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Q91ZQ5

- RPE65_MOUSE

UniProt

Q91ZQ5 - RPE65_MOUSE

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Protein
Retinoid isomerohydrolase
Gene
Rpe65
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 Publications

Catalytic activityi

An all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid.1 Publication

Cofactori

Binds 1 Fe2+ ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi180 – 1801Iron; catalytic By similarity
Metal bindingi241 – 2411Iron; catalytic By similarity
Metal bindingi313 – 3131Iron; catalytic By similarity
Metal bindingi527 – 5271Iron; catalytic By similarity

GO - Molecular functioni

  1. all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity Source: UniProtKB-EC
  2. all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. retinal isomerase activity Source: MGI

GO - Biological processi

  1. cellular response to electrical stimulus Source: MGI
  2. insulin receptor signaling pathway Source: MGI
  3. regulation of rhodopsin gene expression Source: MGI
  4. retina development in camera-type eye Source: MGI
  5. retina morphogenesis in camera-type eye Source: MGI
  6. retinal metabolic process Source: MGI
  7. visual perception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_188277. The canonical retinoid cycle in rods (twilight vision).

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:98001. Rpe65.

Subcellular locationi

Cytoplasm By similarity. Cell membrane; 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.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. organelle membrane Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Involvement in diseasei

Defects in Rpe65 are the cause of light damage susceptibility (LDS) of the retina.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 533532Retinoid isomerohydrolase
PRO_0000143944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei101 – 1011Phosphothreonine By similarity
Modified residuei105 – 1051Phosphothreonine By similarity
Lipidationi112 – 1121S-palmitoyl cysteine; in membrane form By similarity
Modified residuei113 – 1131N6-acetyllysine By similarity
Modified residuei117 – 1171Phosphoserine By similarity
Lipidationi231 – 2311S-palmitoyl cysteine; in membrane form By similarity
Lipidationi329 – 3291S-palmitoyl cysteine; in membrane form By similarity
Lipidationi330 – 3301S-palmitoyl cysteine; in membrane form By similarity

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

PRIDEiQ91ZQ5.

PTM databases

PhosphoSiteiQ91ZQ5.

Expressioni

Tissue specificityi

Retinal pigment epithelium specific.2 Publications

Gene expression databases

CleanExiMM_RPE65.
GenevestigatoriQ91ZQ5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029824.

Structurei

3D structure databases

ProteinModelPortaliQ91ZQ5.
SMRiQ91ZQ5. Positions 4-533.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3670.
GeneTreeiENSGT00500000044783.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ91ZQ5.
KOiK11158.
OMAiTIREPSV.
TreeFamiTF314019.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q91ZQ5-1 [UniParc]FASTAAdd to Basket

« Hide

MSIQIEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF    50
EVGSEPFYHL FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI 100
TEFGTCAFPD PCKNIFSRFF SYFKGVEVTD NALVNIYPVG EDYYACTETN 150
FITKINPETL ETIKQVDLCN YISVNGATAH PHIESDGTVY NIGNCFGKNF 200
TVAYNIIKIP PLKADKEDPI NKSEVVVQFP CSDRFKPSYV HSFGLTPNYI 250
VFVETPVKIN LFKFLSSWSL WGANYMDCFE SNESMGVWLH VADKKRRKYF 300
NNKYRTSPFN LFHHINTYED NGFLIVDLCC WKGFEFVYNY LYLANLRENW 350
EEVKRNAMKA PQPEVRRYVL PLTIDKVDTG RNLVTLPHTT ATATLRSDET 400
IWLEPEVLFS GPRQAFEFPQ INYQKFGGKP YTYAYGLGLN HFVPDKLCKM 450
NVKTKEIWMW QEPDSYPSEP IFVSQPDALE EDDGVVLSVV VSPGAGQKPA 500
YLLVLNAKDL SEIARAEVET NIPVTFHGLF KRS 533
Length:533
Mass (Da):61,085
Last modified:December 11, 2013 - v4
Checksum:iBBDA3EBDF5B7A5E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti450 – 4501M → L Increased light damage susceptibility. 2 Publications

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF410461 mRNA. Translation: AAL01119.1.
AC163272 Genomic DNA. No translation available.
CH466532 Genomic DNA. Translation: EDL11842.1.
BC130028 mRNA. Translation: AAI30029.1.
AH011240 Genomic DNA. Translation: AAL39096.1.
CCDSiCCDS38683.1.
RefSeqiNP_084263.2. NM_029987.2.
UniGeneiMm.131708.

