Protein

Retinoid isomerohydrolase

Gene

RPE65

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

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:16116091). Essential for the production of 11-cis retinal for both rod and cone photoreceptors (PubMed:17848510). 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).By similarity3 Publications

Catalytic activityⁱ

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

Lutein = (3R,3'S)-zeaxanthin.1 Publication

Cofactorⁱ

Fe²⁺By similarityNote: Binds 1 Fe²⁺ ion per subunit.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	180	Iron; catalyticBy similarity	1
Metal bindingⁱ	241	Iron; catalyticBy similarity	1
Metal bindingⁱ	313	Iron; catalyticBy similarity	1
Metal bindingⁱ	527	Iron; catalyticBy similarity	1

GO - Molecular functionⁱ

all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity Source: AgBase
all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity Source: Reactome
cardiolipin binding Source: AgBase
isomerase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 28874556
metal ion binding Source: UniProtKB-KW
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: InterPro
phosphatidylcholine binding Source: AgBase
phosphatidylserine binding Source: AgBase
retinal isomerase activity Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to electrical stimulus Source: Ensembl
circadian rhythm Source: Ensembl
detection of light stimulus involved in visual perception
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15557452
insulin receptor signaling pathway Source: Ensembl
neural retina development Source: Ensembl
regulation of rhodopsin gene expression Source: Ensembl
retina homeostasis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15557452
retinal metabolic process Source: Ensembl
retina morphogenesis in camera-type eye Source: Ensembl
retinoid metabolic process Source: Reactome
visual perception
Source: ProtInc
Traceable author statementⁱ
- 9326941
vitamin A metabolic process
Source: ProtInc
Traceable author statementⁱ
- 9326941
zeaxanthin biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 28874556

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Isomerase
Biological process	Sensory transduction, Vision
Ligand	Iron, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000116745-MONOMER
Reactomeⁱ	R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)

Chemistry databases

SwissLipidsⁱ	SLP:000000687

SwissLipidsⁱ

SLP:000000687

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Retinoid isomerohydrolase (EC:3.1.1.64By similarity) Alternative name(s): All-trans-retinyl-palmitate hydrolase Meso-zeaxanthin isomerase1 Publication (EC:5.3.3.-1 Publication) Retinal pigment epithelium-specific 65 kDa protein Retinol isomerase
Gene namesⁱ	Name:RPE65
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000116745.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10294 RPE65
MIMⁱ	180069 gene
neXtProtⁱ	NX_Q16518

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Leber congenital amaurosis 2 (LCA2)13 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.

Retinitis pigmentosa 20 (RP20)6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_071672	60	L → P in RP20. 1 Publication	1
Natural variantⁱVAR_060809	79	Y → H in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752869EnsemblClinVar.	1
Natural variantⁱVAR_060810	85	R → H in RP20; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs61752870EnsemblClinVar.	1
Natural variantⁱVAR_017130	91	R → W in RP20. 5 PublicationsCorresponds to variant dbSNP:rs61752871EnsemblClinVar.	1
Natural variantⁱVAR_060811	95	E → Q in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752874EnsemblClinVar.	1
Natural variantⁱVAR_017132	132	A → T in RP20; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs61752878EnsemblClinVar.	1
Natural variantⁱVAR_060817	294	K → T in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752901EnsemblClinVar.	1
Natural variantⁱVAR_017137	341	L → S in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752909EnsemblClinVar.	1
Natural variantⁱVAR_017139	368	Y → H in RP20. 2 PublicationsCorresponds to variant dbSNP:rs62653011EnsemblClinVar.	1
Natural variantⁱVAR_060821	436	G → V in RP20. 1 PublicationCorresponds to variant dbSNP:rs62637002EnsemblClinVar.	1
Natural variantⁱVAR_017142	452	V → G in RP20. 1 PublicationCorresponds to variant dbSNP:rs62637004EnsemblClinVar.	1
Natural variantⁱVAR_060823	473	V → D in RP20. 3 PublicationsCorresponds to variant dbSNP:rs62637007EnsemblClinVar.	1
Natural variantⁱVAR_037619	515	R → W in RP20; this mutation has been found in compound heterozygosity in LCA2. 1 PublicationCorresponds to variant dbSNP:rs121917745EnsemblClinVar.	1
Natural variantⁱVAR_060824	528	G → V in RP20. 1 Publication	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	106	C → A: No loss of enzymatic activity. No effect on palmitoylation. No loss of membrane association. 1 Publication	1
Mutagenesisⁱ	112	C → A: Loss of enzymatic activity. No palmitoylation. Loss of membrane association. 1 Publication	1
Mutagenesisⁱ	180	H → A: Loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	241	H → A: Decreasing protein levels. Loss of enzymatic activity. Significantly decreased protein stability. 1 Publication	1
Mutagenesisⁱ	313	H → A: Decreasing protein levels. Loss of enzymatic activity. Significantly decreased protein stability. 1 Publication	1
Mutagenesisⁱ	469	E → A: Decreasing protein levels. Loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	469	E → Q: Decreasing protein levels. Loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	527	H → A: Decreasing protein levels. Loss of enzymatic activity. Significantly decreased protein stability. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6121
GeneReviewsⁱ	RPE65
MalaCards human disease database More...MalaCardsⁱ	RPE65
MIMⁱ	204100 phenotype 613794 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000116745
Orphanetⁱ	180 Choroideremia 65 Leber congenital amaurosis 791 Retinitis pigmentosa 364055 Severe early-childhood-onset retinal dystrophy
PharmGKBⁱ	PA34655

