ID K7FCZ1_PELSI Unreviewed; 533 AA.
AC K7FCZ1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Lutein isomerase {ECO:0000256|ARBA:ARBA00041301};
DE AltName: Full=Meso-zeaxanthin isomerase {ECO:0000256|ARBA:ARBA00042900};
GN Name=RPE65 {ECO:0000313|Ensembl:ENSPSIP00000005901.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000005901.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000005901.1}
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 -!- 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; AGCU01088945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006123418.1; XM_006123356.2.
DR AlphaFoldDB; K7FCZ1; -.
DR STRING; 13735.ENSPSIP00000005901; -.
DR Ensembl; ENSPSIT00000005936.1; ENSPSIP00000005901.1; ENSPSIG00000005421.1.
DR GeneID; 102456788; -.
DR KEGG; pss:102456788; -.
DR CTD; 6121; -.
DR eggNOG; KOG1285; Eukaryota.
DR GeneTree; ENSGT00950000182913; -.
DR HOGENOM; CLU_016472_1_1_1; -.
DR OMA; VHHPFDG; -.
DR OrthoDB; 294919at2759; -.
DR TreeFam; TF314019; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
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:0052884; F:all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity; IEA:Ensembl.
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:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR GO; GO:1901827; P:zeaxanthin biosynthetic process; IEA:Ensembl.
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:UP000007267};
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; 61081 MW; 9E04F0E4BBBEB9BD CRC64;
MSSQIEHPAG GYKKLFETVE ELSSPVTAHV TGRIPIWLRG SLLRCGPGLF EVGSEPFYHL
FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI TEFGTYAYPD PCKNIFSRFF
SYFRGVEVTD NALVNVYPVG EDYYACTETN FITKINPETL ETIKQVDLCK YVSINGVTAH
PHIENDGTVY NIGNCFGKNF AIAYNIVRIP PLQADKKDPM NKSEVVVQFP CSDRFKPSYV
HSFGLTPNYI VFVETPVKIN LLKFLSSWSL WGANYMDCFE SNETMGVWLH VADKKKGKYL
NIKYRTSAFN LFHHINTYED NGFLIVDLCT WKGFEFVYNY LYLANLRSNW EEVKKHAEKA
PQPEARRYVL PLNIDKADTG KNLVTLPYTT ATATLHSDET IWLEPEILFS GARQAFEFPQ
INYKKYAGKP YTYAYGLGLN HFVPDRLCKM NVKTKETWVW QEPDSYPSEP IFVSHPDALE
EDDGVVLSVI VNPGTGQKPA YLLILNAKDM SEVARAEVEI NIPVTFHGMF KRS
//
