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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_HUMAN             Reviewed;         643 AA.
Q8TC92; A4GU15; A6NMH9; B7Z5K1; Q2TU81; Q5VT11; Q9NWE0;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
20-JUN-2018, entry version 136.
RecName: Full=Ecto-NOX disulfide-thiol exchanger 1;
AltName: Full=Candidate growth-related and time keeping constitutive hydroquinone [NADH] oxidase;
Short=cCNOX;
AltName: Full=Cell proliferation-inducing gene 38 protein;
AltName: Full=Constitutive Ecto-NOX;
Short=cNOX;
Includes:
RecName: Full=Hydroquinone [NADH] oxidase;
EC=1.-.-.-;
Includes:
RecName: Full=Protein disulfide-thiol oxidoreductase;
EC=1.-.-.-;
Name=ENOX1; ORFNames=PIG38;
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), FUNCTION, AND VARIANT ASP-16.
TISSUE=Cervix carcinoma;
PubMed=19055324; DOI=10.1021/bi801073p;
Jiang Z., Gorenstein N.M., Morre D.M., Morre D.J.;
"Molecular cloning and characterization of a candidate human growth-
related and time-keeping constitutive cell surface hydroquinone (NADH)
oxidase.";
Biochemistry 47:14028-14038(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kim J.W.;
"Identification of a human cell proliferation inducing gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryo;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=11360993; DOI=10.1006/abbi.2000.2180;
Sedlak D., Moore D.M., Moore D.J.;
"A drug-unresponsive and protease-resistant CNOX protein from human
sera.";
Arch. Biochem. Biophys. 386:106-116(2001).
[8]
FUNCTION, AND ENZYME REGULATION.
PubMed=12565167; DOI=10.1016/S0304-3835(02)00616-X;
Wang S., Morre D.M., Morre D.J.;
"Sera from cancer patients contain two oscillating ECTO-NOX activities
with different period lengths.";
Cancer Lett. 190:135-141(2003).
[9]
FUNCTION, AND COFACTOR.
PubMed=17027975; DOI=10.1016/j.jinorgbio.2006.08.007;
Jiang Z., Morre D.M., Morre D.J.;
"A role for copper in biological time-keeping.";
J. Inorg. Biochem. 100:2140-2149(2006).
-!- FUNCTION: 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 24 minutes and play a role in control of the
ultradian cellular biological clock. {ECO:0000269|PubMed:11360993,
ECO:0000269|PubMed:12565167, ECO:0000269|PubMed:17027975,
ECO:0000269|PubMed:19055324}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:17027975};
-!- ENZYME REGULATION: Not inhibited by the antitumor sulfonylurea
LY181984, the vabilloid capsaicin, and retinoids.
{ECO:0000269|PubMed:11360993, ECO:0000269|PubMed:12565167}.
-!- INTERACTION:
Q16206-2:ENOX2; NbExp=3; IntAct=EBI-713221, EBI-10179508;
Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-713221, EBI-739467;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-713221, EBI-739832;
O00560:SDCBP; NbExp=3; IntAct=EBI-713221, EBI-727004;
Q96BQ3:TRIM43; NbExp=5; IntAct=EBI-713221, EBI-2129899;
Q96E35:ZMYND19; NbExp=5; IntAct=EBI-713221, EBI-746595;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11360993}.
Secreted, extracellular space {ECO:0000269|PubMed:11360993}.
Note=Extracellular and plasma membrane-associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TC92-1; Sequence=Displayed;
Name=2;
IsoId=Q8TC92-2; Sequence=VSP_056985, VSP_056986, VSP_056987;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in lymphocyte cells, breast and
breast cancer (at protein level). Found in the sera of cancer
patients with a wide variety of cancers including breast,
prostate, lung and ovarian cancers, leukemias, and lymphomas.
Found also in the serum of healthy volunteers or patients with
disorders other than cancer. Probably shed into serum by cancer
cells.
-!- SIMILARITY: Belongs to the ENOX family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; EF432052; ABO28524.1; -; mRNA.
EMBL; AY513282; AAT08035.1; -; mRNA.
EMBL; AK000956; BAA91442.1; -; mRNA.
EMBL; AK299053; BAH12937.1; -; mRNA.
EMBL; AL136959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL161714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL162713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL445703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL607148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL627430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08693.1; -; Genomic_DNA.
EMBL; BC024178; AAH24178.1; -; mRNA.
CCDS; CCDS9389.1; -. [Q8TC92-1]
RefSeq; NP_001121087.1; NM_001127615.2. [Q8TC92-1]
RefSeq; NP_001229792.1; NM_001242863.2. [Q8TC92-1]
RefSeq; NP_001334893.1; NM_001347964.1. [Q8TC92-1]
RefSeq; NP_001334894.1; NM_001347965.1. [Q8TC92-1]
RefSeq; NP_001334895.1; NM_001347966.1. [Q8TC92-1]
RefSeq; NP_001334896.1; NM_001347967.1. [Q8TC92-1]
RefSeq; NP_001334897.1; NM_001347968.1. [Q8TC92-1]
RefSeq; NP_001334898.1; NM_001347969.1. [Q8TC92-1]
RefSeq; NP_060463.2; NM_017993.4. [Q8TC92-1]
RefSeq; XP_011533428.1; XM_011535126.2. [Q8TC92-1]
RefSeq; XP_011533429.1; XM_011535127.2. [Q8TC92-1]
RefSeq; XP_016876126.1; XM_017020637.1. [Q8TC92-1]
RefSeq; XP_016876127.1; XM_017020638.1. [Q8TC92-1]
UniGene; Hs.128258; -.
