ID W5PPC6_SHEEP Unreviewed; 533 AA.
AC W5PPC6; A0A6P3E426;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Retinoid isomerohydrolase {ECO:0000256|ARBA:ARBA00040820};
DE EC=3.1.1.64 {ECO:0000256|ARBA:ARBA00039141};
DE EC=5.3.3.22 {ECO:0000256|ARBA:ARBA00038936};
DE AltName: Full=All-trans-retinyl-palmitate hydrolase {ECO:0000256|ARBA:ARBA00042047};
DE AltName: Full=Lutein isomerase {ECO:0000256|ARBA:ARBA00041301};
DE AltName: Full=Meso-zeaxanthin isomerase {ECO:0000256|ARBA:ARBA00042900};
DE AltName: Full=Retinal pigment epithelium-specific 65 kDa protein {ECO:0000256|ARBA:ARBA00042696};
DE AltName: Full=Retinol isomerase {ECO:0000256|ARBA:ARBA00030541};
GN Name=RPE65 {ECO:0000313|Ensembl:ENSOARP00000012302.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000012302.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000012302.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000012302.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000012302.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = 11-cis-retinol + H(+)
CC + hexadecanoate; Xref=Rhea:RHEA:31775, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302,
CC ChEBI:CHEBI:17616; EC=3.1.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00035843};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:31771, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:63410; EC=3.1.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00036037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein = (3R,3'S)-zeaxanthin; Xref=Rhea:RHEA:12729,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:138919; EC=5.3.3.22;
CC Evidence={ECO:0000256|ARBA:ARBA00035787};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SUBUNIT: Interacts with MYO7A; this mediates light-dependent
CC intracellular transport of RPE65. {ECO:0000256|ARBA:ARBA00038755}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787, ECO:0000256|RuleBase:RU003799}.
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DR EMBL; AMGL01002210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01002211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004002119.1; XM_004002070.3.
DR AlphaFoldDB; W5PPC6; -.
DR SMR; W5PPC6; -.
DR STRING; 9940.ENSOARP00000012302; -.
DR PaxDb; 9940-ENSOARP00000012302; -.
DR Ensembl; ENSOART00000012477.1; ENSOARP00000012302.1; ENSOARG00000011470.1.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_1_1_1; -.
DR OMA; VHHPFDG; -.
DR OrthoDB; 294919at2759; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000011470; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052885; F:all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity; ISS:AgBase.
DR GO; GO:1901612; F:cardiolipin binding; ISS:AgBase.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:AgBase.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:AgBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR PANTHER; PTHR10543:SF57; RETINOID ISOMEROHYDROLASE; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 313
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 527
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 533 AA; 61011 MW; EF5BAA54DCD27736 CRC64;
MSIQVEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF EVGSEPFYHL
FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI TEFGTCAFPD PCKNIFSRFF
SYFRGVEVTD NALVNIYPVG EDYYACTETN FITKINPETL ETIKQVDLCN YVSVNGATAH
PHIENDGTVY NIGNCFGKNF SIAYNIVKIP PLQADKEDPI SKSEIVVQFP CSDRFKPSYV
HSFGLTPNYI VFVETPVKIN LFKFLSSWSL WGANYMDCFE SNETMGVWLH IADKKRKKYI
NNKYRTSPFN LFHHINTYED HEFLIVDLCC WKGFEFVYNY LYLANLRENW EEVKKNARKA
PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATAILCSDET IWLEPEVLFS GPRQAFEFPQ
INYQKYGGKP YTYAYGLGLN HFVPDRLCKL NVKTKETWVW QEPDSYPSEP IFVSHPDALE
EDDGVVLSVV VSPGAGQKPA YLLILNAKDL SEVARAEVEI NIPVTFHGLF KKS
//
