QOR_RAT
ID QOR_RAT Reviewed; 329 AA.
AC Q6AYT0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
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}.
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DR EMBL; BC078927; AAH78927.1; -; mRNA.
DR RefSeq; NP_001012183.1; NM_001012183.2.
DR RefSeq; XP_006233582.1; XM_006233520.3.
DR AlphaFoldDB; Q6AYT0; -.
DR SMR; Q6AYT0; -.
DR STRING; 10116.ENSRNOP00000038188; -.
DR iPTMnet; Q6AYT0; -.
DR PhosphoSitePlus; Q6AYT0; -.
DR jPOST; Q6AYT0; -.
DR PaxDb; Q6AYT0; -.
DR PRIDE; Q6AYT0; -.
DR Ensembl; ENSRNOT00000032808; ENSRNOP00000038188; ENSRNOG00000028319.
DR GeneID; 362061; -.
DR KEGG; rno:362061; -.
DR CTD; 1429; -.
DR RGD; 1311639; Cryz.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000154882; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; Q6AYT0; -.
DR OMA; THIATRE; -.
DR OrthoDB; 863952at2759; -.
DR PhylomeDB; Q6AYT0; -.
DR TreeFam; TF314255; -.
DR PRO; PR:Q6AYT0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000028319; Expressed in kidney and 20 other tissues.
DR Genevisible; Q6AYT0; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; NADP; Oxidoreductase; Reference proteome;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q08257"
FT CHAIN 2..329
FT /note="Quinone oxidoreductase"
FT /id="PRO_0000160910"
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 229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 246..249
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 269..271
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 296
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47199"
SQ SEQUENCE 329 AA; 34975 MW; 02BD613047BF4B04 CRC64;
MATGQKLMRA IRVFEFGGPE VLKLQSDVVV PAPQSHQVLI KVHACGVNPV ETYIRSGTYS
RKPALPYTPG SDVAGIIESV GDGVSAFKKG DRVFCFSTVS GGYAEFALSA DNTTYPLPET
LDFRQGAALG IPYFTACRAL FHSARARAGE SVLVHGASGG VGLATCQIAR AHGLKVLGTA
GSEEGKKLVL QNGAHEVFNH KEANYIDKIK TSAGDKGVDV IIEMLANKNL SNDLKLLSCG
GRVIVVGCRG SIEINPRDTM AKETSIIGVS LFSSTKEEFQ QFAGILQAGI EKGWVKPVIG
SEYPLEKAAQ AHEDIIHSSG KMGKMILLL
