| Identification |
|---|
| HMDB Protein ID
| HMDBP13938 |
| Secondary Accession Numbers
| None |
| Name
| Retinoid isomerohydrolase |
| Synonyms
|
- All-trans-retinyl-palmitate hydrolase
- Lutein isomerase
- Meso-zeaxanthin isomerase
- Retinal pigment epithelium-specific 65 kDa protein
- Retinol isomerase
|
| Gene Name
| RPE65 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific 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 (PubMed:19490105). Essential for the production of 11-cis retinal for both rod and cone photoreceptors (By similarity). Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (PubMed:28874556). 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 (By similarity). |
| Pathways
|
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| visual perception |
| zeaxanthin biosynthetic process |
| response to stimulus |
| retinoid metabolic process |
| Cellular Component |
| membrane |
| endoplasmic reticulum membrane |
| plasma membrane |
| Molecular Function |
| isomerase activity |
| phosphatidylcholine binding |
| oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity |
| all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity |
| phosphatidylserine binding |
| cardiolipin binding |
| retinal isomerase activity |
| retinol isomerase activity |
| metal ion binding |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 533 |
| Molecular Weight
| 60930.06 |
| Theoretical pI
| 6.834 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q9YGX2 |
| UniProtKB/Swiss-Prot Entry Name
| RPE65_CHICK |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Nikolaeva O, Takahashi Y, Moiseyev G, Ma JX: Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane. FEBS J. 2009 Jun;276(11):3020-30. doi: 10.1111/j.1742-4658.2009.07021.x. Epub 2009 Apr 20. [PubMed:19490105 ]
- Takahashi Y, Moiseyev G, Ma JX: Identification of key residues determining isomerohydrolase activity of human RPE65. J Biol Chem. 2014 Sep 26;289(39):26743-26751. doi: 10.1074/jbc.M114.558619. Epub 2014 Aug 11. [PubMed:25112876 ]
- Shyam R, Gorusupudi A, Nelson K, Horvath MP, Bernstein PS: RPE65 has an additional function as the lutein to meso-zeaxanthin isomerase in the vertebrate eye. Proc Natl Acad Sci U S A. 2017 Oct 10;114(41):10882-10887. doi: 10.1073/pnas.1706332114. Epub 2017 Sep 5. [PubMed:28874556 ]
|
