 1.-.-.-) (Mitogenic oxidase 1) (MOX-1) (NADH/NADPH mitogenic oxidase subunit P65-MOX) (NOH-1)
[ECI2 DRS1 HCA88 PECI] Enoyl-CoA delta isomerase 2, mitochondrial (EC 5.3.3.8) (DRS-1) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Diazepam-binding inhibitor-related protein 1) (DBI-related protein 1) (Dodecenoyl-CoA isomerase) (Hepatocellular carcinoma-associated antigen 88) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI) (Renal carcinoma antigen NY-REN-1)
[FAS APT1 FAS1 TNFRSF6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[IRAK4] Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-64)
[PDPN GP36 PSEC0003 PSEC0025] Podoplanin (Aggrus) (Glycoprotein 36) (Gp36) (PA2.26 antigen) (T1-alpha) (T1A) [Cleaved into: 29kDa cytosolic podoplanin intracellular domain (PICD)]
[PDIA3 ERP57 ERP60 GRP58] Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60)
[Fas Apt1 Tnfrsf6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[NOXA1 P51NOX] NADPH oxidase activator 1 (NOX activator 1) (Antigen NY-CO-31) (NCF2-like protein) (P67phox-like factor) (p51-nox)
[TYRP1 CAS2 TYRP TYRRP] 5,6-dihydroxyindole-2-carboxylic acid oxidase (DHICA oxidase) (EC 1.14.18.-) (Catalase B) (Glycoprotein 75) (Melanoma antigen gp75) (Tyrosinase-related protein 1) (TRP) (TRP-1) (TRP1)
[MAGEC2 HCA587 MAGEE1] Melanoma-associated antigen C2 (Cancer/testis antigen 10) (CT10) (Hepatocellular carcinoma-associated antigen 587) (MAGE-C2 antigen) (MAGE-E1 antigen)
[Ceacam1] Carcinoembryonic antigen-related cell adhesion molecule 1 (ATP-dependent taurocolate-carrier protein) (Cell-CAM 105) (C-CAM 105) (Ecto-ATPase) (GP110) (pp120) (CD antigen CD66a)
[TRMT10C MRPP1 RG9MTD1] tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)
[ENTPD1 CD39] Ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) (EC 3.6.1.5) (Ecto-ATP diphosphohydrolase 1) (Ecto-ATPDase 1) (Ecto-ATPase 1) (Ecto-apyrase) (Lymphoid cell activation antigen) (CD antigen CD39)
[SLC3A2 MDU1] 4F2 cell-surface antigen heavy chain (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98)
[VTE3 APG1 IE37 At3g63410 MAA21.40] 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase, chloroplastic (EC 2.1.1.295) (37 kDa inner envelope membrane protein) (E37) (MPBQ/MSBQ methyltransferase) (Protein ALBINO OR PALE GREEN MUTANT 1) (Protein INNER ENVELOPE PROTEIN 37) (Protein VITAMIN E DEFECTIVE 3)

Bibliography :
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