[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=3536915 [NCBI, ExPASy, EBI, Israel, Japan] Robertson J.A., Chen H.-C., Nebert D.W.; "NAD(P)H:menadione oxidoreductase. Novel purification of enzyme cDNA and complete amino acid sequence, and gene regulation."; J. Biol. Chem. 261:15794-15799(1986).
[2]	NUCLEOTIDE SEQUENCE. Robertson J.A., Nebert D.W., Hankinson O.; "Autoregulation plus positive and negative elements controlling transcription of genes in the [Ah] battery."; Chem. Scr. 27:83-87(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Liver; PubMed=3100515 [NCBI, ExPASy, EBI, Israel, Japan] Bayney R.M., Rodkey J.A., Bennett C.D., Lu A.Y.H., Pickett C.B.; "Rat liver NAD(P)H: quinone reductase nucleotide sequence analysis of a quinone reductase cDNA clone and prediction of the amino acid sequence of the corresponding protein."; J. Biol. Chem. 262:572-575(1987).
[4]	NUCLEOTIDE SEQUENCE. TISSUE=Liver; PubMed=2480957 [NCBI, ExPASy, EBI, Israel, Japan] Bayney R.M., Morton M.R., Favreau L.V., Pickett C.B.; "Rat liver NAD(P)H:quinone reductase. Regulation of quinone reductase gene expression by planar aromatic compounds and determination of the exon structure of the quinone reductase structural gene."; J. Biol. Chem. 264:21793-21797(1989).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Heart; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	PROTEIN SEQUENCE OF 2-274. DOI=10.1021/bi00418a033; PubMed=3143406 [NCBI, ExPASy, EBI, Israel, Japan] Haniu M., Yuan H., Chen S.A., Iyanagi T., Lee T.D., Shively J.E.; "Structure-function relationship of NAD(P)H:quinone reductase: characterization of NH2-terminal blocking group and essential tyrosine and lysine residues."; Biochemistry 27:6877-6883(1988).
[7]	NUCLEOTIDE SEQUENCE OF 1-57. DOI=10.1016/0003-9861(88)90516-4; PubMed=2963593 [NCBI, ExPASy, EBI, Israel, Japan] Bayney R.M., Pickett C.B.; "Rat liver NAD(P)H:quinone reductase: isolation of a quinone reductase structural gene and prediction of the NH2 terminal sequence of the protein by double-stranded sequencing of exons 1 and 2."; Arch. Biochem. Biophys. 260:847-850(1988).
[8]	PROTEIN SEQUENCE OF 2-21. DOI=10.1016/0003-9861(90)90648-I; PubMed=1703398 [NCBI, ExPASy, EBI, Israel, Japan] Ma Q., Wang R., Yang C.S., Lu A.Y.H.; "Expression of mammalian DT-diaphorase in Escherichia coli: purification and characterization of the expressed protein."; Arch. Biochem. Biophys. 283:311-317(1990).
[9]	PROTEIN SEQUENCE OF 24-131 AND 156-270. DOI=10.1016/0006-2952(88)90336-X; PubMed=3144286 [NCBI, ExPASy, EBI, Israel, Japan] Knox R.J., Boland M.P., Friedlos F., Coles B., Southan C., Roberts J.J.; "The nitroreductase enzyme in Walker cells that activates 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) to 5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide is a form of NAD(P)H dehydrogenase (quinone) (EC 1.6.99.2)."; Biochem. Pharmacol. 37:4671-4677(1988).
[10]	NUCLEOTIDE SEQUENCE OF 80-274. PubMed=2504488 [NCBI, ExPASy, EBI, Israel, Japan] Dear T.N., McDonald D.A., Kefford R.F.; "Transcriptional down-regulation of a rat gene, WDNM2, in metastatic DMBA-8 cells."; Cancer Res. 49:5323-5328(1989).
[11]	PROTEIN SEQUENCE OF 147-156 AND 263-271. PubMed=2499768 [NCBI, ExPASy, EBI, Israel, Japan] Liu X.F., Yuan H., Haniu M., Iyanagi T., Shively J.E., Chen S.A.; "Reaction of rat liver DT-diaphorase (NAD(P)H:quinone acceptor reductase) with 5'-[p-(fluorosulfonyl)benzoyl]-adenosine."; Mol. Pharmacol. 35:818-822(1989).
[12]	MUTAGENESIS. DOI=10.1016/0006-291X(90)92006-L; PubMed=2141979 [NCBI, ExPASy, EBI, Israel, Japan] Forrest G.L., Qian J., Ma J.-X., Kaplan W.D., Akman S., Doroshow J., Chen S.A.; "Rat liver NAD(P)H:quinone oxidoreductase: cDNA expression and site-directed mutagenesis."; Biochem. Biophys. Res. Commun. 169:1087-1093(1990).
[13]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). TISSUE=Liver; PubMed=7568029 [NCBI, ExPASy, EBI, Israel, Japan] Li R., Bianchet M.A., Talalay P., Amzel L.M.; "The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction."; Proc. Natl. Acad. Sci. U.S.A. 92:8846-8850(1995).
[14]	ERRATUM. Li R., Bianchet M.A., Talalay P., Amzel L.M.; Proc. Natl. Acad. Sci. U.S.A. 92:10815-10815(1995).

