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Protein

NAD(P)H dehydrogenase [quinone] 1

Gene

Nqo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121FAD1 Publication
Binding sitei67 – 671FAD1 Publication
Binding sitei156 – 1561FAD1 Publication
Binding sitei201 – 2011FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 192FAD1 Publication
Nucleotide bindingi104 – 1074FAD1 Publication
Nucleotide bindingi148 – 1514FAD1 Publication

GO - Molecular functioni

GO - Biological processi

  • aging Source: Ensembl
  • negative regulation of catalytic activity Source: MGI
  • positive regulation of neuron apoptotic process Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to nutrient Source: Ensembl
  • response to oxidative stress Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BRENDAi1.6.5.2. 3474.
ReactomeiR-MMU-350562. Regulation of ornithine decarboxylase (ODC).

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Nqo1
Synonyms:Dia4, Nmo1, Nmor1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:103187. Nqo1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 274273NAD(P)H dehydrogenase [quinone] 1PRO_0000071623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ64669.
PaxDbiQ64669.
PRIDEiQ64669.

PTM databases

iPTMnetiQ64669.
PhosphoSiteiQ64669.

Expressioni

Inductioni

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

Gene expression databases

BgeeiQ64669.
CleanExiMM_NQO1.
ExpressionAtlasiQ64669. baseline and differential.
GenevisibleiQ64669. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003947.

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi18 – 3215Combined sources
Beta strandi36 – 416Combined sources
Helixi42 – 454Combined sources
Helixi68 – 7710Combined sources
Helixi83 – 9412Combined sources
Beta strandi96 – 1038Combined sources
Helixi111 – 12010Combined sources
Turni123 – 1253Combined sources
Beta strandi129 – 1313Combined sources
Helixi133 – 1353Combined sources
Turni137 – 1404Combined sources
Beta strandi141 – 15111Combined sources
Helixi153 – 1564Combined sources
Beta strandi160 – 1623Combined sources
Helixi165 – 1739Combined sources
Turni174 – 1763Combined sources
Helixi177 – 1804Combined sources
Beta strandi188 – 1914Combined sources
Turni193 – 1953Combined sources
Helixi198 – 21215Combined sources
Helixi213 – 2175Combined sources
Helixi226 – 2283Combined sources
Turni233 – 2364Combined sources
Beta strandi237 – 2393Combined sources
Helixi241 – 2477Combined sources
Beta strandi254 – 2563Combined sources
Turni268 – 2703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXQX-ray2.80A/B/C/D2-274[»]
ProteinModelPortaliQ64669.
SMRiQ64669. Positions 2-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64669.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1283Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IKWF. Eukaryota.
COG2249. LUCA.
GeneTreeiENSGT00440000033410.
HOGENOMiHOG000149970.
HOVERGENiHBG029104.
InParanoidiQ64669.
KOiK00355.
OMAiYDKGPFQ.
OrthoDBiEOG7CZK6F.
PhylomeDBiQ64669.
TreeFamiTF300296.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARRALIVL AHSEKTSFNY AMKEAAVEAL KKRGWEVLES DLYAMNFNPI
60 70 80 90 100
ISRNDITGEL KDSKNFQYPS ESSLAYKEGR LSPDIVAEHK KLEAADLVIF
110 120 130 140 150
QFPLQWFGVP AILKGWFERV LVAGFAYTYA AMYDNGPFQN KKTLLSITTG
160 170 180 190 200
GSGSMYSLQG VHGDMNVILW PIQSGILRFC GFQVLEPQLV YSIGHTPPDA
210 220 230 240 250
RMQILEGWKK RLETVWEETP LYFAPSSLFD LNFQAGFLMK KEVQEEQKKN
260 270
KFGLSVGHHL GKSIPADNQI KARK
Length:274
Mass (Da):30,960
Last modified:January 23, 2007 - v3
Checksum:i68F380922FD72965
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12961 mRNA. Translation: AAA80184.1.
S75951 mRNA. Translation: AAB32718.1.
CCDSiCCDS40465.1.
PIRiA57691.
RefSeqiNP_032732.3. NM_008706.5.
UniGeneiMm.252.

Genome annotation databases

EnsembliENSMUST00000003947; ENSMUSP00000003947; ENSMUSG00000003849.
GeneIDi18104.
KEGGimmu:18104.
UCSCiuc009nhq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12961 mRNA. Translation: AAA80184.1.
S75951 mRNA. Translation: AAB32718.1.
CCDSiCCDS40465.1.
PIRiA57691.
RefSeqiNP_032732.3. NM_008706.5.
UniGeneiMm.252.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXQX-ray2.80A/B/C/D2-274[»]
ProteinModelPortaliQ64669.
SMRiQ64669. Positions 2-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003947.

Chemistry

ChEMBLiCHEMBL5611.

PTM databases

iPTMnetiQ64669.
PhosphoSiteiQ64669.

Proteomic databases

MaxQBiQ64669.
PaxDbiQ64669.
PRIDEiQ64669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003947; ENSMUSP00000003947; ENSMUSG00000003849.
GeneIDi18104.
KEGGimmu:18104.
UCSCiuc009nhq.1. mouse.

Organism-specific databases

CTDi1728.
MGIiMGI:103187. Nqo1.

Phylogenomic databases

eggNOGiENOG410IKWF. Eukaryota.
COG2249. LUCA.
GeneTreeiENSGT00440000033410.
HOGENOMiHOG000149970.
HOVERGENiHBG029104.
InParanoidiQ64669.
KOiK00355.
OMAiYDKGPFQ.
OrthoDBiEOG7CZK6F.
PhylomeDBiQ64669.
TreeFamiTF300296.

Enzyme and pathway databases

BRENDAi1.6.5.2. 3474.
ReactomeiR-MMU-350562. Regulation of ornithine decarboxylase (ODC).

Miscellaneous databases

EvolutionaryTraceiQ64669.
NextBioi293281.
PROiQ64669.
SOURCEiSearch...

Gene expression databases

BgeeiQ64669.
CleanExiMM_NQO1.
ExpressionAtlasiQ64669. baseline and differential.
GenevisibleiQ64669. MM.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Spleen and Testis.
  4. "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.

Entry informationi

Entry nameiNQO1_MOUSE
AccessioniPrimary (citable) accession number: Q64669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.