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Database: UniProt
Entry: A0A2Y9IWN6_ENHLU
LinkDB: A0A2Y9IWN6_ENHLU
Original site: A0A2Y9IWN6_ENHLU 
ID   A0A2Y9IWN6_ENHLU        Unreviewed;       533 AA.
AC   A0A2Y9IWN6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=LOC111143374 {ECO:0000313|RefSeq:XP_022352781.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022352781.1};
RN   [1] {ECO:0000313|RefSeq:XP_022352781.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022352781.1};
RG   RefSeq;
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   RefSeq; XP_022352781.1; XM_022497073.1.
DR   AlphaFoldDB; A0A2Y9IWN6; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0120254; P:olefinic compound metabolic process; IEA:UniProt.
DR   GO; GO:0001523; P:retinoid metabolic process; IEA:UniProt.
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:UP000248482};
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;  60991 MW;  6BA67A0975297781 CRC64;
     MSIQVEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF EVGSEPFYHL
     FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI TEFGTCAFPD PCKNIFSRFF
     SYFRGVEVTD NTLVNIYPVG EDYYACTETN FITKINPETL ETIKQVDLCN YVSVNGATAH
     PHIESDGTVY NIGNCFGKNF SIAYNIVKIP PLQADKEDPI SKSEVVVQFP CSDRFKPSYV
     HSFGLTPNYI VFVETPVKIN LFKFLSSWSL WGANYIDCFE SNETMGVWLH IADKKRRKYL
     NNKYRTSSFN LFHHINTYED NGFLIVDLCC WKGFEFVYNY LYLANLRENW EEVKKNARKA
     PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATAILCSDET IWLEPEVLFS GPRQAFEFPQ
     INYQKYGGKP YTYAYGLGLN HFIPDRLCKL NVKTKETWVW QEPDSYPSEP IFVSHPDALE
     EDDGVVLSVV VSPGAGQKPA YLLILNAKDL SEVARAEVEI NIPVTFHGWF KKS
//
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