Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01135
Entry Name
UniProt Accession
Theoretical PI
6.05
Molecular Weight
60947.55
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Retinoid isomerohydrolase
Protein Synonyms/Alias
3.1.1.64; All-trans-retinyl-palmitate hydrolase; Retinal pigment epithelium-specific 65 kDa protein; Retinol isomerase;
Gene Name
RPE65
Gene Synonyms/Alias
Created Date
10-OCT-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
112
Canonical
TCAFPDPCKNIFSRF
[3]
S-Palmitoylation
231
Canonical
EIVVQFPCSDRFKPS
[1][2]
S-Palmitoylation
329
Canonical
GFLIVDLCCWKGFEF
[1][2]
S-Palmitoylation
330
Canonical
FLIVDLCCWKGFEFV
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Xue L, Gollapalli DR, Maiti P, Jahng WJ, Rando RR. A palmitoylation switchmechanism in the regulation of the visual cycle. Cell. 2004 Jun 11;117(6):761-71.[PMID:15186777]
[2] Takahashi Y, Moiseyev G, Chen Y, Ma JX. The roles of three palmitoylationsites of RPE65 in its membrane association and isomerohydrolase activity. Invest Ophthalmol Vis Sci. 2006 Dec;47(12):5191-6.[PMID:17122102]
[3] Takahashi Y, Moiseyev G, Ablonczy Z, Chen Y, Crouch RK, Ma JX. Identification of a novel palmitylation site essential for membrane association andisomerohydrolase activity of RPE65. J Biol Chem. 2009 Jan 30;284(5):3211-8. doi: 10.1074/jbc.M807248200. Epub 2008 Dec 1.[PMID:19049981]
Functional Description
Plays important roles in the production of 11-cis retinal and in visual pigment regeneration. 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. The enzymatic activity is linearly dependent of the expression levels and membrane association.
Sequence Annotation
Metal binding site: 180 180 Iron; catalytic.
Metal binding site: 241 241 Iron; catalytic.
Metal binding site: 313 313 Iron; catalytic.
Metal binding site: 527 527 Iron; catalytic.
Modified residue: 2 2 N-acetylserine.
Modified residue: 101 101 Phosphothreonine.
Modified residue: 105 105 Phosphothreonine.
Modified residue: 113 113 N6-acetyllysine.
Modified residue: 117 117 Phosphoserine.
Protein Length
533 AA.
Protein Sequence
(Canonical)
MSIQVEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF EVGSEPFYHL  60
FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI TEFGTCAFPD PCKNIFSRFF  120
SYFRGVEVTD NALVNVYPVG EDYYACTETN FITKINPETL ETIKQVDLCN YVSVNGATAH  180
PHIENDGTVY NIGNCFGKNF SIAYNIVKIP PLQADKEDPI SKSEIVVQFP CSDRFKPSYV  240
HSFGLTPNYI VFVETPVKIN LFKFLSSWSL WGANYMDCFE SNETMGVWLH IADKKRKKYL  300
NNKYRTSPFN LFHHINTYED NGFLIVDLCC WKGFEFVYNY LYLANLRENW EEVKKNARKA  360
PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATAILCSDET IWLEPEVLFS GPRQAFEFPQ  420
INYQKYCGKP YTYAYGLGLN HFVPDRLCKL NVKTKETWVW QEPDSYPSEP IFVSHPDALE  480
EDDGVVLSVV VSPGAGQKPA YLLILNAKDL SEVARAEVEI NIPVTFHGLF KKS         533
FASTA
(Canonical)
>LipidDB-9606-01135|Q16518
MSIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHL
FDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFF
SYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAH
PHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEIVVQFPCSDRFKPSYV
HSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYL
NNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKA
PQPEVRRYVLPLNIDKADTGKNLVTLPNTTATAILCSDETIWLEPEVLFSGPRQAFEFPQ
INYQKYCGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALE
EDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS
Gene Ontology
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0052885; F:all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity; IEA:UniProtKB-EC
GO:0052884; F:all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity; IEA:UniProtKB-EC
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004744; F:retinal isomerase activity; IEA:Ensembl
GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl
GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProt
GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl
GO:0007603; P:phototransduction, visible light; TAS:Reactome
GO:0007468; P:regulation of rhodopsin gene expression; IEA:Ensembl
GO:0001895; P:retina homeostasis; IMP:UniProt
GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl
GO:0042574; P:retinal metabolic process; IEA:Ensembl
GO:0001523; P:retinoid metabolic process; TAS:Reactome
GO:0007601; P:visual perception; TAS:ProtInc
GO:0006776; P:vitamin A metabolic process; TAS:ProtInc
Interpro
InterPro; IPR004294; Carotenoid_Oase
Pfam
Pfam; PF03055; RPE65;
SMART
PROSITE
PRINTS