ENOX2_MOUSE
ID ENOX2_MOUSE Reviewed; 598 AA.
AC Q8R0Z2; B1B073; Q8BY59; Q8R372;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH25915.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 328-598 (ISOFORM 3).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH25915.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH25915.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH26450.1};
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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q16206}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q16206};
CC -!- ACTIVITY REGULATION: Inhibited by the antitumor sulfonylurea LY181984,
CC the vabilloid capsaicin, and retinoids. {ECO:0000250|UniProtKB:Q16206}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted,
CC extracellular space {ECO:0000250}. Note=Extracellular and plasma
CC membrane-associated. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000305};
CC IsoId=Q8R0Z2-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8R0Z2-2; Sequence=VSP_051830;
CC Name=3 {ECO:0000305};
CC IsoId=Q8R0Z2-3; Sequence=VSP_051831;
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q16206}.
CC -!- SIMILARITY: Belongs to the ENOX family. {ECO:0000305}.
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DR EMBL; AK034058; BAC28565.1; -; mRNA.
DR EMBL; AK041822; BAC31077.1; -; mRNA.
DR EMBL; BX294194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025915; AAH25915.1; -; mRNA.
DR EMBL; BC026450; AAH26450.1; -; mRNA.
DR CCDS; CCDS30115.1; -. [Q8R0Z2-1]
DR CCDS; CCDS72377.1; -. [Q8R0Z2-3]
DR CCDS; CCDS72378.1; -. [Q8R0Z2-2]
DR RefSeq; NP_001258376.1; NM_001271447.1. [Q8R0Z2-1]
DR RefSeq; NP_001258377.1; NM_001271448.1. [Q8R0Z2-1]
DR RefSeq; NP_001258378.1; NM_001271449.1. [Q8R0Z2-1]
DR RefSeq; NP_001258379.1; NM_001271450.1. [Q8R0Z2-2]
DR RefSeq; NP_666063.1; NM_145951.5. [Q8R0Z2-1]
DR RefSeq; XP_011249302.1; XM_011251000.2. [Q8R0Z2-1]
DR AlphaFoldDB; Q8R0Z2; -.
DR STRING; 10090.ENSMUSP00000110568; -.
DR iPTMnet; Q8R0Z2; -.
DR PhosphoSitePlus; Q8R0Z2; -.
DR EPD; Q8R0Z2; -.
DR MaxQB; Q8R0Z2; -.
DR PaxDb; Q8R0Z2; -.
DR PRIDE; Q8R0Z2; -.
DR ProteomicsDB; 275865; -. [Q8R0Z2-1]
DR ProteomicsDB; 275866; -. [Q8R0Z2-2]
DR ProteomicsDB; 275867; -. [Q8R0Z2-3]
DR Antibodypedia; 354; 195 antibodies from 29 providers.
DR DNASU; 209224; -.
DR Ensembl; ENSMUST00000033437; ENSMUSP00000033437; ENSMUSG00000031109. [Q8R0Z2-1]
DR Ensembl; ENSMUST00000114911; ENSMUSP00000110561; ENSMUSG00000031109. [Q8R0Z2-2]
DR Ensembl; ENSMUST00000114912; ENSMUSP00000110562; ENSMUSG00000031109. [Q8R0Z2-3]
DR Ensembl; ENSMUST00000114914; ENSMUSP00000110564; ENSMUSG00000031109. [Q8R0Z2-1]
DR Ensembl; ENSMUST00000114918; ENSMUSP00000110568; ENSMUSG00000031109. [Q8R0Z2-1]
DR Ensembl; ENSMUST00000167659; ENSMUSP00000128885; ENSMUSG00000031109. [Q8R0Z2-1]
DR GeneID; 209224; -.
DR KEGG; mmu:209224; -.
DR UCSC; uc009tcv.2; mouse. [Q8R0Z2-1]
DR UCSC; uc009tcz.2; mouse. [Q8R0Z2-3]
DR UCSC; uc012hgt.2; mouse. [Q8R0Z2-2]
DR CTD; 10495; -.
DR MGI; MGI:2384799; Enox2.
DR VEuPathDB; HostDB:ENSMUSG00000031109; -.
DR eggNOG; ENOG502QQ8G; Eukaryota.
DR GeneTree; ENSGT00390000006788; -.
DR HOGENOM; CLU_019282_1_1_1; -.
DR InParanoid; Q8R0Z2; -.
DR OMA; FNVYRNH; -.
DR OrthoDB; 357901at2759; -.
DR PhylomeDB; Q8R0Z2; -.
DR TreeFam; TF323802; -.
DR BioGRID-ORCS; 209224; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Enox2; mouse.
DR PRO; PR:Q8R0Z2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8R0Z2; protein.
DR Bgee; ENSMUSG00000031109; Expressed in habenula and 250 other tissues.
DR Genevisible; Q8R0Z2; MM.
DR GO; GO:0009897; C:external side of plasma membrane; ISS: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; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0007624; P:ultradian rhythm; ISS: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 2: Evidence at transcript level;
KW Alternative splicing; Biological rhythms; Cell membrane; Coiled coil;
KW Copper; Electron transport; Glycoprotein; Growth regulation; Membrane; NAD;
KW Oxidoreductase; Reference proteome; Secreted; Transport.
FT CHAIN 1..598
FT /note="Ecto-NOX disulfide-thiol exchanger 2"
FT /id="PRO_0000079276"
FT DOMAIN 99..178
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT COILED 264..299
FT /evidence="ECO:0000255"
FT COILED 352..476
FT /evidence="ECO:0000255"
FT VAR_SEQ 463..473
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051830"
FT VAR_SEQ 540..555
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051831"
SQ SEQUENCE 598 AA; 68285 MW; C115D1130E4D6094 CRC64;
MTLPVSDPAA WATAMNNLGM APLGIAGQPI LPDFDPALGM MTGIPPITPM MPGLGIVPPP
IPPDMPVAKE IIHCKSCTLF PPNPNLPPPA TRERPPGCKT VFVGGLPENG TEQIIVEVFE
QCGEIIAIRK SKKNFCHIRF AEEYMVDKAL YLSGYRIRLG SSTDKKDTGR LHVDFAQARD
DLYEWECKQR MLAREERHRR RMEEERMRPP SPPPVVHYSD HECSIVAEKL KDDSKFSEAV
QTLLTWIERG EVNRRSANHF YSMIQSANSH VRRLVNEKAT HEKEMEEAKE KFKQALSGIL
IQFEQIVAVY HSASKQKAWD HFTKAQRKNI SVWCKQAEEI RNIHNDELMG IRREEEMEMS
DDEIEETTET KETEESALVS QAEALKEEND SLRWQLDAYR NEVELLKQEQ GKAHREDDPN
KEQQLKLLQQ ALQGMQQHLL KVQEEYKKKE AELDRIKDDN LQVEQLLENF HEKQENCGSR
LCASSQEGEQ PLEKTAVSNP VKSEREALLV GIISTFLHVH PFGASIEYIC SYLNRLDNKA
SYQIPSKLTT SPLLPISTSD VESLMSRLQH TFRQEMTGVG ASLEKRWKFC GFEGLKLT
