ENOX2_HUMAN
ID ENOX2_HUMAN Reviewed; 610 AA.
AC Q16206; A8K197; A8K1C2; Q5VTJ1; Q5VTJ2; Q8WUX0; Q9NTP6; Q9UH82;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ecto-NOX disulfide-thiol exchanger 2;
DE AltName: Full=APK1 antigen;
DE AltName: Full=Cytosolic ovarian carcinoma antigen 1;
DE AltName: Full=Tumor-associated hydroquinone oxidase;
DE Short=tNOX;
DE Includes:
DE RecName: Full=Hydroquinone [NADH] oxidase;
DE EC=1.-.-.-;
DE Includes:
DE RecName: Full=Protein disulfide-thiol oxidoreductase;
DE EC=1.-.-.-;
GN Name=ENOX2; Synonyms=COVA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ACTIVITY REGULATION, MUTAGENESIS OF
RP MET-396; CYS-505; CYS-510; HIS-546; CYS-558; HIS-562; CYS-569; CYS-575;
RP GLY-592 AND CYS-602, AND COFACTOR.
RX PubMed=11888291; DOI=10.1021/bi012041t;
RA Chueh P.-J., Kim C., Cho N., Morre D.M., Morre D.J.;
RT "Molecular cloning and characterization of a tumor-associated, growth-
RT related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa
RT cell surface.";
RL Biochemistry 41:3732-3741(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-405.
RA Rhodes S., Huckle E.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 86-90; 249-266 AND 318-333.
RC TISSUE=Cervix carcinoma;
RX PubMed=11437345; DOI=10.1006/abbi.2001.2404;
RA Yantiri F., Morre D.J.;
RT "Isolation and characterization of a tumor-associated NADH oxidase (tNOX)
RT from the HeLa cell surface.";
RL Arch. Biochem. Biophys. 391:149-159(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 275-610, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC TISSUE=Ovarian carcinoma;
RX PubMed=8150545; DOI=10.1002/ijc.2910570117;
RA Chang K., Pastan I.;
RT "Molecular cloning and expression of a cDNA encoding a protein detected by
RT the K1 antibody from an ovarian carcinoma (OVCAR-3) cell line.";
RL Int. J. Cancer 57:90-97(1994).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=9046026; DOI=10.1023/a:1006866726050;
RA Dai S., Morre D.J., Geilen C.C., Almond-Roesler B., Orfanos C.E.,
RA Morre D.M.;
RT "Inhibition of plasma membrane NADH oxidase activity and growth of HeLa
RT cells by natural and synthetic retinoids.";
RL Mol. Cell. Biochem. 166:101-109(1997).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=9932650; DOI=10.1023/a:1020594214379;
RA Morre D.J., Chueh P.-J., Lawler J., Morre D.M.;
RT "The sulfonylurea-inhibited NADH oxidase activity of HeLa cell plasma
RT membranes has properties of a protein disulfide-thiol oxidoreductase with
RT protein disulfide-thiol interchange activity.";
RL J. Bioenerg. Biomembr. 30:477-487(1998).
RN [11]
RP HYDROQUINONE OXIDASE ACTIVITY.
RX PubMed=10354495; DOI=10.1016/s0005-2728(99)00049-3;
RA Kishi T., Morre D.M., Morre D.J.;
RT "The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase
RT activity.";
RL Biochim. Biophys. Acta 1412:66-77(1999).
RN [12]
RP PRION-LIKE PROPERTIES.
RX PubMed=11412089; DOI=10.1021/bi010596i;
RA Kelker M., Kim C., Chueh P.-J., Guimont R., Morre D.M., Morre D.J.;
RT "Cancer isoform of a tumor-associated cell surface NADH oxidase (tNOX) has
RT properties of a prion.";
RL Biochemistry 40:7351-7354(2001).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=11488599; DOI=10.1006/abbi.2001.2436;
RA Morre D.J., Sedlak D., Tang X., Chueh P.-J., Geng T., Morre D.M.;
RT "Surface NADH oxidase of HeLa cells lacks intrinsic membrane binding
RT motifs.";
RL Arch. Biochem. Biophys. 392:251-256(2001).
RN [14]
RP DISEASE.
RX PubMed=11941450; DOI=10.1007/s00262-001-0262-2;
RA Cho N., Chueh P.-J., Kim C., Caldwell S., Morre D.M., Morre D.J.;
RT "Monoclonal antibody to a cancer-specific and drug-responsive hydroquinone
RT (NADH) oxidase from the sera of cancer patients.";
RL Cancer Immunol. Immunother. 51:121-129(2002).
RN [15]
RP FUNCTION IN BIOLOGICAL CLOCK CONTROL.
