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Q91ZQ5

- RPE65_MOUSE

UniProt

Q91ZQ5 - RPE65_MOUSE

Protein

Retinoid isomerohydrolase

Gene

Rpe65

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 4 (11 Dec 2013)
      Previous versions | rss
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    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; catalyticBy similarity
    Metal bindingi241 – 2411Iron; catalyticBy similarity
    Metal bindingi313 – 3131Iron; catalyticBy similarity
    Metal bindingi527 – 5271Iron; catalyticBy 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. retinal metabolic process Source: MGI
    6. retina morphogenesis in camera-type eye Source: MGI
    7. visual perception Source: MGI

    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 By similarity; 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.By similarity

    GO - Cellular componenti

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

    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 – 11RemovedBy similarity
    Chaini2 – 533532Retinoid isomerohydrolasePRO_0000143944Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei101 – 1011PhosphothreonineBy similarity
    Modified residuei105 – 1051PhosphothreonineBy similarity
    Lipidationi112 – 1121S-palmitoyl cysteine; in membrane formBy similarity
    Modified residuei113 – 1131N6-acetyllysineBy similarity
    Modified residuei117 – 1171PhosphoserineBy similarity
    Lipidationi231 – 2311S-palmitoyl cysteine; in membrane formBy similarity
    Lipidationi329 – 3291S-palmitoyl cysteine; in membrane formBy similarity
    Lipidationi330 – 3301S-palmitoyl cysteine; in membrane formBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the carotenoid oxygenase family.Curated

    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

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    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

    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: October 1, 2014
    This is version 88 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