ID   QOR_PIG                 Reviewed;         329 AA.
AC   Q0MVN8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Ibrahim H.M., Curthoys N.P.;
RT   "Sus scrofa renal zeta-crystallin (NADPH quinone reductase) cDNA.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ841573; ABH10011.1; -; mRNA.
DR   AlphaFoldDB; Q0MVN8; -.
DR   SMR; Q0MVN8; -.
DR   STRING; 9823.ENSSSCP00000004089; -.
DR   PaxDb; Q0MVN8; -.
DR   PeptideAtlas; Q0MVN8; -.
DR   PRIDE; Q0MVN8; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   InParanoid; Q0MVN8; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
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: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; Phosphoprotein;
KW   Reference proteome; 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_0000251735"
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         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08257"
SQ   SEQUENCE   329 AA;  34997 MW;  2D62ECE3555D0AC3 CRC64;
     MATGQKLMSA IRVFKFGGPE VMKLQSDVAI PIPKDNQVLI KVHACGVNPV DTYIRSGTHN
     MKPLLPYTPG LDVAGIVEAV GEHVSSFKKG DRVFTVSTLS GGYAEYALAA DDTVYMLPEK
     LDFKQGAAIG IPYFTACLAL LHSACVKAGE IVLIHGASGG VGIAACQIAR AYGLKVLGTA
     GTEEGQNIVL QNGAHEVFNH REVNYIDKIK KSVGEKGIDV IIEMLANVNL SNDLNLLSHG
     GRVIIVGSRG PIEINPRDTM TKGSSIKGVA LYSSTKEEFQ QLAAALQAGM EVGWLRPVIG
     PVYPLEKAAQ AHEDIIHSRG ATGKMILLL