Comments

FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
CATALYTIC ACTIVITY: NAD(P)H + a quinone = NAD(P)⁺ + a hydroquinone.
COFACTOR: FAD.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: By polycyclic hydrocarbons (Governed by the aromatic hydrocarbon-responsive (AH) locus).
MISCELLANEOUS: Quinone reductase accepts electrons from both NADH and NADPH with equal efficiency.
MISCELLANEOUS: This protein is inhibited by dicoumarol.
SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CAUTION: Ref.4 sequence seems incorrectly to be attributed to a mouse sequence while it really seems to correspond to the rat sequence.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02608; AAA41716.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02679; AAA41715.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36660; AAA39829.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02640; AAA41988.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31805; AAA41989.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31801; AAA41989.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31802; AAA41989.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31804; AAA41989.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33039; AAA41990.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33038; AAA41990.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC083542; AAH83542.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17464; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

A34162; A34162.

NP_058696.2; -.

3D structure databases

PDB

1QRD; X-ray; 2.40 A; A/B=1-274.

[ExPASy / RCSB / EBI]

PDBsum

1QRD; -.

ModBase

P05982.

Organism-specific databases

RGD

2503; Nqo1.

Gene expression databases

ArrayExpress

P05982; -.

GermOnline

ENSRNOG00000012772; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0003955;	Molecular function: NAD(P)H dehydrogenase (quinone) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003680; Flavodoxin_fold.
Graphical view of domain structure.

Pfam

PF02525; Flavodoxin_2; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSRNOG00000012772; Rattus norvegicus. [Contig view]

GeneID

24314; -.

KEGG

rno:24314; -.

NMPDR

fig|10116.3.peg.14965; -.

Phylogenomic databases

HOVERGEN

P05982; -.

Other

LinkHub

P05982; -.

NextBio

602959; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 274`	`273`	`NAD(P)H dehydrogenase [quinone] 1.`	`PRO_0000071625`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MUTAGEN`	`117 118`		`FE->KK: Destroys enzyme activity.`
`MUTAGEN`	`161 161`		`V->D: Destroys enzyme activity.`
`MUTAGEN`	`164 164`		`D->Q: Destroys enzyme activity.`
`CONFLICT`	`31 31`		`Missing (in Ref. 9; AA sequence).`
`CONFLICT`	`80 80`		`R -> G (in Ref. 10; X17464).`
`CONFLICT`	`135 135`		`K -> Q (in Ref. 3; AAA41988).`
`CONFLICT`	`216 216`		`W -> E (in Ref. 9; AA sequence).`
`CONFLICT`	`227 227`		`S -> E (in Ref. 9; AA sequence).`
`CONFLICT`	`263 263`		`S -> I (in Ref. 9; AA sequence).`
`CONFLICT`	`269 269`		`Q -> E (in Ref. 11; AA sequence).`
`STRAND`	`5 10`	`6`
`HELIX`	`18 32`	`15`
`STRAND`	`36 41`	`6`
`TURN`	`42 46`	`5`
`HELIX`	`53 55`	`3`
`HELIX`	`68 78`	`11`
`HELIX`	`83 94`	`12`
`STRAND`	`96 103`	`8`
`HELIX`	`111 120`	`10`
`TURN`	`123 125`	`3`
`HELIX`	`133 135`	`3`
`TURN`	`137 140`	`4`
`STRAND`	`142 148`	`7`
`HELIX`	`153 156`	`4`
`HELIX`	`165 173`	`9`
`HELIX`	`174 178`	`5`
`TURN`	`179 181`	`3`
`STRAND`	`188 190`	`3`
`HELIX`	`193 195`	`3`
`HELIX`	`198 212`	`15`
`HELIX`	`215 217`	`3`
`HELIX`	`226 228`	`3`
`TURN`	`233 236`	`4`
`STRAND`	`237 239`	`3`
`HELIX`	`241 247`	`7`
`STRAND`	`254 256`	`3`
`TURN`	`266 270`	`5`

Sequence information

Length: 274 AA [This is the length of the unprocessed precursor]

Molecular weight: 30947 Da [This is the MW of the unprocessed precursor]

CRC64: 40E8801320A20F09 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVRRALIVL AHAERTSFNY AMKEAAVEAL KKKGWEVVES DLYAMNFNPL ISRNDITGEP 

        70         80         90        100        110        120 
KDSENFQYPV ESSLAYKEGR LSPDIVAEQK KLEAADLVIF QFPLYWFGVP AILKGWFERV 

       130        140        150        160        170        180 
LVAGFAYTYA TMYDKGPFQN KKTLLSITTG GSGSMYSLQG VHGDMNVILW PIQSGILRFC 

       190        200        210        220        230        240 
GFQVLEPQLV YSIGHTPPDA RVQVLEGWKK RLETVWEESP LYFAPSSLFD LNFQAGFLLK 

       250        260        270 
KEVQEEQKKN KFGLSVGHHL GKSIPADNQI KARK

P05982 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools