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Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Meso-zeaxanthin isomerase) (EC 5.3.3.-) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase)

 RPE65_CANLF             Reviewed;         533 AA.
Q9TVB8; O97623; Q8MJY9;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 93.
RecName: Full=Retinoid isomerohydrolase;
EC=3.1.1.64 {ECO:0000250|UniProtKB:Q28175};
AltName: Full=All-trans-retinyl-palmitate hydrolase;
AltName: Full=Meso-zeaxanthin isomerase;
EC=5.3.3.- {ECO:0000250|UniProtKB:Q16518};
AltName: Full=Retinal pigment epithelium-specific 65 kDa protein;
AltName: Full=Retinol isomerase;
Name=RPE65;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9808841;
Aguirre G.D., Baldwin V., Pearce-Kelling S., Narfstrom K., Ray K.,
Acland G.M.;
"Congenital stationary night blindness in the dog: common mutation in
the RPE65 gene indicates founder effect.";
Mol. Vis. 4:23-23(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Druttne N0606; TISSUE=Retinal pigment epithelium;
PubMed=10191083; DOI=10.1006/geno.1999.5754;
Veske A., Nilsson S.E.G., Narfstrom K., Gal A.;
"Retinal dystrophy of Swedish briard/briard-beagle dogs is due to a 4-
bp deletion in RPE65.";
Genomics 57:57-61(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-533.
Dekomien G., Epplen J.T.;
"Evaluation of the RPE65 gene as a candidate gene for generalised
progressive retinal atrophy.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[4]
COFACTOR, MUTAGENESIS OF HIS-180; CYS-231; HIS-241; HIS-313; CYS-329;
329-CYS-CYS-330; CYS-330; GLU-417 AND HIS-527, AND METAL-BINDING.
PubMed=16150724; DOI=10.1073/pnas.0504167102;
Redmond T.M., Poliakov E., Yu S., Tsai J.Y., Lu Z., Gentleman S.;
"Mutation of key residues of RPE65 abolishes its enzymatic role as
isomerohydrolase in the visual cycle.";
Proc. Natl. Acad. Sci. U.S.A. 102:13658-13663(2005).
-!- FUNCTION: Critical isomerohydrolase in the retinoid cycle involved
in regeneration of 11-cis-retinal, the chromophore of rod and cone
opsins. Catalyzes the cleavage and isomerization of all-trans-
retinyl fatty acid esters to 11-cis-retinol which is further
oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use
as visual chromophore. Essential for the production of 11-cis
retinal for both rod and cone photoreceptors. Also capable of
catalyzing the isomerization of lutein to meso-zeaxanthin an eye-
specific carotenoid. The soluble form binds vitamin A (all-trans-
retinol), making it available for LRAT processing to all-trans-
retinyl ester. The membrane form, palmitoylated by LRAT, binds
all-trans-retinyl esters, making them available for IMH
(isomerohydrolase) processing to all-cis-retinol. The soluble form
is regenerated by transferring its palmitoyl groups onto 11-cis-
retinol, a reaction catalyzed by LRAT.
{ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}.
-!- CATALYTIC ACTIVITY: An all-trans-retinyl ester + H(2)O = 11-cis-
retinol + a fatty acid. {ECO:0000250|UniProtKB:Q28175}.
-!- CATALYTIC ACTIVITY: Lutein = (3R,3'S)-zeaxanthin.
{ECO:0000250|UniProtKB:Q16518}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:16150724};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:16150724};
-!- SUBUNIT: Interacts with MYO7A; this mediates light-dependent
intracellular transport of RPE65. {ECO:0000250|UniProtKB:Q16518}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}.
Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor
{ECO:0000250|UniProtKB:Q28175}. Microsome membrane
{ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a
lipid anchor when palmitoylated (membrane form), soluble when
unpalmitoylated. Undergoes light-dependent intracellular transport
to become more concentrated in the central region of the retina
pigment epithelium cells (By similarity).
{ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}.
-!- TISSUE SPECIFICITY: Retinal pigment epithelium specific.
-!- PTM: Palmitoylation by LRAT regulates ligand binding specificity;
the palmitoylated form (membrane form) specifically binds all-
trans-retinyl-palmitate, while the soluble unpalmitoylated form
binds all-trans-retinol (vitamin A).
{ECO:0000250|UniProtKB:Q28175}.
-!- SIMILARITY: Belongs to the carotenoid oxygenase family.
{ECO:0000305}.
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EMBL; AF084537; AAC72356.1; -; mRNA.
EMBL; Y16567; CAA76290.1; -; mRNA.
EMBL; AJ506754; CAD45010.1; -; Genomic_DNA.
EMBL; AJ506755; CAD45010.1; JOINED; Genomic_DNA.
EMBL; AJ506756; CAD45010.1; JOINED; Genomic_DNA.
EMBL; AJ506757; CAD45010.1; JOINED; Genomic_DNA.