Chemistry databases

ChEMBLⁱ	CHEMBL3831182

ChEMBLⁱ

CHEMBL3831182

Polymorphism and mutation databases

BioMutaⁱ	RPE65
DMDMⁱ	44888872

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity
ChainⁱPRO_0000143943	2 – 533	Retinoid isomerohydrolaseAdd BLAST		532

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineBy similarity	1
Modified residueⁱ	101	Phosphothreonine1 Publication	1
Modified residueⁱ	105	Phosphothreonine1 Publication	1
Lipidationⁱ	112	S-palmitoyl cysteine; in membrane form1 Publication	1
Modified residueⁱ	113	N6-acetyllysine1 Publication	1
Modified residueⁱ	117	Phosphoserine1 Publication	1
Lipidationⁱ	231	S-palmitoyl cysteine; in membrane formBy similarity	1
Lipidationⁱ	329	S-palmitoyl cysteine; in membrane formBy similarity	1
Lipidationⁱ	330	S-palmitoyl cysteine; in membrane formBy similarity	1

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).By similarity

Keywords - PTMⁱ

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbⁱ	Q16518
PeptideAtlas More...PeptideAtlasⁱ	Q16518
PRIDEⁱ	Q16518
ProteomicsDBⁱ	60891

PTM databases

iPTMnetⁱ	Q16518
PhosphoSitePlusⁱ	Q16518
SwissPalmⁱ	Q16518

Expressionⁱ

Tissue specificityⁱ

Retina (at protein level). Retinal pigment epithelium specific.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000116745
CleanExⁱ	HS_RPE65
Genevisibleⁱ	Q16518 HS

Interactionⁱ

Subunit structureⁱ

Interacts with MYO7A; this mediates light-dependent intracellular transport of RPE65.1 Publication

Protein-protein interaction databases

BioGridⁱ	112041, 8 interactors
IntActⁱ	Q16518, 1 interactor
STRINGⁱ	9606.ENSP00000262340

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q16518
SMRⁱ	Q16518
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the carotenoid oxygenase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1285 Eukaryota COG3670 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00500000044783
HOGENOMⁱ	HOG000232156
HOVERGENⁱ	HBG050679
InParanoidⁱ	Q16518
KEGG Orthology (KO) More...KOⁱ	K11158
OMAⁱ	ITEFGTF
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G04WW
PhylomeDBⁱ	Q16518
TreeFamⁱ	TF314019

Family and domain databases

InterProⁱ	View protein in InterPro IPR004294 Carotenoid_Oase
PANTHERⁱ	PTHR10543 PTHR10543, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03055 RPE65, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

Q16518-1 [UniParc]FASTA Add 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 SKSEIVVQFP CSDRFKPSYV HSFGLTPNYI 
       260        270        280        290        300
VFVETPVKIN LFKFLSSWSL WGANYMDCFE SNETMGVWLH IADKKRKKYL 
       310        320        330        340        350
NNKYRTSPFN LFHHINTYED NGFLIVDLCC WKGFEFVYNY LYLANLRENW 
       360        370        380        390        400
EEVKKNARKA PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATAILCSDET 
       410        420        430        440        450
IWLEPEVLFS GPRQAFEFPQ INYQKYCGKP YTYAYGLGLN HFVPDRLCKL 
       460        470        480        490        500
NVKTKETWVW QEPDSYPSEP IFVSHPDALE EDDGVVLSVV VSPGAGQKPA 
       510        520        530 
YLLILNAKDL SEVARAEVEI NIPVTFHGLF KKS

