QOR_BOVIN
ID QOR_BOVIN Reviewed; 330 AA.
AC O97764; Q0VCY2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Zeta-crystallin;
GN Name=CRYZ;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Lens;
RX PubMed=9154917; DOI=10.1021/bi9622985;
RA Rao P.V., Gonzalez P., Persson B., Joernvall H., Garland D.,
RA Zigler J.S. Jr.;
RT "Guinea pig and bovine zeta-crystallins have distinct functional
RT characteristics highlighting replacements in otherwise similar
RT structures.";
RL Biochemistry 36:5353-5362(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interacts with (AU)-rich elements (ARE) in the 3'-UTR of
CC target mRNA species and enhances their stability. NADPH binding
CC interferes with mRNA binding (By similarity). Has minimal or no quinone
CC reductase activity. Binds strongly to single-stranded DNA.
CC {ECO:0000250, ECO:0000269|PubMed:9154917}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; U70048; AAD10290.1; -; mRNA.
DR EMBL; BC119936; AAI19937.1; -; mRNA.
DR RefSeq; NP_776450.2; NM_174025.3.
DR RefSeq; XP_005204423.1; XM_005204366.2.
DR RefSeq; XP_010801667.1; XM_010803365.2.
DR AlphaFoldDB; O97764; -.
DR SMR; O97764; -.
DR STRING; 9913.ENSBTAP00000041239; -.
DR PaxDb; O97764; -.
DR PeptideAtlas; O97764; -.
DR PRIDE; O97764; -.
DR Ensembl; ENSBTAT00000043686; ENSBTAP00000041239; ENSBTAG00000003162.
DR Ensembl; ENSBTAT00000084653; ENSBTAP00000059114; ENSBTAG00000003162.
DR GeneID; 281093; -.
DR KEGG; bta:281093; -.
DR CTD; 1429; -.
DR VEuPathDB; HostDB:ENSBTAG00000003162; -.
DR VGNC; VGNC:27746; CRYZ.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000154882; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; O97764; -.
DR OMA; THIATRE; -.
DR OrthoDB; 863952at2759; -.
DR TreeFam; TF314255; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000003162; Expressed in metanephros cortex and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IDA:MGI.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
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; DNA-binding; NADP; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q08257"
FT CHAIN 2..330
FT /note="Zeta-crystallin"
FT /id="PRO_0000160904"
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 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 CONFLICT 142
FT /note="H -> Y (in Ref. 1; AAD10290)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="C -> P (in Ref. 1; AAD10290)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="D -> N (in Ref. 1; AAD10290)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="N -> D (in Ref. 1; AAD10290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 35383 MW; 5E41DFC82B214A39 CRC64;
MATGQKLMRA IRVFEFGGPE VLKLQSDVAV PIPKDHQVLI KVQACGVNPV DTYIRSGTHN
IKPLLPYTPG FDVAGIIEAV GESVSAFKKG DRVFTTRTIS GGYAEYALAA DHTVYTLPEK
LDFKQGAAIG IPYFTAYRAL LHSACVKPGE SVLVHGASGG VGIAACQIAR AYGLKVLGTA
STEEGQKIVL ENGAHKVFNH KEADYIDKIK KSVGEKGVDV IIEMLANVNL SNDLNLLSHG
GRVIVVGSRG TIEINPRDTM TKESSIKGVT LFSSTKEEFQ QFAAALQAGM EIGWLRPVIG
PQYLLEKATQ AHENIIHSSG ATGKMILLLN