Genome annotation databases

EnsembliENSMUST00000029824; ENSMUSP00000029824; ENSMUSG00000028174.
GeneIDi19892.
KEGGimmu:19892.
UCSCiuc008rwb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF410461 mRNA. Translation: AAL01119.1 .
AC163272 Genomic DNA. No translation available.
CH466532 Genomic DNA. Translation: EDL11842.1 .
BC130028 mRNA. Translation: AAI30029.1 .
AH011240 Genomic DNA. Translation: AAL39096.1 .
CCDSi CCDS38683.1.
RefSeqi NP_084263.2. NM_029987.2.
UniGenei Mm.131708.

3D structure databases

ProteinModelPortali Q91ZQ5.
SMRi Q91ZQ5. Positions 4-533.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000029824.

PTM databases

PhosphoSitei Q91ZQ5.

Proteomic databases

PRIDEi Q91ZQ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029824 ; ENSMUSP00000029824 ; ENSMUSG00000028174 .
GeneIDi 19892.
KEGGi mmu:19892.
UCSCi uc008rwb.1. mouse.

Organism-specific databases

CTDi 6121.
MGIi MGI:98001. Rpe65.

Phylogenomic databases

eggNOGi COG3670.
GeneTreei ENSGT00500000044783.
HOGENOMi HOG000232156.
HOVERGENi HBG050679.
InParanoidi Q91ZQ5.
KOi K11158.
OMAi TIREPSV.
TreeFami TF314019.

Enzyme and pathway databases

Reactomei REACT_188277. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

NextBioi 297412.
PROi Q91ZQ5.
SOURCEi Search...

Gene expression databases

CleanExi MM_RPE65.
Genevestigatori Q91ZQ5.

Family and domain databases

InterProi IPR004294. Carotenoid_Oase.
[Graphical view ]
PANTHERi PTHR10543. PTHR10543. 1 hit.
Pfami PF03055. RPE65. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Retinal degeneration 12 (rd12): a new, spontaneously arising mouse model for human Leber congenital amaurosis (LCA)."
    Pang J.J., Chang B., Hawes N.L., Hurd R.E., Davisson M.T., Li J., Noorwez S.M., Malhotra R., McDowell J.H., Kaushal S., Hauswirth W.W., Nusinowitz S., Thompson D.A., Heckenlively J.R.
    Mol. Vis. 11:152-162(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Retina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-450.
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Sequence and structure of the mouse gene for RPE65."
    Boulanger A., Liu S., Yu S., Redmond T.M.
    Mol. Vis. 7:283-287(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-483.
    Strain: 129/Sv.
  6. "The Rpe65 Leu450Met variation increases retinal resistance against light-induced degeneration by slowing rhodopsin regeneration."
    Wenzel A., Reme C.E., Williams T.P., Hafezi F., Grimm C.
    J. Neurosci. 21:53-58(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-450.
  7. "Fatty acid transport protein 4 (FATP4) prevents light-induced degeneration of cone and rod photoreceptors by inhibiting RPE65 isomerase."
    Li S., Lee J., Zhou Y., Gordon W.C., Hill J.M., Bazan N.G., Miner J.H., Jin M.
    J. Neurosci. 33:3178-3189(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRPE65_MOUSE
AccessioniPrimary (citable) accession number: Q91ZQ5
Secondary accession number(s): A1L3D1
, E9QNS6, H9KUX9, Q8VHP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 11, 2013
Last modified: September 3, 2014
This is version 87 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi