ID   B4DLR8_HUMAN            Unreviewed;       202 AA.
AC   B4DLR8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=NAD(P)H dehydrogenase [quinone] 1 {ECO:0000256|ARBA:ARBA00040776};
DE            EC=1.6.5.2 {ECO:0000256|ARBA:ARBA00012648};
DE   AltName: Full=Azoreductase {ECO:0000256|ARBA:ARBA00042298};
DE   AltName: Full=DT-diaphorase {ECO:0000256|ARBA:ARBA00042416};
DE   AltName: Full=Menadione reductase {ECO:0000256|ARBA:ARBA00042248};
DE   AltName: Full=NAD(P)H:quinone oxidoreductase 1 {ECO:0000256|ARBA:ARBA00042288};
DE   AltName: Full=Phylloquinone reductase {ECO:0000256|ARBA:ARBA00041787};
DE   AltName: Full=Quinone reductase 1 {ECO:0000256|ARBA:ARBA00042364};
GN   Name=NQO1 {ECO:0000313|Ensembl:ENSP00000398330.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG59630.1};
RN   [1] {ECO:0000313|Ensembl:ENSP00000398330.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [2] {ECO:0000313|EMBL:BAG59630.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [4] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [5] {ECO:0007829|PubMed:28112733}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [6] {ECO:0000313|Ensembl:ENSP00000398330.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10;
CC         Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183;
CC         Evidence={ECO:0000256|ARBA:ARBA00036802};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985;
CC         Evidence={ECO:0000256|ARBA:ARBA00036802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + menadione + NADH = menadiol + NAD(+);
CC         Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000256|ARBA:ARBA00036047};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696;
CC         Evidence={ECO:0000256|ARBA:ARBA00036047};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00036936};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46161;
CC         Evidence={ECO:0000256|ARBA:ARBA00036936};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00036270};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165;
CC         Evidence={ECO:0000256|ARBA:ARBA00036270};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC       {ECO:0000256|ARBA:ARBA00006252}.
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DR   EMBL; AC092115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK297125; BAG59630.1; -; mRNA.
DR   RefSeq; NP_001273066.1; NM_001286137.1.
DR   ProteomicsDB; 4555; -.
DR   Antibodypedia; 1549; 919 antibodies from 43 providers.
DR   DNASU; 1728; -.
DR   Ensembl; ENST00000439109.6; ENSP00000398330.2; ENSG00000181019.13.
DR   GeneID; 1728; -.
DR   UCSC; uc010vll.4; human.
DR   CTD; 1728; -.
DR   HGNC; HGNC:2874; NQO1.
DR   VEuPathDB; HostDB:ENSG00000181019; -.
DR   GeneTree; ENSGT00940000159150; -.
DR   OrthoDB; 5471423at2759; -.
DR   BioGRID-ORCS; 1728; 20 hits in 1161 CRISPR screens.
DR   ChiTaRS; NQO1; human.
DR   GenomeRNAi; 1728; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; ENSG00000181019; Expressed in endometrium epithelium and 202 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.50.360; -; 2.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   PANTHER; PTHR10204; NAD P H OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR10204:SF1; NAD(P)H DEHYDROGENASE [QUINONE] 1; 1.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
PE   1: Evidence at protein level;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Proteomics identification {ECO:0007829|EPD:B4DLR8,
KW   ECO:0007829|MaxQB:B4DLR8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          5..102
FT                   /note="Flavodoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF02525"
SQ   SEQUENCE   202 AA;  22793 MW;  845809C562CA8320 CRC64;
     MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL
     KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QSGILHFCGF QVLEPQLTYS
     IGHTPADARI QILEGWKKRL ENIWDETPLY FAPSSLFDLN FQAGFLMKKE VQDEEKNKKF
     GLSVGHHLGK SIPTDNQIKA RK
//