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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.
30-AUG-2017, entry version 150.
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), ENZYME 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]
ENZYME 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 ENZYME 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};
-!- ENZYME 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; CAI43113.1; -; Genomic_DNA.
EMBL; AL591908; CAI43113.1; JOINED; Genomic_DNA.
EMBL; AL049733; CAI43114.1; -; Genomic_DNA.
EMBL; AL591908; CAI43114.1; JOINED; Genomic_DNA.
EMBL; AL591908; CAH71675.1; -; Genomic_DNA.
EMBL; AL049733; CAH71675.1; JOINED; Genomic_DNA.
EMBL; AL591908; CAH71676.1; -; Genomic_DNA.
EMBL; AL049733; CAH71676.1; JOINED; 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]
UniGene; Hs.171458; -.
ProteinModelPortal; Q16206; -.
SMR; Q16206; -.
BioGrid; 115758; 14.
IntAct; Q16206; 12.
MINT; MINT-4825886; -.
STRING; 9606.ENSP00000337146; -.
ChEMBL; CHEMBL3714292; -.
DrugBank; DB04915; Phenoxodiol.
iPTMnet; Q16206; -.
PhosphoSitePlus; Q16206; -.
BioMuta; ENOX2; -.
DMDM; 34978371; -.
MaxQB; Q16206; -.
PaxDb; Q16206; -.
PeptideAtlas; Q16206; -.
PRIDE; Q16206; -.
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; -.
HOVERGEN; HBG051083; -.
InParanoid; Q16206; -.
OMA; GRLQHTF; -.
OrthoDB; EOG091G038C; -.
PhylomeDB; Q16206; -.
TreeFam; TF323802; -.
SIGNOR; Q16206; -.
ChiTaRS; ENOX2; human.
GeneWiki; ENOX2; -.
GenomeRNAi; 10495; -.
PRO; PR:Q16206; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000165675; -.
CleanEx; HS_ENOX2; -.
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:0016049; P:cell growth; NAS: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.
InterPro; IPR034140; ENOX_RRM.
InterPro; IPR000504; RRM_dom.
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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