Length:533

Mass (Da):60,948

Last modified:January 23, 2007 - v3

Checksum:ⁱ7193C93F3325798D

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	254	E → G in BAF82614 (PubMed:14702039).Curated		1
Sequence conflictⁱ	274	N → D in BAF82614 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_017126	22	L → P in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61751277EnsemblClinVar.	1
Natural variantⁱVAR_060808	36 – 38	Missing in LCA2. 1 Publication	3
Natural variantⁱVAR_017127	40	G → S in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61751281EnsemblClinVar.	1
Natural variantⁱVAR_017128	44	R → Q in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61751282EnsemblClinVar.	1
Natural variantⁱVAR_071672	60	L → P in RP20. 1 Publication	1
Natural variantⁱVAR_070172	67	L → R Found in a patient with relatively mild LCA2; uncertain pathological significance. 1 Publication	1
Natural variantⁱVAR_017129	68	H → Y in LCA2. 1 PublicationCorresponds to variant dbSNP:rs61752866EnsemblClinVar.	1
Natural variantⁱVAR_067160	70	F → V in LCA2 and RP20. 2 Publications	1
Natural variantⁱVAR_060809	79	Y → H in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752869EnsemblClinVar.	1
Natural variantⁱVAR_060810	85	R → H in RP20; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs61752870EnsemblClinVar.	1
Natural variantⁱVAR_067161	91	R → P in LCA2. 1 PublicationCorresponds to variant dbSNP:rs61752873EnsemblClinVar.	1
Natural variantⁱVAR_017131	91	R → Q in LCA2. 1 PublicationCorresponds to variant dbSNP:rs61752873EnsemblClinVar.	1
Natural variantⁱVAR_017130	91	R → W in RP20. 5 PublicationsCorresponds to variant dbSNP:rs61752871EnsemblClinVar.	1
Natural variantⁱVAR_060811	95	E → Q in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752874EnsemblClinVar.	1
Natural variantⁱVAR_067162	99	V → I Found in a patient with LCA2; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs143056561Ensembl.	1
Natural variantⁱVAR_060812	102	E → K in RP20 and LCA2. 2 PublicationsCorresponds to variant dbSNP:rs62642584EnsemblClinVar.	1
Natural variantⁱVAR_017132	132	A → T in RP20; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs61752878EnsemblClinVar.	1
Natural variantⁱVAR_017133	144	Y → D in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61752880EnsemblClinVar.	1
Natural variantⁱVAR_060813	148	E → D in LCA2. 1 PublicationCorresponds to variant dbSNP:rs61752882EnsemblClinVar.	1
Natural variantⁱVAR_060814	167	D → Y in RP20 and LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61752883EnsemblClinVar.	1
Natural variantⁱVAR_060815	182	H → N in LCA2. 1 PublicationCorresponds to variant dbSNP:rs61752884EnsemblClinVar.	1
Natural variantⁱVAR_017134	182	H → Y in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61752884EnsemblClinVar.	1
Natural variantⁱVAR_080043	234 – 533	Missing in LCA2; unknown pathological significance. 1 PublicationAdd BLAST	300
Natural variantⁱVAR_060816	239	Y → D in LCA2 and RP20. 2 PublicationsCorresponds to variant dbSNP:rs61752896EnsemblClinVar.	1
Natural variantⁱVAR_017135	287	V → F in LCA2. 1 PublicationCorresponds to variant dbSNP:rs281865289EnsemblClinVar.	1
Natural variantⁱVAR_060817	294	K → T in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752901EnsemblClinVar.	1
Natural variantⁱVAR_067163	313	H → R in LCA2. 1 Publication	1
Natural variantⁱVAR_017136	321	N → K3 PublicationsCorresponds to variant dbSNP:rs149916178EnsemblClinVar.	1
Natural variantⁱVAR_060818	330	C → Y in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs61752908EnsemblClinVar.	1
Natural variantⁱVAR_067164	333	G → R Found in a patient with LCA2. 1 Publication	1
Natural variantⁱVAR_017137	341	L → S in RP20. 1 PublicationCorresponds to variant dbSNP:rs61752909EnsemblClinVar.	1
Natural variantⁱVAR_017138	363	P → T in LCA2. 3 PublicationsCorresponds to variant dbSNP:rs121917744EnsemblClinVar.	1
Natural variantⁱVAR_070173	368	Y → C Found in a patient with relatively mild LCA2; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs62653012EnsemblClinVar.	1
Natural variantⁱVAR_017139	368	Y → H in RP20. 2 PublicationsCorresponds to variant dbSNP:rs62653011EnsemblClinVar.	1
Natural variantⁱVAR_060819	393	A → E in LCA2. 1 Publication	1
Natural variantⁱVAR_017140	393	A → G in LCA2. 1 PublicationCorresponds to variant dbSNP:rs62635773EnsemblClinVar.	1
Natural variantⁱVAR_017141	417	E → Q in LCA2. 1 PublicationCorresponds to variant dbSNP:rs62636299EnsemblClinVar.	1
Natural variantⁱVAR_018151	431	Y → C in LCA2. 1 PublicationCorresponds to variant dbSNP:rs62636300EnsemblClinVar.	1
Natural variantⁱVAR_034477	434	A → V in LCA2. 2 PublicationsCorresponds to variant dbSNP:rs34627040EnsemblClinVar.	1
Natural variantⁱVAR_060820	435	Y → C in LCA2. 1 PublicationCorresponds to variant dbSNP:rs62636302EnsemblClinVar.	1
Natural variantⁱVAR_060821	436	G → V in RP20. 1 PublicationCorresponds to variant dbSNP:rs62637002EnsemblClinVar.	1
Natural variantⁱVAR_017142	452	V → G in RP20. 1 PublicationCorresponds to variant dbSNP:rs62637004EnsemblClinVar.	1
Natural variantⁱVAR_060822	470	P → L in LCA2. 1 Publication	1
Natural variantⁱVAR_060823	473	V → D in RP20. 3 PublicationsCorresponds to variant dbSNP:rs62637007EnsemblClinVar.	1
Natural variantⁱVAR_067757	477	D → G Probable disease-associated mutation found in autosomal dominant retinitis pigmentosa with choroidal involvement. 1 Publication	1
Natural variantⁱVAR_037619	515	R → W in RP20; this mutation has been found in compound heterozygosity in LCA2. 1 PublicationCorresponds to variant dbSNP:rs121917745EnsemblClinVar.	1
Natural variantⁱVAR_060824	528	G → V in RP20. 1 Publication	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U18991 mRNA Translation: AAA99012.1 U20510 U20486 Genomic DNA Translation: AAC14586.1 AF039868 AF039867 Genomic DNA Translation: AAC39660.1 AK289925 mRNA Translation: BAF82614.1 AL139413 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX06478.1 BC075035 mRNA Translation: AAH75035.1 BC075036 mRNA Translation: AAH75036.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS643.1
NCBI Reference Sequences More...RefSeqⁱ	NP_000320.1, NM_000329.2
UniGeneⁱ	Hs.2133

