NQO2_MOUSE
ID NQO2_MOUSE Reviewed; 231 AA.
AC Q9JI75;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone];
DE EC=1.10.5.1;
DE AltName: Full=NRH dehydrogenase [quinone] 2;
DE AltName: Full=NRH:quinone oxidoreductase 2;
DE AltName: Full=Quinone reductase 2;
DE Short=QR2;
GN Name=Nqo2; Synonyms=Nmor2;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Kidney;
RX PubMed=10903442; DOI=10.1016/s0378-1119(00)00221-3;
RA Long D.J. II, Jaiswal A.K.;
RT "Mouse NRH:quinone oxidoreductase (NQO2): cloning of cDNA and gene- and
RT tissue-specific expression.";
RL Gene 252:107-117(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The enzyme apparently serves as a quinone reductase in
CC connection with conjugation reactions of hydroquinones involved in
CC detoxification pathways as well as in biosynthetic processes such as
CC the vitamin K-dependent gamma-carboxylation of glutamate residues in
CC prothrombin synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone +
CC H(+) = a quinol + beta-nicotinamide D-riboside; Xref=Rhea:RHEA:12364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:55458, ChEBI:CHEBI:132124; EC=1.10.5.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than
CC NAD(P)H as an electron donor.
CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC {ECO:0000305}.
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DR EMBL; AF252260; AAF97785.1; -; mRNA.
DR EMBL; AF254081; AAF97789.1; -; Genomic_DNA.
DR EMBL; AF254076; AAF97789.1; JOINED; Genomic_DNA.
DR EMBL; AF254077; AAF97789.1; JOINED; Genomic_DNA.
DR EMBL; AF254078; AAF97789.1; JOINED; Genomic_DNA.
DR EMBL; AF254079; AAF97789.1; JOINED; Genomic_DNA.
DR EMBL; AF254080; AAF97789.1; JOINED; Genomic_DNA.
DR EMBL; AK010842; BAB27217.1; -; mRNA.
DR EMBL; BC027629; AAH27629.1; -; mRNA.
DR CCDS; CCDS26442.1; -.
DR RefSeq; NP_001156713.1; NM_001163241.1.
DR RefSeq; NP_001156714.1; NM_001163242.1.
DR RefSeq; NP_064678.1; NM_020282.3.
DR RefSeq; XP_006516637.1; XM_006516574.3.
DR AlphaFoldDB; Q9JI75; -.
DR SMR; Q9JI75; -.
DR BioGRID; 201791; 4.
DR STRING; 10090.ENSMUSP00000021843; -.
DR iPTMnet; Q9JI75; -.
DR PhosphoSitePlus; Q9JI75; -.
DR EPD; Q9JI75; -.
DR jPOST; Q9JI75; -.
DR MaxQB; Q9JI75; -.
DR PaxDb; Q9JI75; -.
DR PRIDE; Q9JI75; -.
DR ProteomicsDB; 293887; -.
DR Antibodypedia; 9328; 555 antibodies from 34 providers.
DR DNASU; 18105; -.
DR Ensembl; ENSMUST00000021843; ENSMUSP00000021843; ENSMUSG00000046949.
DR Ensembl; ENSMUST00000058978; ENSMUSP00000053809; ENSMUSG00000046949.
DR Ensembl; ENSMUST00000222740; ENSMUSP00000152294; ENSMUSG00000046949.
DR GeneID; 18105; -.
DR KEGG; mmu:18105; -.
DR UCSC; uc007qas.2; mouse.
DR CTD; 4835; -.
DR MGI; MGI:104513; Nqo2.
DR VEuPathDB; HostDB:ENSMUSG00000046949; -.
DR eggNOG; ENOG502QRQH; Eukaryota.
DR GeneTree; ENSGT00940000156563; -.
DR HOGENOM; CLU_058643_2_0_1; -.
DR InParanoid; Q9JI75; -.
DR OMA; LFPIHHG; -.
DR OrthoDB; 1394543at2759; -.
DR PhylomeDB; Q9JI75; -.
DR TreeFam; TF300296; -.
DR BRENDA; 1.10.5.1; 3474.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 18105; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Nqo2; mouse.
DR PRO; PR:Q9JI75; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JI75; protein.
DR Bgee; ENSMUSG00000046949; Expressed in lumbar dorsal root ganglion and 224 other tissues.
DR ExpressionAtlas; Q9JI75; baseline and differential.
DR Genevisible; Q9JI75; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; ISO:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISO:MGI.
DR GO; GO:0071949; F:FAD binding; ISO:MGI.
DR GO; GO:1904408; F:melatonin binding; ISO:MGI.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:1905594; F:resveratrol binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1901662; P:quinone catabolic process; ISO:MGI.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR003680; Flavodoxin_fold.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="Ribosyldihydronicotinamide dehydrogenase [quinone]"
FT /id="PRO_0000071627"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 18..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 104..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16083"
SQ SEQUENCE 231 AA; 26248 MW; D5D9AB805C4AD9F5 CRC64;
MAGKKVLIVY AHQEPKSFNG SLKKVAVEEL SKQGCTVTVS DLYSMNFEPR ATRNDITGAP
SNPDVFSYGI ETHEAYKKKA LTSDIFEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV
LCRGFAFDIP GFYDSGFLKG KLALLSLTTG GTAEMYTKDG VSGDFRYFLW PLQHGTLHFC
GFKVLAPQIS FGLDVSSEEE RKVMLASWAQ RLKSIWKEEP IHCTPPWYFQ E