RX PubMed=12356293; DOI=10.1021/bi020392h;
RA Morre D.J., Chueh P.-J., Pletcher J., Tang X., Wu L.Y., Morre D.M.;
RT "Biochemical basis for the biological clock.";
RL Biochemistry 41:11941-11945(2002).
RN [16]
RP VARIANT ILE-202.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: May be involved in cell growth. Probably acts as a terminal
CC oxidase of plasma electron transport from cytosolic NAD(P)H via
CC hydroquinones to acceptors at the cell surface. Hydroquinone oxidase
CC activity alternates with a protein disulfide-thiol
CC interchange/oxidoreductase activity which may control physical membrane
CC displacements associated with vesicle budding or cell enlargement. The
CC activities oscillate with a period length of 22 minutes and play a role
CC in control of the ultradian cellular biological clock.
CC {ECO:0000269|PubMed:12356293, ECO:0000269|PubMed:9932650}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:11888291};
CC -!- ACTIVITY REGULATION: Inhibited by the antitumor sulfonylurea LY181984,
CC the vabilloid capsaicin, and retinoids. {ECO:0000269|PubMed:11888291,
CC ECO:0000269|PubMed:9046026, ECO:0000269|PubMed:9932650}.
CC -!- INTERACTION:
CC Q16206-2; Q96Q77: CIB3; NbExp=3; IntAct=EBI-10179508, EBI-10292696;
CC Q16206-2; Q8TC92: ENOX1; NbExp=3; IntAct=EBI-10179508, EBI-713221;
CC Q16206-2; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-10179508, EBI-10178634;
CC Q16206-2; Q6P2C6: MLLT6; NbExp=3; IntAct=EBI-10179508, EBI-5773143;
CC Q16206-2; P09012: SNRPA; NbExp=3; IntAct=EBI-10179508, EBI-607085;
CC Q16206-2; O00463: TRAF5; NbExp=3; IntAct=EBI-10179508, EBI-523498;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Secreted, extracellular space.
CC Note=Extracellular and plasma membrane-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16206-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16206-2; Sequence=VSP_015719;
CC -!- TISSUE SPECIFICITY: Found in the sera of cancer patients with a wide
CC variety of cancers including breast, prostate, lung and ovarian
CC cancers, leukemias, and lymphomas. Not found in the serum of healthy
CC volunteers or patients with disorders other than cancer. Probably shed
CC into serum by cancer cells. Found on the cell borders of renal, kidney
CC and ovarian carcinomas but not on the borders of surrounding non-
CC cancerous stromal cells.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8150545}.
CC -!- MISCELLANEOUS: Has several properties associated with prions including
CC resistance to proteases, resistance to cyanogen bromide digestion, and
CC the ability to form amyloid filaments resembling those of spongiform
CC encephalopathies.
CC -!- SIMILARITY: Belongs to the ENOX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB30428.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF207881; AAF20934.2; -; mRNA.
DR EMBL; AK000353; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK289837; BAF82526.1; -; mRNA.
DR EMBL; AK289812; BAF82501.1; -; mRNA.
DR EMBL; AL049733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471107; EAX11796.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11797.1; -; Genomic_DNA.
DR EMBL; BC019254; AAH19254.2; -; mRNA.
DR EMBL; BC140874; AAI40875.1; -; mRNA.
DR EMBL; AL133207; CAB61581.2; -; mRNA.
DR EMBL; S72904; AAB30428.1; ALT_FRAME; mRNA.
DR CCDS; CCDS14626.1; -. [Q16206-1]
DR CCDS; CCDS14627.1; -. [Q16206-2]
DR PIR; I54780; I54780.
DR RefSeq; NP_001268665.1; NM_001281736.1. [Q16206-2]
DR RefSeq; NP_006366.2; NM_006375.3. [Q16206-2]
DR RefSeq; NP_872114.1; NM_182314.2. [Q16206-1]
DR RefSeq; XP_005262411.1; XM_005262354.3.
DR RefSeq; XP_011529549.1; XM_011531247.2. [Q16206-1]
DR RefSeq; XP_011529551.1; XM_011531249.2. [Q16206-1]
DR RefSeq; XP_011529553.1; XM_011531251.2. [Q16206-2]
DR RefSeq; XP_016884715.1; XM_017029226.1.
DR RefSeq; XP_016884716.1; XM_017029227.1. [Q16206-1]
DR RefSeq; XP_016884717.1; XM_017029228.1. [Q16206-1]
DR AlphaFoldDB; Q16206; -.
DR BioGRID; 115758; 32.
DR IntAct; Q16206; 13.
DR MINT; Q16206; -.
DR STRING; 9606.ENSP00000337146; -.
DR ChEMBL; CHEMBL3714292; -.
DR DrugBank; DB04915; Idronoxil.
