NQO2_RAT
ID NQO2_RAT Reviewed; 231 AA.
AC Q6AY80;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PROTEIN SEQUENCE OF 184-201, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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. {ECO:0000250}.
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; BC079157; AAH79157.1; -; mRNA.
DR RefSeq; NP_001004214.1; NM_001004214.1.
DR RefSeq; XP_006253929.1; XM_006253867.3.
DR AlphaFoldDB; Q6AY80; -.
DR SMR; Q6AY80; -.
DR STRING; 10116.ENSRNOP00000024141; -.
DR PaxDb; Q6AY80; -.
DR PRIDE; Q6AY80; -.
DR GeneID; 291084; -.
DR KEGG; rno:291084; -.
DR UCSC; RGD:1303320; rat.
DR CTD; 4835; -.
DR RGD; 1303320; Nqo2.
DR VEuPathDB; HostDB:ENSRNOG00000017820; -.
DR eggNOG; ENOG502QRQH; Eukaryota.
DR HOGENOM; CLU_058643_2_0_1; -.
DR InParanoid; Q6AY80; -.
DR OMA; LFPIHHG; -.
DR OrthoDB; 1394543at2759; -.
DR PhylomeDB; Q6AY80; -.
DR TreeFam; TF300296; -.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR PRO; PR:Q6AY80; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017820; Expressed in heart and 19 other tissues.
DR Genevisible; Q6AY80; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031404; F:chloride ion binding; ISO:RGD.
DR GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; ISO:RGD.
DR GO; GO:0009055; F:electron transfer activity; ISO:RGD.
DR GO; GO:0071949; F:FAD binding; ISO:RGD.
DR GO; GO:1904408; F:melatonin binding; ISO:RGD.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:1905594; F:resveratrol binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:1901662; P:quinone catabolic process; ISO:RGD.
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; Direct protein sequencing; FAD; Flavoprotein; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="Ribosyldihydronicotinamide dehydrogenase [quinone]"
FT /id="PRO_0000071629"
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; 26275 MW; 9B15F21CD005850A CRC64;
MAGKKVLLVY AHQEPKSFNG SMKQVAVEEL SKQGCTVTVS DLYTMNFEPR ATRNDVTGAL
SNPEVFKYGI EAYEAYKKKA LTSDILEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV
LCQGFAFDVP GFYDSGFLKD KLALLSFTTG GTAEMYTKAG VNGDFRYFLW PLQHGTLHFC
GFKVLAPQIS FGPEVSSEEQ RKVMLASWVQ RLKSIWKEEP IHCTPSWYFQ G
