ID   QOR_PONAB               Reviewed;         329 AA.
AC   Q5R4S7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR861167; CAH93239.1; -; mRNA.
DR   RefSeq; NP_001126904.1; NM_001133432.1.
DR   AlphaFoldDB; Q5R4S7; -.
DR   SMR; Q5R4S7; -.
DR   STRING; 9601.ENSPPYP00000001437; -.
DR   GeneID; 100173920; -.
DR   KEGG; pon:100173920; -.
DR   CTD; 1429; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   InParanoid; Q5R4S7; -.
DR   OrthoDB; 863952at2759; -.
DR   Proteomes; UP000001595; 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_0000160909"
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"
FT   MOD_RES         296
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47199"
SQ   SEQUENCE   329 AA;  35083 MW;  6C0E97E7F832F7D9 CRC64;
     MATGQKLMRA VRVFEFGGPE VLKLQSDIAV PIPKDHQALI KVHACGVNPV ETYIRSGTYS
     RKPLLPYTPG SDVAGVIEAV GGNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK
     LDFKQGAAIG IPYFTAYRAL IHSAHVKAGE SVLVHGASGG VGLAACQIAR AYGLKVLGTA
     GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDV IIEMLANVNL NKDLSLLSHG
     GQVIVVGSRG TIEINPRDTM AKESSIIGVT VFSSTKEEFQ QYAAALQAGM EIGWLKPVIG
     SQYPLEKVAE AHENIIHGSG ATGKMILLL