DR GlyGen; Q16206; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16206; -.
DR PhosphoSitePlus; Q16206; -.
DR BioMuta; ENOX2; -.
DR DMDM; 34978371; -.
DR EPD; Q16206; -.
DR jPOST; Q16206; -.
DR MassIVE; Q16206; -.
DR MaxQB; Q16206; -.
DR PaxDb; Q16206; -.
DR PeptideAtlas; Q16206; -.
DR PRIDE; Q16206; -.
DR ProteomicsDB; 60838; -. [Q16206-1]
DR ProteomicsDB; 60839; -. [Q16206-2]
DR Antibodypedia; 354; 195 antibodies from 29 providers.
DR DNASU; 10495; -.
DR Ensembl; ENST00000338144.8; ENSP00000337146.3; ENSG00000165675.19. [Q16206-1]
DR Ensembl; ENST00000370927.5; ENSP00000359965.1; ENSG00000165675.19. [Q16206-1]
DR Ensembl; ENST00000370935.5; ENSP00000359973.1; ENSG00000165675.19. [Q16206-2]
DR Ensembl; ENST00000394363.6; ENSP00000377890.1; ENSG00000165675.19. [Q16206-2]
DR GeneID; 10495; -.
DR KEGG; hsa:10495; -.
DR MANE-Select; ENST00000394363.6; ENSP00000377890.1; NM_006375.4; NP_006366.2. [Q16206-2]
DR UCSC; uc004evw.5; human. [Q16206-1]
DR CTD; 10495; -.
DR DisGeNET; 10495; -.
DR GeneCards; ENOX2; -.
DR HGNC; HGNC:2259; ENOX2.
DR HPA; ENSG00000165675; Low tissue specificity.
DR MIM; 300282; gene.
DR neXtProt; NX_Q16206; -.
DR OpenTargets; ENSG00000165675; -.
DR PharmGKB; PA162385106; -.
DR VEuPathDB; HostDB:ENSG00000165675; -.
DR eggNOG; ENOG502QQ8G; Eukaryota.
DR GeneTree; ENSGT00390000006788; -.
DR HOGENOM; CLU_019282_1_1_1; -.
DR InParanoid; Q16206; -.
DR OMA; FNVYRNH; -.
DR OrthoDB; 357901at2759; -.
DR PhylomeDB; Q16206; -.
DR TreeFam; TF323802; -.
DR PathwayCommons; Q16206; -.
DR SignaLink; Q16206; -.
DR SIGNOR; Q16206; -.
DR BioGRID-ORCS; 10495; 12 hits in 705 CRISPR screens.
DR ChiTaRS; ENOX2; human.
DR GeneWiki; ENOX2; -.
DR GenomeRNAi; 10495; -.
DR Pharos; Q16206; Tbio.
DR PRO; PR:Q16206; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q16206; protein.
DR Bgee; ENSG00000165675; Expressed in calcaneal tendon and 195 other tissues.
DR ExpressionAtlas; Q16206; baseline and differential.
DR Genevisible; Q16206; HS.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0007624; P:ultradian rhythm; IDA:UniProtKB.
DR CDD; cd12228; RRM_ENOX; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR038876; ENOX.
DR InterPro; IPR034140; ENOX_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR16001; PTHR16001; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cell membrane; Coiled coil;
KW Copper; Direct protein sequencing; Electron transport; Glycoprotein;
KW Growth regulation; Membrane; NAD; Oxidoreductase; Reference proteome;
KW Secreted; Transport.
FT CHAIN 1..610
FT /note="Ecto-NOX disulfide-thiol exchanger 2"
FT /id="PRO_0000079275"
FT DOMAIN 128..207
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT COILED 293..328
FT /evidence="ECO:0000255"
FT COILED 381..505
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015719"
FT VARIANT 202
FT /note="V -> I (in dbSNP:rs754363472)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069427"
FT MUTAGEN 396
FT /note="M->A: No effect on activity but response to
FT capsaicin is lost."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 505
FT /note="C->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 510
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 546
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 558
FT /note="C->A: Period length of activity extended to 42
FT minutes."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 562
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 569
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 575
FT /note="C->A: Period length of activity extended to 36
FT minutes."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 592
FT /note="G->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11888291"
FT MUTAGEN 602
FT /note="C->A: Period length of activity extended to 36
FT minutes."
FT /evidence="ECO:0000269|PubMed:11888291"
FT CONFLICT 123
FT /note="R -> G (in Ref. 2; AK000353)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="E -> G (in Ref. 2; AK000353)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="S -> V (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="I -> V (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="F -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..407
FT /note="Missing (in Ref. 5; AAH19254)"
FT /evidence="ECO:0000305"
SQ 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
