Q9TVB8 · RPE65_CANLF
- ProteinRetinoid isomerohydrolase
- GeneRPE65
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids533 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Catalytic activity
- an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid + H+
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity | |
Molecular Function | all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity | |
Molecular Function | beta-carotene 15,15'-dioxygenase activity | |
Molecular Function | cardiolipin binding | |
Molecular Function | isomerase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatidylcholine binding | |
Molecular Function | phosphatidylserine binding | |
Molecular Function | retinol isomerase activity | |
Biological Process | retinal metabolic process | |
Biological Process | retinoid metabolic process | |
Biological Process | visual perception | |
Biological Process | zeaxanthin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRetinoid isomerohydrolase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionQ9TVB8
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
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).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 180 | Loss of enzymatic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 231 | Does not affect isomerization activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 241 | Loss of isomerohydrolase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 313 | Loss of isomerohydrolase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 329 | Decreasing protein levels. isomerohydrolase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 329-330 | Decreasing protein levels. Loss of isomerohydrolase activity. | ||||
Sequence: CC → SS | ||||||
Mutagenesis | 330 | Does not affect isomerohydrolase activity. | ||||
Sequence: C → T | ||||||
Mutagenesis | 417 | Loss of enzymatic isomerohydrolase. | ||||
Sequence: E → A | ||||||
Mutagenesis | 477 | Does not affect isomerohydrolase activity. | ||||
Sequence: D → G, E, or N | ||||||
Mutagenesis | 527 | Loss of isomerohydrolase activity. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000143941 | 2-533 | Retinoid isomerohydrolase | |||
Sequence: SIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLLKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYLNNKYRTSSFNLFHHINTYEDNEFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATATLRSDETIWLEPEVLFSGPRQAFEFPQINYQKSGGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS | ||||||
Modified residue | 101 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 105 | Phosphothreonine | ||||
Sequence: T | ||||||
Lipidation | 112 | S-palmitoyl cysteine; in membrane form | ||||
Sequence: C | ||||||
Modified residue | 113 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 117 | Phosphoserine | ||||
Sequence: S | ||||||
Lipidation | 231 | S-palmitoyl cysteine; in membrane form | ||||
Sequence: C | ||||||
Lipidation | 329 | S-palmitoyl cysteine; in membrane form | ||||
Sequence: C | ||||||
Lipidation | 330 | S-palmitoyl cysteine; in membrane form | ||||
Sequence: C |
Post-translational modification
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).
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Retinal pigment epithelium specific.
Interaction
Subunit
Interacts with MYO7A; this mediates light-dependent intracellular transport of RPE65.
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the carotenoid oxygenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length533
- Mass (Da)60,880
- Last updated2007-01-23 v3
- ChecksumEBEC87458BA4C91B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 368 | in Ref. 1; AAC72356 | ||||
Sequence: Y → S | ||||||
Sequence conflict | 426 | in Ref. 1; AAC72356 | ||||
Sequence: S → Y |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF084537 EMBL· GenBank· DDBJ | AAC72356.1 EMBL· GenBank· DDBJ | mRNA | ||
Y16567 EMBL· GenBank· DDBJ | CAA76290.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ506754 EMBL· GenBank· DDBJ | CAD45010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ506755 EMBL· GenBank· DDBJ | CAD45010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ506756 EMBL· GenBank· DDBJ | CAD45010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ506757 EMBL· GenBank· DDBJ | CAD45010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ251207 EMBL· GenBank· DDBJ | CAD45010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ506759 EMBL· GenBank· DDBJ | CAD45010.1 EMBL· GenBank· DDBJ | Genomic DNA |