ID   QOR_LAMGU               Reviewed;         330 AA.
AC   Q28452;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Lama guanicoe (Guanaco) (Lama glama guanicoe).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Lama.
OX   NCBI_TaxID=9840;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RX   PubMed=7476124; DOI=10.1093/oxfordjournals.molbev.a040255;
RA   Gonzalez P., Rao P.V., Nunez S.B., Zigler J.S. Jr.;
RT   "Evidence for independent recruitment of zeta-crystallin/quinone reductase
RT   (CRYZ) as a crystallin in camelids and hystricomorph rodents.";
RL   Mol. Biol. Evol. 12:773-781(1995).
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.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR   EMBL; L34159; AAA99986.1; -; mRNA.
DR   AlphaFoldDB; Q28452; -.
DR   SMR; Q28452; -.
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; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q08257"
FT   CHAIN           2..330
FT                   /note="Quinone oxidoreductase"
FT                   /id="PRO_0000160907"
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   330 AA;  35187 MW;  E784E414D2BA23D6 CRC64;
     MATGQRLMRA IRVSEFGGPE VLKLQSDVAV PIPEEHQVLI KVQACGVNPV DTYIRSGTYS
     RKPRLPYTPG LDVAGLIEAV GERVSAFKKG DRVFTTSTVS GGYAEYALAA DHTVYKLPGE
     LDFQKGAAIG VPYFTAYRAL LHSACAKAGE SVLVHGASGG VGLAACQIAR ACCFKVLGTA
     GTEEGQRVVL QNGAHEVFNH REDINIDKIK KSVGEKGIDV IIEMLANVNL SNDLNLLSQG
     GRVIIVGSKG PVEINPRDTM TKESSIKGVT LFSSTKEEFQ QFAAALQAGM EIGWLRPVIG
     SQYPLEKVAQ AHEDLTHSSG AAGKVVLLLK