QOR_HUMAN
ID QOR_HUMAN Reviewed; 329 AA.
AC Q08257; A6NN60; D3DQ76; Q53FT0; Q59EU7; Q5HYE7; Q6NSK9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Quinone oxidoreductase;
DE EC=1.6.5.5;
DE AltName: Full=NADPH:quinone reductase;
DE AltName: Full=Zeta-crystallin;
GN Name=CRYZ;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8466529; DOI=10.1006/bbrc.1993.1302;
RA Gonzalez P., Rao P.V., Zigler J.S. Jr.;
RT "Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA
RT from human liver.";
RL Biochem. Biophys. Res. Commun. 191:902-907(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8088825; DOI=10.1006/geno.1994.1272;
RA Gonzalez P., Rao P.V., Zigler J.S. Jr.;
RT "Organization of the human zeta-crystallin/quinone reductase gene (CRYZ).";
RL Genomics 21:317-324(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-176.
RC TISSUE=Brain, Kidney proximal tubule, and Lung;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-66.
RC TISSUE=Testis;
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 [9]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=17497241; DOI=10.1007/s00018-007-7091-1;
RA Fernandez M.R., Porte S., Crosas E., Barbera N., Farres J., Biosca J.A.,
RA Pares X.;
RT "Human and yeast zeta-crystallins bind AU-rich elements in RNA.";
RL Cell. Mol. Life Sci. 64:1419-1427(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20103721; DOI=10.1096/fj.09-140459;
RA Lapucci A., Lulli M., Amedei A., Papucci L., Witort E., Di Gesualdo F.,
RA Bertolini F., Brewer G., Nicolin A., Bevilacqua A., Schiavone N.,
RA Morello D., Donnini M., Capaccioli S.;
RT "{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2
RT overexpression in T-cell acute lymphocytic leukemia.";
RL FASEB J. 24:1852-1865(2010).
RN [12]
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., Buerckstuemmer 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH NADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human zeta-crystallin at 1.85 A.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP and
CC acts through a one-electron transfer process. Orthoquinones, such as
CC 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates
CC (in vitro). May act in the detoxification of xenobiotics. Interacts
CC with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species.
CC Enhances the stability of mRNA coding for BCL2. NADPH binding
CC interferes with mRNA binding. {ECO:0000269|PubMed:17497241,
CC ECO:0000269|PubMed:20103721}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone +
CC NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC EC=1.6.5.5; Evidence={ECO:0000269|PubMed:17497241};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17497241,
CC ECO:0000269|Ref.17}.
CC -!- INTERACTION:
CC Q08257; Q08257: CRYZ; NbExp=3; IntAct=EBI-1044627, EBI-1044627;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20103721}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08257-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08257-2; Sequence=VSP_042927, VSP_042928;
CC Name=3;
CC IsoId=Q08257-3; Sequence=VSP_046425;
CC -!- TISSUE SPECIFICITY: Only very low amounts in the lens.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; L13278; AAA36536.1; -; mRNA.
DR EMBL; L31526; AAK40311.1; -; Genomic_DNA.
DR EMBL; L31521; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31522; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31523; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31524; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31525; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; AB209714; BAD92951.1; -; mRNA.
DR EMBL; AK223150; BAD96870.1; -; mRNA.
DR EMBL; AK223201; BAD96921.1; -; mRNA.
DR EMBL; BX647883; CAI46072.1; -; mRNA.
DR EMBL; AK314813; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC091611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06409.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06410.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06411.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06412.1; -; Genomic_DNA.
DR EMBL; BC039578; AAH39578.1; -; mRNA.
DR EMBL; BC070058; AAH70058.1; -; mRNA.
DR CCDS; CCDS44162.1; -. [Q08257-3]
DR CCDS; CCDS44163.1; -. [Q08257-2]
DR CCDS; CCDS665.1; -. [Q08257-1]
DR PIR; PN0448; PN0448.
DR RefSeq; NP_001123514.1; NM_001130042.1. [Q08257-1]
DR RefSeq; NP_001123515.1; NM_001130043.1. [Q08257-3]
DR RefSeq; NP_001128231.1; NM_001134759.1. [Q08257-2]
DR RefSeq; NP_001880.2; NM_001889.3. [Q08257-1]
DR RefSeq; XP_005270548.1; XM_005270491.4. [Q08257-2]
DR RefSeq; XP_011539049.1; XM_011540747.1. [Q08257-1]
DR RefSeq; XP_016855856.1; XM_017000367.1. [Q08257-3]
DR RefSeq; XP_016855857.1; XM_017000368.1. [Q08257-2]
DR PDB; 1YB5; X-ray; 1.85 A; A/B=1-329.
