QOR_MOUSE
ID QOR_MOUSE Reviewed; 331 AA.
AC P47199; Q62508; Q99L63;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8170370; DOI=10.1093/oxfordjournals.molbev.a040111;
RA Gonzalez P., Hernandez-Calzadilla C., Rao P.V., Rodriguez I.R.,
RA Zigler J.S. Jr., Borras T.;
RT "Comparative analysis of the zeta-crystallin/quinone reductase gene in
RT guinea pig and mouse.";
RL Mol. Biol. Evol. 11:305-315(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-331.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
RA Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
RA Sugaya E.;
RT "Molecular characterization of seizure-related genes isolated by
RT differential screening.";
RL Biochem. Biophys. Res. Commun. 219:795-799(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 and
CC enhances their stability. NADPH binding interferes with mRNA binding
CC (By similarity). {ECO:0000250}.
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;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S70056; AAB30620.2; -; mRNA.
DR EMBL; BC003800; AAH03800.1; -; mRNA.
DR EMBL; D78646; BAA11463.1; -; mRNA.
DR CCDS; CCDS17927.1; -.
DR PIR; A54932; A54932.
DR RefSeq; NP_034098.1; NM_009968.3.
DR RefSeq; XP_006501036.1; XM_006500973.2.
DR RefSeq; XP_011238308.1; XM_011240006.1.
DR AlphaFoldDB; P47199; -.
DR SMR; P47199; -.
DR BioGRID; 198924; 3.
DR IntAct; P47199; 1.
DR STRING; 10090.ENSMUSP00000029850; -.
DR BindingDB; P47199; -.
DR ChEMBL; CHEMBL4332; -.
DR iPTMnet; P47199; -.
DR PhosphoSitePlus; P47199; -.
DR SwissPalm; P47199; -.
DR REPRODUCTION-2DPAGE; IPI00134704; -.
DR REPRODUCTION-2DPAGE; P47199; -.
DR CPTAC; non-CPTAC-3666; -.
DR EPD; P47199; -.
DR jPOST; P47199; -.
DR MaxQB; P47199; -.
DR PaxDb; P47199; -.
DR PeptideAtlas; P47199; -.
DR PRIDE; P47199; -.
DR ProteomicsDB; 301906; -.
DR Antibodypedia; 19697; 114 antibodies from 21 providers.
DR DNASU; 12972; -.
DR Ensembl; ENSMUST00000029850; ENSMUSP00000029850; ENSMUSG00000028199.
DR Ensembl; ENSMUST00000192462; ENSMUSP00000142105; ENSMUSG00000028199.
DR GeneID; 12972; -.
DR KEGG; mmu:12972; -.
DR UCSC; uc008rup.3; mouse.
DR CTD; 1429; -.
DR MGI; MGI:88527; Cryz.
DR VEuPathDB; HostDB:ENSMUSG00000028199; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000154882; -.
DR InParanoid; P47199; -.
DR OMA; THIATRE; -.
DR OrthoDB; 863952at2759; -.
DR PhylomeDB; P47199; -.
DR TreeFam; TF314255; -.
DR BioGRID-ORCS; 12972; 2 hits in 75 CRISPR screens.
DR PRO; PR:P47199; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P47199; protein.
DR Bgee; ENSMUSG00000028199; Expressed in adult mammalian kidney and 246 other tissues.
DR ExpressionAtlas; P47199; baseline and differential.
DR Genevisible; P47199; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISS: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 Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q08257"
FT CHAIN 2..331
FT /note="Quinone oxidoreductase"
FT /id="PRO_0000160908"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 271..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q08257"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08257"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 298
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 58
FT /note="A -> T (in Ref. 2; AAH03800)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..133
FT /note="IPY -> TMD (in Ref. 3; BAA11463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 35269 MW; 35816C043EFE16A2 CRC64;
MATGQKLMRA IRVFEFGGPE VLKLQSDVVV PVPQSHQVLI KVHACGVNPV ETYIRSGAYS
RKPALPYTPG SDVAGIIESV GDKVSAFKKG DRVFCYSTVS GGYAEFALAA DDTIYPLPET
LNFRQGAALG IPYFTACRAL FHSARARAGE SVLVHGASGG VGLATCQIAR AHGLKVLGTA
GSEEGKKLVL QNGAHEVFNH KEANYIDKIK MSVGDKDKGV DVIIEMLANE NLSNDLKLLS
HGGRVVVVGC RGPIEINPRD TMAKETSIIG VSLSSSTKEE FQQFAGLLQA GIEKGWVKPV
IGSEYPLEKA AQAHEDIIHG SGKTGKMILL L