Genome annotation databases

Ensemblⁱ	ENST00000262340; ENSP00000262340; ENSG00000116745
GeneIDⁱ	6121
KEGGⁱ	hsa:6121
UCSC genome browser More...UCSCⁱ	uc001dei.2 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q16518	RPE65 isoform 1		PANTR		533
RPE65 isoform 1		PONAB		533
RPE65, retinoid isomerohydrolase		Cebus capucinus imitator		533
RPE65, retinoid isomerohydrolase		PANPA		533
RPE65, retinoid isomerohydrolase		NOMLE		533
+111

Protein	Similar proteins		Species	Score	Length
Q16518	RPE65 isoform 1		PANTR		533
RPE65 isoform 1		PONAB		533
RPE65, retinoid isomerohydrolase		Cebus capucinus imitator		533
RPE65, retinoid isomerohydrolase		PANPA		533
RPE65, retinoid isomerohydrolase		NOMLE		533
+172

ChEMBLⁱ	CHEMBL3831182
SwissLipidsⁱ	SLP:000000687

Structural Biology Knowledgebase	Search...

CTDⁱ	6121
DisGeNET More...DisGeNETⁱ	6121
EuPathDBⁱ	HostDB:ENSG00000116745.6
GeneCardsⁱ	RPE65
GeneReviewsⁱ	RPE65
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10294 RPE65
MalaCards human disease database More...MalaCardsⁱ	RPE65
MIMⁱ	180069 gene 204100 phenotype 613794 phenotype
neXtProtⁱ	NX_Q16518
Open Targets More...OpenTargetsⁱ	ENSG00000116745
Orphanetⁱ	180 Choroideremia 65 Leber congenital amaurosis 791 Retinitis pigmentosa 364055 Severe early-childhood-onset retinal dystrophy
PharmGKBⁱ	PA34655
GenAtlas: human gene database More...GenAtlasⁱ	Search...

ChiTaRSⁱ	RPE65 human
GeneWikiⁱ	RPE65
GenomeRNAiⁱ	6121
Protein Ontology More...PROⁱ	PR:Q16518
SOURCEⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RPE65_HUMAN
Accessionⁱ	Q16518Primary (citable) accession number: Q16518 Secondary accession number(s): A8K1L0, Q5T9U3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
	Last sequence update:	January 23, 2007
	Last modified:	June 20, 2018
	This is version 153 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

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Supporting data

UniProtKB - Q16518 (RPE65_HUMAN)

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Retinoid isomerohydrolase

RPE65

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Endoplasmic reticulum

Other locations

Endoplasmic reticulum

Plasma Membrane

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