| Identification |
|---|
| HMDB Protein ID
| HMDBP13939 |
| 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. 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. |
| Pathways
|
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| retinoid metabolic process |
| visual perception |
| response to stimulus |
| zeaxanthin biosynthetic process |
| Cellular Component |
| endoplasmic reticulum membrane |
| plasma membrane |
| membrane |
| Molecular Function |
| metal ion binding |
| 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 |
|
| 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
| 60879.88 |
| Theoretical pI
| 6.484 |
| 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
| Q9TVB8 |
| UniProtKB/Swiss-Prot Entry Name
| RPE65_CANLF |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Aguirre GD, Baldwin V, Pearce-Kelling S, Narfstrom K, Ray K, Acland GM: Congenital stationary night blindness in the dog: common mutation in the RPE65 gene indicates founder effect. Mol Vis. 1998 Oct 30;4:23. [PubMed:9808841 ]
- Veske A, Nilsson SE, Narfstrom K, Gal A: Retinal dystrophy of Swedish briard/briard-beagle dogs is due to a 4-bp deletion in RPE65. Genomics. 1999 Apr 1;57(1):57-61. doi: 10.1006/geno.1999.5754. [PubMed:10191083 ]
- Redmond TM, Poliakov E, Yu S, Tsai JY, 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. 2005 Sep 20;102(38):13658-63. doi: 10.1073/pnas.0504167102. Epub 2005 Sep 6. [PubMed:16150724 ]
- Li Y, Furhang R, Ray A, Duncan T, Soucy J, Mahdi R, Chaitankar V, Gieser L, Poliakov E, Qian H, Liu P, Dong L, Rogozin IB, Redmond TM: Aberrant RNA splicing is the major pathogenic effect in a knock-in mouse model of the dominantly inherited c.1430A>G human RPE65 mutation. Hum Mutat. 2019 Apr;40(4):426-443. doi: 10.1002/humu.23706. Epub 2019 Jan 25. [PubMed:30628748 ]
|