ProteinModelPortal; Q8TC92; -.
SMR; Q8TC92; -.
BioGrid; 120385; 16.
IntAct; Q8TC92; 13.
STRING; 9606.ENSP00000261488; -.
iPTMnet; Q8TC92; -.
PhosphoSitePlus; Q8TC92; -.
BioMuta; ENOX1; -.
DMDM; 74760449; -.
EPD; Q8TC92; -.
MaxQB; Q8TC92; -.
PaxDb; Q8TC92; -.
PeptideAtlas; Q8TC92; -.
PRIDE; Q8TC92; -.
ProteomicsDB; 74102; -.
Ensembl; ENST00000261488; ENSP00000261488; ENSG00000120658. [Q8TC92-1]
GeneID; 55068; -.
KEGG; hsa:55068; -.
UCSC; uc001uzc.5; human. [Q8TC92-1]
CTD; 55068; -.
DisGeNET; 55068; -.
EuPathDB; HostDB:ENSG00000120658.12; -.
GeneCards; ENOX1; -.
H-InvDB; HIX0011276; -.
HGNC; HGNC:25474; ENOX1.
HPA; HPA038355; -.
MIM; 610914; gene.
neXtProt; NX_Q8TC92; -.
OpenTargets; ENSG00000120658; -.
PharmGKB; PA162385069; -.
eggNOG; ENOG410IEVY; Eukaryota.
eggNOG; ENOG410XVWG; LUCA.
GeneTree; ENSGT00390000006788; -.
HOGENOM; HOG000049275; -.
HOVERGEN; HBG051083; -.
InParanoid; Q8TC92; -.
OMA; FCAFEGI; -.
OrthoDB; EOG091G038C; -.
PhylomeDB; Q8TC92; -.
TreeFam; TF323802; -.
ChiTaRS; ENOX1; human.
GenomeRNAi; 55068; -.
PRO; PR:Q8TC92; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000120658; -.
CleanEx; HS_ENOX1; -.
ExpressionAtlas; Q8TC92; baseline and differential.
Genevisible; Q8TC92; HS.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; Electron transport; Membrane; NAD;
Oxidoreductase; Polymorphism; Reference proteome; Secreted; Transport.
CHAIN 1 643 Ecto-NOX disulfide-thiol exchanger 1.
/FTId=PRO_0000295900.
DOMAIN 142 221 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COILED 307 342 {ECO:0000255}.
COILED 425 570 {ECO:0000255}.
COMPBIAS 89 139 Pro-rich.
VAR_SEQ 1 187 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056985.
VAR_SEQ 421 422 AL -> GA (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056986.
VAR_SEQ 423 643 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056987.
VARIANT 16 16 E -> D (in dbSNP:rs7338624).
{ECO:0000269|PubMed:19055324}.
/FTId=VAR_052205.
CONFLICT 62 62 L -> S (in Ref. 2; AAT08035).
{ECO:0000305}.
CONFLICT 279 279 F -> S (in Ref. 2; AAT08035 and 3;
BAA91442). {ECO:0000305}.
SEQUENCE 643 AA; 73348 MW; 501DC6905F326610 CRC64;
MVDAGGVENI TQLPQELPQM MAAAADGLGS IAIDTTQLNM SVTDPTAWAT AMNNLGMVPV
GLPGQQLVSD SICVPGFDPS LNMMTGITPI NPMIPGLGLV PPPPPTEVAV VKEIIHCKSC
TLFPQNPNLP PPSTRERPPG CKTVFVGGLP ENATEEIIQE VFEQCGDITA IRKSKKNFCH
IRFAEEFMVD KAIYLSGYRM RLGSSTDKKD SGRLHVDFAQ ARDDFYEWEC KQRMRAREER
HRRKLEEDRL RPPSPPAIMH YSEHEAALLA EKLKDDSKFS EAITVLLSWI ERGEVNRRSA
NQFYSMVQSA NSHVRRLMNE KATHEQEMEE AKENFKNALT GILTQFEQIV AVFNASTRQK
AWDHFSKAQR KNIDIWRKHS EELRNAQSEQ LMGIRREEEM EMSDDENCDS PTKKMRVDES
ALAAQAYALK EENDSLRWQL DAYRNEVELL KQEKEQLFRT EENLTKDQQL QFLQQTMQGM
QQQLLTIQEE LNNKKSELEQ AKEEQSHTQA LLKVLQEQLK GTKELVETNG HSHEDSNEIN
VLTVALVNQD RENNIEKRSQ GLKSEKEALL IGIISTFLHV HPFGANIEYL WSYMQQLDSK
ISANEIEMLL MRLPRMFKQE FTGVGATLEK RWKLCAFEGI KTT


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