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Q64669 (NQO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NAD(P)H dehydrogenase [quinone] 1
EC=1.6.5.2
Alternative name(s):
Azoreductase
DT-diaphorase
Short name=DTD
Menadione reductase
NAD(P)H:quinone oxidoreductase 1
Phylloquinone reductase
Quinone reductase 1
Short name=QR1
Gene names
Name:Nqo1
Synonyms:Dia4, Nmo1, Nmor1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 By similarity.

Catalytic activity

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.

Cofactor

FAD.

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm.

Induction

By polycyclic hydrocarbons such as dioxin (Governed by the aromatic hydrocarbon-responsive (AH) locus).

Sequence similarities

Belongs to the NAD(P)H dehydrogenase (quinone) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 274273NAD(P)H dehydrogenase [quinone] 1
PRO_0000071623

Regions

Nucleotide binding18 – 192FAD
Nucleotide binding104 – 1074FAD
Nucleotide binding148 – 1514FAD
Region126 – 1283Substrate binding By similarity

Sites

Binding site121FAD
Binding site671FAD
Binding site1561FAD
Binding site2011FAD

Amino acid modifications

Modified residue21N-acetylalanine

Secondary structure

1 ................................................... 274
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q64669 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 68F380922FD72965

FASTA27430,960
        10         20         30         40         50         60 
MAARRALIVL AHSEKTSFNY AMKEAAVEAL KKRGWEVLES DLYAMNFNPI ISRNDITGEL 

        70         80         90        100        110        120 
KDSKNFQYPS ESSLAYKEGR LSPDIVAEHK KLEAADLVIF QFPLQWFGVP AILKGWFERV 

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

       190        200        210        220        230        240 
GFQVLEPQLV YSIGHTPPDA RMQILEGWKK RLETVWEETP LYFAPSSLFD LNFQAGFLMK 

       250        260        270 
KEVQEEQKKN KFGLSVGHHL GKSIPADNQI KARK

« Hide

References

[1]"Mouse dioxin-inducible NAD(P)H: menadione oxidoreductase: NMO1 cDNA sequence and genetic differences in mRNA levels."
Vasiliou V., Theurer M.J., Puga A., Reuter S.F., Nebert D.W.
Pharmacogenetics 4:341-348(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"Mouse liver NAD(P)H:quinone acceptor oxidoreductase: protein sequence analysis by tandem mass spectrometry, cDNA cloning, expression in Escherichia coli, and enzyme activity analysis."
Chen S., Clarke P.E., Martino P.A., Deng P.S., Yeh C.H., Lee T.D., Prochaska H.J., Talalay P.
Protein Sci. 3:1296-1304(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[3]"Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release."
Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D., Amzel L.M.
Proc. Natl. Acad. Sci. U.S.A. 97:3177-3182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U12961 mRNA. Translation: AAA80184.1.
S75951 mRNA. Translation: AAB32718.1.
IPIIPI00263899.
PIRA57691.
RefSeqNP_032732.3. NM_008706.5.
UniGeneMm.252.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXQX-ray2.80A/B/C/D2-274[»]
ProteinModelPortalQ64669.
SMRQ64669. Positions 2-274.
ModBaseSearch...

PTM databases

PhosphoSiteQ64669.

Proteomic databases

PaxDbQ64669.
PRIDEQ64669.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003947; ENSMUSP00000003947; ENSMUSG00000003849.
GeneID18104.
KEGGmmu:18104.

Organism-specific databases

CTD1728.
MGIMGI:103187. Nqo1.

Phylogenomic databases

eggNOGCOG2249.
GeneTreeENSGT00440000033410.
HOGENOMHOG000149970.
HOVERGENHBG029104.
InParanoidQ64669.
KOK00355.
OMAGILHYPG.
OrthoDBEOG44BB36.

Gene expression databases

ArrayExpressQ64669.
BgeeQ64669.
CleanExMM_NQO1.
GenevestigatorQ64669.
GermOnlineENSMUSG00000003849. Mus musculus.

Family and domain databases

InterProIPR003680. Flavodoxin_fold.
[Graphical view]
PfamPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5611.
EvolutionaryTraceQ64669.
NextBio293281.
SOURCESearch...

Entry information

Entry nameNQO1_MOUSE
AccessionPrimary (citable) accession number: Q64669
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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