ENOX1_MOUSE
ID ENOX1_MOUSE Reviewed; 643 AA.
AC Q8BHR2; Q80WS5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ecto-NOX disulfide-thiol exchanger 1;
DE AltName: Full=Constitutive Ecto-NOX;
DE Short=cNOX;
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=Enox1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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: Probably acts as a terminal oxidase of plasma electron
CC transport from cytosolic NAD(P)H via hydroquinones to acceptors at the
CC cell surface. Hydroquinone oxidase activity alternates with a protein
CC disulfide-thiol interchange/oxidoreductase activity which may control
CC physical membrane displacements associated with vesicle budding or cell
CC enlargement. The activities oscillate with a period length of 24
CC minutes and play a role in control of the ultradian cellular biological
CC clock (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Not inhibited by the antitumor sulfonylurea
CC LY181984, the vabilloid capsaicin, and retinoids. {ECO:0000250}.
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=2;
CC Name=1;
CC IsoId=Q8BHR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHR2-2; Sequence=VSP_027122;
CC -!- SIMILARITY: Belongs to the ENOX family. {ECO:0000305}.
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DR EMBL; AK051821; BAC34782.1; -; mRNA.
DR EMBL; BC052062; AAH52062.1; -; mRNA.
DR CCDS; CCDS27290.1; -. [Q8BHR2-1]
DR CCDS; CCDS88717.1; -. [Q8BHR2-2]
DR RefSeq; NP_001240688.1; NM_001253759.1. [Q8BHR2-2]
DR RefSeq; NP_766401.1; NM_172813.3. [Q8BHR2-1]
DR RefSeq; XP_006519062.1; XM_006518999.3. [Q8BHR2-2]
DR RefSeq; XP_006519063.1; XM_006519000.3. [Q8BHR2-2]
DR RefSeq; XP_006519064.1; XM_006519001.3. [Q8BHR2-2]
DR RefSeq; XP_011243365.1; XM_011245063.2. [Q8BHR2-2]
DR RefSeq; XP_011243366.1; XM_011245064.2. [Q8BHR2-2]
DR RefSeq; XP_011243367.1; XM_011245065.2. [Q8BHR2-2]
DR RefSeq; XP_011243368.1; XM_011245066.2. [Q8BHR2-1]
DR RefSeq; XP_017171507.1; XM_017316018.1. [Q8BHR2-1]
DR AlphaFoldDB; Q8BHR2; -.
DR SMR; Q8BHR2; -.
DR STRING; 10090.ENSMUSP00000022589; -.
DR iPTMnet; Q8BHR2; -.
DR PhosphoSitePlus; Q8BHR2; -.
DR PaxDb; Q8BHR2; -.
DR PeptideAtlas; Q8BHR2; -.
DR PRIDE; Q8BHR2; -.
DR ProteomicsDB; 275455; -. [Q8BHR2-1]
DR ProteomicsDB; 275456; -. [Q8BHR2-2]
DR Antibodypedia; 23523; 94 antibodies from 22 providers.
DR Ensembl; ENSMUST00000022589; ENSMUSP00000022589; ENSMUSG00000022012. [Q8BHR2-1]
DR Ensembl; ENSMUST00000227662; ENSMUSP00000154512; ENSMUSG00000022012. [Q8BHR2-2]
DR GeneID; 239188; -.
DR KEGG; mmu:239188; -.
DR UCSC; uc007urv.2; mouse. [Q8BHR2-1]
DR UCSC; uc007urz.2; mouse. [Q8BHR2-2]
DR CTD; 55068; -.
DR MGI; MGI:2444896; Enox1.
DR VEuPathDB; HostDB:ENSMUSG00000022012; -.
DR eggNOG; ENOG502QQ8G; Eukaryota.
DR GeneTree; ENSGT00390000006788; -.
DR HOGENOM; CLU_019282_1_1_1; -.
DR InParanoid; Q8BHR2; -.
DR OMA; MSDDETC; -.
DR OrthoDB; 357901at2759; -.
DR PhylomeDB; Q8BHR2; -.
DR TreeFam; TF323802; -.
DR BioGRID-ORCS; 239188; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Enox1; mouse.
DR PRO; PR:Q8BHR2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BHR2; protein.
DR Bgee; ENSMUSG00000022012; Expressed in animal zygote and 176 other tissues.
DR ExpressionAtlas; Q8BHR2; baseline and differential.
DR Genevisible; Q8BHR2; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISO:MGI.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISO:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0007624; P:ultradian rhythm; IEA:InterPro.
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; Membrane; NAD; Oxidoreductase;
KW Reference proteome; Secreted; Transport.
FT CHAIN 1..643
FT /note="Ecto-NOX disulfide-thiol exchanger 1"
FT /id="PRO_0000295901"
FT DOMAIN 142..221
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT COILED 307..342
FT /evidence="ECO:0000255"
FT COILED 425..521
FT /evidence="ECO:0000255"
FT VAR_SEQ 420
FT /note="S -> SEADIEDCAGDPADRGLHSA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027122"
SQ SEQUENCE 643 AA; 73281 MW; 42D58E3EC6B2FF53 CRC64;
MVDAAGFESV AQCPRELHQM MAAAADGLGS IALDTTQLNM SVTDPTAWAT AMNNLGMVPV
GLPGQQLVSD SICVPGFDPG LNMMTGITPI NPMIPGLGLV PPPPPTEVAV VKEIIHCKSC
TLFPQNPNLP PPSTRERPPG CKTVFVGGLP ENATEEIIQE VFEQCGDITA IRKSKKNFCH
IRFAEEFMVD KAIYLSGYRM RLGSSTDKKD SGRLHVDFAQ ARDDFYEWEC KQRMRAREER
HRRKLEEDRL RPPSPPAIMH YSEHEAALLA DKLKDDSKFS EAITVLLSWI ERGEVNRRSA
NQFYSMVQSA NSHVRRLMNE KATHEQEMEE AKENFKNALT GILTQFEQIV AVFNASTRQK
AWDHFSKAQR KNIDIWRKHS EELRNAQSEQ LMGIRREEEM EMSDDENCDS PTKKMRVDES
ALAAQAYALK EENDSLRWQL DAYRNEVELL KQEKEQLFRT EENLTKDQQL QFLQQTMQGM
QQQLLAIQEE LNNKKSELEQ AKEEQSHTQA LLKVLQEQLK GTKDLVETNG HSHEDANEIN
VLTVALVNQD RENNTEKRSQ GLKSEKEALL IGIISTFLHV HPFGANIEYL WSYMQQLDSK
ISANEIEMLL MRLPRMFKQE FTGVGATLEK RWKLCAFEGI KTT
