QOR_CAVPO
ID QOR_CAVPO Reviewed; 329 AA.
AC P11415;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2777081; DOI=10.1016/0378-1119(89)90224-2;
RA Rodokanaki A., Holmes R.K., Borras T.;
RT "Zeta-crystallin, a novel protein from the guinea pig lens is related to
RT alcohol dehydrogenases.";
RL Gene 78:215-224(1989).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=1420281;
RA Rao P.V., Zigler J.S. Jr.;
RT "Purification and characterization of zeta-crystallin/quinone reductase
RT from guinea pig liver.";
RL Biochim. Biophys. Acta 1117:315-320(1992).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=1370456; DOI=10.1016/s0021-9258(18)48464-5;
RA Rao P.V., Krishna C.M., Zigler J.S. Jr.;
RT "Identification and characterization of the enzymatic activity of zeta-
RT crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase.";
RL J. Biol. Chem. 267:96-102(1992).
RN [4]
RP INVOLVEMENT IN CATARACT.
RX PubMed=1390943; DOI=10.1016/0925-4439(92)90025-i;
RA Rodriguez I.R., Gonzalez P., Zigler J.S. Jr., Borras T.;
RT "A guinea-pig hereditary cataract contains a splice-site deletion in a
RT crystallin gene.";
RL Biochim. Biophys. Acta 1180:44-52(1992).
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 {ECO:0000269|PubMed:1370456, ECO:0000269|PubMed:1420281}.
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; Evidence={ECO:0000269|PubMed:1370456,
CC ECO:0000269|PubMed:1420281};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: In guinea pigs it constitutes about 10% of the
CC water soluble proteins of the lens.
CC -!- DISEASE: Note=A genomic mutation causing the deletion of 34 amino acids
CC was clearly associated with a hereditary nuclear cataract in a line of
CC strain 13 guinea pigs. {ECO:0000269|PubMed:1390943}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; M26936; AAA37035.1; -; mRNA.
DR PIR; JS0230; CYGPZ.
DR RefSeq; NP_001166407.1; NM_001172936.1.
DR RefSeq; XP_005007806.1; XM_005007749.2.
DR RefSeq; XP_012998113.1; XM_013142659.1.
DR AlphaFoldDB; P11415; -.
DR SMR; P11415; -.
DR STRING; 10141.ENSCPOP00000005873; -.
DR MoonProt; P11415; -.
DR Ensembl; ENSCPOT00000006587; ENSCPOP00000005873; ENSCPOG00000006521.
DR GeneID; 100135507; -.
DR KEGG; ag:AAA37035; -.
DR KEGG; cpoc:100135507; -.
DR CTD; 1429; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000154882; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; P11415; -.
DR OMA; THIATRE; -.
DR OrthoDB; 863952at2759; -.
DR TreeFam; TF314255; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000006521; Expressed in adult mammalian kidney and 13 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IDA:CAFA.
DR GO; GO:0005212; F:structural constituent of eye lens; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:1901662; P:quinone catabolic process; IDA:CAFA.
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; Direct protein sequencing; Eye lens protein; NADP;
KW Oxidoreductase; 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_0000160905"
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; 35202 MW; 1463632C672C234F CRC64;
MATGQKLMRA IRVFEFGGPE VLKVQSDVAV PIPKDHQVLI KVHACGINPV ETYIRSGTYT
RIPLLPYTPG TDVAGVVESI GNDVSAFKKG DRVFTTSTIS GGYAEYALAS DHTVYRLPEK
LDFRQGAAIG IPYFTACRAL FHSARAKAGE SVLVHGASGG VGLAACQIAR AYGLKVLGTA
GTEEGQKVVL QNGAHEVFNH RDAHYIDEIK KSIGEKGVDV IIEMLANVNL SNDLKLLSCG
GRVIIVGCRG SIEINPRDTM AKESTISGVS LFSSTKEEFQ QFASTIQAGM ELGWVKPVIG
SQYPLEKASQ AHENIIHSSG TVGKTVLLM
