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Protein

Retinoid isomerohydrolase

Gene

RPE65

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

An all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid.

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi180Iron; catalytic1
Metal bindingi241Iron; catalytic1
Metal bindingi313Iron; catalytic1
Metal bindingi527Iron; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoid isomerohydrolase (EC:3.1.1.64)
Alternative name(s):
All-trans-retinyl-palmitate hydrolase
Retinal pigment epithelium-specific 65 kDa protein
Retinol isomerase
Gene namesi
Name:RPE65
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity; Lipid-anchor By similarity
  • Microsome membrane By similarity

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180H → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi231C → S: Isomerization activity. 1 Publication1
Mutagenesisi241H → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi313H → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi329 – 330CC → SS: Decreasing protein levels. Loss of enzymatic activity. 1 Publication2
Mutagenesisi329C → S: Decreasing protein levels. Isomerization activity. 1 Publication1
Mutagenesisi330C → T: Isomerization activity. 1 Publication1
Mutagenesisi417E → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi527H → A: Loss of enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001439412 – 533Retinoid isomerohydrolaseAdd BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei101PhosphothreonineBy similarity1
Modified residuei105PhosphothreonineBy similarity1
Lipidationi112S-palmitoyl cysteine; in membrane formBy similarity1
Modified residuei113N6-acetyllysineBy similarity1
Modified residuei117PhosphoserineBy similarity1
Lipidationi231S-palmitoyl cysteine; in membrane formBy similarity1
Lipidationi329S-palmitoyl cysteine; in membrane formBy similarity1
Lipidationi330S-palmitoyl cysteine; in membrane formBy similarity1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ9TVB8.

Expressioni

Tissue specificityi

Retinal pigment epithelium specific.

Interactioni

Subunit structurei

Interacts with MYO7A; this mediates light-dependent intracellular transport of RPE65.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000030301.

Structurei

3D structure databases

ProteinModelPortaliQ9TVB8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the carotenoid oxygenase family.Curated

Phylogenomic databases

eggNOGiKOG1285. Eukaryota.
COG3670. LUCA.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ9TVB8.
KOiK11158.

Family and domain databases

InterProiIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERiPTHR10543. PTHR10543. 2 hits.
PfamiPF03055. RPE65. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9TVB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIQVEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF
60 70 80 90 100
EVGSEPFYHL FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI
110 120 130 140 150
TEFGTCAFPD PCKNIFSRFF SYFRGVEVTD NALVNVYPVG EDYYACTETN
160 170 180 190 200
FITKINPETL ETIKQVDLCN YVSVNGATAH PHIENDGTVY NIGNCFGKNF
210 220 230 240 250
SIAYNIVKIP PLQADKEDPI SKSEVVVQFP CSDRFKPSYV HSFGLTPNYI
260 270 280 290 300
VFVETPVKIN LLKFLSSWSL WGANYMDCFE SNETMGVWLH IADKKRKKYL
310 320 330 340 350
NNKYRTSSFN LFHHINTYED NEFLIVDLCC WKGFEFVYNY LYLANLRENW
360 370 380 390 400
EEVKKNARKA PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATATLRSDET
410 420 430 440 450
IWLEPEVLFS GPRQAFEFPQ INYQKSGGKP YTYAYGLGLN HFVPDRLCKL
460 470 480 490 500
NVKTKETWVW QEPDSYPSEP IFVSHPDALE EDDGVVLSVV VSPGAGQKPA
510 520 530
YLLILNAKDL SEVARAEVEI NIPVTFHGLF KKS
Length:533
Mass (Da):60,880
Last modified:January 23, 2007 - v3
Checksum:iEBEC87458BA4C91B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti368Y → S in AAC72356 (PubMed:9808841).Curated1
Sequence conflicti426S → Y in AAC72356 (PubMed:9808841).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084537 mRNA. Translation: AAC72356.1.
Y16567 mRNA. Translation: CAA76290.1.
AJ506754
, AJ506755, AJ506756, AJ506757, AJ251207, AJ506759 Genomic DNA. Translation: CAD45010.1.
RefSeqiNP_001003176.1. NM_001003176.1.
UniGeneiCfa.3665.

Genome annotation databases

GeneIDi403803.
KEGGicfa:403803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084537 mRNA. Translation: AAC72356.1.
Y16567 mRNA. Translation: CAA76290.1.
AJ506754
, AJ506755, AJ506756, AJ506757, AJ251207, AJ506759 Genomic DNA. Translation: CAD45010.1.
RefSeqiNP_001003176.1. NM_001003176.1.
UniGeneiCfa.3665.

3D structure databases

ProteinModelPortaliQ9TVB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000030301.

Proteomic databases

PaxDbiQ9TVB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403803.
KEGGicfa:403803.

Organism-specific databases

CTDi6121.

Phylogenomic databases

eggNOGiKOG1285. Eukaryota.
COG3670. LUCA.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ9TVB8.
KOiK11158.

Family and domain databases

InterProiIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERiPTHR10543. PTHR10543. 2 hits.
PfamiPF03055. RPE65. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPE65_CANLF
AccessioniPrimary (citable) accession number: Q9TVB8
Secondary accession number(s): O97623, Q8MJY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.