EMBL; AJ251207; CAD45010.1; JOINED; Genomic_DNA.
EMBL; AJ506759; CAD45010.1; JOINED; Genomic_DNA.
RefSeq; NP_001003176.1; NM_001003176.1.
UniGene; Cfa.3665; -.
ProteinModelPortal; Q9TVB8; -.
SMR; Q9TVB8; -.
STRING; 9615.ENSCAFP00000030301; -.
PaxDb; Q9TVB8; -.
GeneID; 403803; -.
KEGG; cfa:403803; -.
CTD; 6121; -.
eggNOG; KOG1285; Eukaryota.
eggNOG; COG3670; LUCA.
HOGENOM; HOG000232156; -.
HOVERGEN; HBG050679; -.
InParanoid; Q9TVB8; -.
KO; K11158; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISS:AgBase.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0052885; F:all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity; ISS:AgBase.
GO; GO:0052884; F:all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity; IEA:UniProtKB-EC.
GO; GO:1901612; F:cardiolipin binding; ISS:AgBase.
GO; GO:0016853; F:isomerase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
GO; GO:0031210; F:phosphatidylcholine binding; ISS:AgBase.
GO; GO:0001786; F:phosphatidylserine binding; ISS:AgBase.
GO; GO:0004744; F:retinal isomerase activity; ISS:UniProtKB.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
GO; GO:1901827; P:zeaxanthin biosynthetic process; ISS:UniProtKB.
InterPro; IPR004294; Carotenoid_Oase.
PANTHER; PTHR10543; PTHR10543; 1.
Pfam; PF03055; RPE65; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Hydrolase; Iron; Isomerase; Lipoprotein;
Membrane; Metal-binding; Microsome; Palmitate; Phosphoprotein;
Reference proteome; Sensory transduction; Vision.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q28175}.
CHAIN 2 533 Retinoid isomerohydrolase.
/FTId=PRO_0000143941.
METAL 180 180 Iron; catalytic.
{ECO:0000269|PubMed:16150724}.
METAL 241 241 Iron; catalytic.
{ECO:0000269|PubMed:16150724}.
METAL 313 313 Iron; catalytic.
{ECO:0000269|PubMed:16150724}.
METAL 527 527 Iron; catalytic.
{ECO:0000269|PubMed:16150724}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q28175}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16518}.
MOD_RES 105 105 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16518}.
MOD_RES 113 113 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16518}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:Q16518}.
LIPID 112 112 S-palmitoyl cysteine; in membrane form.
{ECO:0000250|UniProtKB:Q28175}.
LIPID 231 231 S-palmitoyl cysteine; in membrane form.
{ECO:0000250|UniProtKB:Q28175}.
LIPID 329 329 S-palmitoyl cysteine; in membrane form.
{ECO:0000250|UniProtKB:Q28175}.
LIPID 330 330 S-palmitoyl cysteine; in membrane form.
{ECO:0000250|UniProtKB:Q28175}.
MUTAGEN 180 180 H->A: Loss of enzymatic activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 231 231 C->S: Isomerization activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 241 241 H->A: Loss of enzymatic activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 313 313 H->A: Loss of enzymatic activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 329 330 CC->SS: Decreasing protein levels. Loss
of enzymatic activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 329 329 C->S: Decreasing protein levels.
Isomerization activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 330 330 C->T: Isomerization activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 417 417 E->A: Loss of enzymatic activity.
{ECO:0000269|PubMed:16150724}.
MUTAGEN 527 527 H->A: Loss of enzymatic activity.
{ECO:0000269|PubMed:16150724}.
CONFLICT 368 368 Y -> S (in Ref. 1; AAC72356).
{ECO:0000305}.
CONFLICT 426 426 S -> Y (in Ref. 1; AAC72356).
{ECO:0000305}.
SEQUENCE 533 AA; 60880 MW; EBEC87458BA4C91B CRC64;
MSIQVEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF EVGSEPFYHL
FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI TEFGTCAFPD PCKNIFSRFF
SYFRGVEVTD NALVNVYPVG EDYYACTETN FITKINPETL ETIKQVDLCN YVSVNGATAH
PHIENDGTVY NIGNCFGKNF SIAYNIVKIP PLQADKEDPI SKSEVVVQFP CSDRFKPSYV
HSFGLTPNYI VFVETPVKIN LLKFLSSWSL WGANYMDCFE SNETMGVWLH IADKKRKKYL
NNKYRTSSFN LFHHINTYED NEFLIVDLCC WKGFEFVYNY LYLANLRENW EEVKKNARKA
PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATATLRSDET IWLEPEVLFS GPRQAFEFPQ
INYQKSGGKP YTYAYGLGLN HFVPDRLCKL NVKTKETWVW QEPDSYPSEP IFVSHPDALE
EDDGVVLSVV VSPGAGQKPA YLLILNAKDL SEVARAEVEI NIPVTFHGLF KKS


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