DR PDBsum; 1YB5; -.
DR AlphaFoldDB; Q08257; -.
DR SMR; Q08257; -.
DR BioGRID; 107816; 151.
DR IntAct; Q08257; 12.
DR STRING; 9606.ENSP00000399805; -.
DR BindingDB; Q08257; -.
DR ChEMBL; CHEMBL6118; -.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB00266; Dicoumarol.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR GlyGen; Q08257; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08257; -.
DR PhosphoSitePlus; Q08257; -.
DR SwissPalm; Q08257; -.
DR BioMuta; CRYZ; -.
DR DMDM; 585013; -.
DR REPRODUCTION-2DPAGE; IPI00000792; -.
DR EPD; Q08257; -.
DR jPOST; Q08257; -.
DR MassIVE; Q08257; -.
DR MaxQB; Q08257; -.
DR PaxDb; Q08257; -.
DR PeptideAtlas; Q08257; -.
DR PRIDE; Q08257; -.
DR ProteomicsDB; 1584; -.
DR ProteomicsDB; 58584; -. [Q08257-1]
DR ProteomicsDB; 58585; -. [Q08257-2]
DR Antibodypedia; 19697; 114 antibodies from 21 providers.
DR DNASU; 1429; -.
DR Ensembl; ENST00000340866.10; ENSP00000339399.5; ENSG00000116791.14. [Q08257-1]
DR Ensembl; ENST00000370871.7; ENSP00000359908.3; ENSG00000116791.14. [Q08257-3]
DR Ensembl; ENST00000370872.7; ENSP00000359909.3; ENSG00000116791.14. [Q08257-2]
DR Ensembl; ENST00000417775.5; ENSP00000399805.1; ENSG00000116791.14. [Q08257-1]
DR GeneID; 1429; -.
DR KEGG; hsa:1429; -.
DR MANE-Select; ENST00000340866.10; ENSP00000339399.5; NM_001889.4; NP_001880.2.
DR UCSC; uc001dgj.4; human. [Q08257-1]
DR CTD; 1429; -.
DR DisGeNET; 1429; -.
DR GeneCards; CRYZ; -.
DR HGNC; HGNC:2419; CRYZ.
DR HPA; ENSG00000116791; Tissue enhanced (kidney, liver).
DR MIM; 123691; gene.
DR neXtProt; NX_Q08257; -.
DR OpenTargets; ENSG00000116791; -.
DR PharmGKB; PA26925; -.
DR VEuPathDB; HostDB:ENSG00000116791; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000154882; -.
DR HOGENOM; CLU_026673_19_0_1; -.
DR InParanoid; Q08257; -.
DR OMA; THIATRE; -.
DR OrthoDB; 863952at2759; -.
DR PhylomeDB; Q08257; -.
DR TreeFam; TF314255; -.
DR BRENDA; 1.3.1.27; 2681.
DR BRENDA; 1.6.5.5; 2681.
DR PathwayCommons; Q08257; -.
DR SignaLink; Q08257; -.
DR BioGRID-ORCS; 1429; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; CRYZ; human.
DR EvolutionaryTrace; Q08257; -.
DR GeneWiki; CRYZ; -.
DR GenomeRNAi; 1429; -.
DR Pharos; Q08257; Tbio.
DR PRO; PR:Q08257; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q08257; protein.
DR Bgee; ENSG00000116791; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; Q08257; baseline and differential.
DR Genevisible; Q08257; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..329
FT /note="Quinone oxidoreductase"
FT /id="PRO_0000160906"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 158..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 246..249
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 269..271
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 296
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47199"
FT VAR_SEQ 1..5
FT /note="MATGQ -> MHLLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_042927"
FT VAR_SEQ 6..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_042928"
FT VAR_SEQ 211..244
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046425"
FT VARIANT 66
FT /note="P -> S (in dbSNP:rs11551729)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_022913"
FT VARIANT 176
FT /note="I -> V (in dbSNP:rs3819946)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022914"
FT VARIANT 183
FT /note="E -> K (in dbSNP:rs17095822)"
FT /id="VAR_048200"
FT CONFLICT 105
FT /note="E -> G (in Ref. 3; AK314813)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1YB5"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:1YB5"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1YB5"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:1YB5"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1YB5"
SQ SEQUENCE 329 AA; 35207 MW; 68C1828911486D4E CRC64;
MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS
RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK
LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA
GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG
GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG
SQYPLEKVAE AHENIIHGSG ATGKMILLL
