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Q91ZQ5 (RPE65_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Rpe65
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7

Catalytic activity

An all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid. Ref.7

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subunit structure

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

Subcellular location

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.

Tissue specificity

Retinal pigment epithelium specific. Ref.1 Ref.7

Post-translational modification

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.

Involvement in disease

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

Sequence similarities

Belongs to the carotenoid oxygenase family.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Microsome
   DiseaseDisease mutation
   LigandIron
Metal-binding
   Molecular functionHydrolase
Isomerase
   PTMAcetylation
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to electrical stimulus

Inferred from mutant phenotype PubMed 21052544. Source: MGI

insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 17272282. Source: MGI

regulation of rhodopsin gene expression

Inferred from mutant phenotype PubMed 11897783. Source: MGI

retina development in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

retina morphogenesis in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

retinal metabolic process

Inferred from mutant phenotype PubMed 11897783. Source: MGI

visual perception

Inferred from mutant phenotype PubMed 11897783. Source: MGI

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

organelle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionall-trans-retinyl-ester hydrolase, 11-cis retinol forming activity

Inferred from electronic annotation. Source: UniProtKB-EC

all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

retinal isomerase activity

Inferred from mutant phenotype PubMed 18195010. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 533532Retinoid isomerohydrolase
PRO_0000143944

Sites

Metal binding1801Iron; catalytic By similarity
Metal binding2411Iron; catalytic By similarity
Metal binding3131Iron; catalytic By similarity
Metal binding5271Iron; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue1011Phosphothreonine By similarity
Modified residue1051Phosphothreonine By similarity
Modified residue1131N6-acetyllysine By similarity
Modified residue1171Phosphoserine By similarity
Lipidation1121S-palmitoyl cysteine; in membrane form By similarity
Lipidation2311S-palmitoyl cysteine; in membrane form By similarity
Lipidation3291S-palmitoyl cysteine; in membrane form By similarity
Lipidation3301S-palmitoyl cysteine; in membrane form By similarity

Natural variations

Natural variant4501M → L Increased light damage susceptibility. Ref.2 Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q91ZQ5 [UniParc].

Last modified December 11, 2013. Version 4.
Checksum: BBDA3EBDF5B7A5E2

FASTA53361,085
        10         20         30         40         50         60 
MSIQIEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF EVGSEPFYHL 

        70         80         90        100        110        120 
FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI TEFGTCAFPD PCKNIFSRFF 

       130        140        150        160        170        180 
SYFKGVEVTD NALVNIYPVG EDYYACTETN FITKINPETL ETIKQVDLCN YISVNGATAH 

       190        200        210        220        230        240 
PHIESDGTVY NIGNCFGKNF TVAYNIIKIP PLKADKEDPI NKSEVVVQFP CSDRFKPSYV 

       250        260        270        280        290        300 
HSFGLTPNYI VFVETPVKIN LFKFLSSWSL WGANYMDCFE SNESMGVWLH VADKKRRKYF 

       310        320        330        340        350        360 
NNKYRTSPFN LFHHINTYED NGFLIVDLCC WKGFEFVYNY LYLANLRENW EEVKRNAMKA 

       370        380        390        400        410        420 
PQPEVRRYVL PLTIDKVDTG RNLVTLPHTT ATATLRSDET IWLEPEVLFS GPRQAFEFPQ 

       430        440        450        460        470        480 
INYQKFGGKP YTYAYGLGLN HFVPDKLCKM NVKTKEIWMW QEPDSYPSEP IFVSQPDALE 

       490        500        510        520        530 
EDDGVVLSVV VSPGAGQKPA YLLVLNAKDL SEIARAEVET NIPVTFHGLF KRS 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS38683.1.
RefSeqNP_084263.2. NM_029987.2.
UniGeneMm.131708.

3D structure databases

ProteinModelPortalQ91ZQ5.
SMRQ91ZQ5. Positions 4-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000029824.

PTM databases

PhosphoSiteQ91ZQ5.

Proteomic databases

PRIDEQ91ZQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029824; ENSMUSP00000029824; ENSMUSG00000028174.
GeneID19892.
KEGGmmu:19892.
UCSCuc008rwb.1. mouse.

Organism-specific databases

CTD6121.
MGIMGI:98001. Rpe65.

Phylogenomic databases

eggNOGCOG3670.
GeneTreeENSGT00500000044783.
HOGENOMHOG000232156.
HOVERGENHBG050679.
InParanoidQ91ZQ5.
KOK11158.
OMATIREPSV.
TreeFamTF314019.

Gene expression databases

CleanExMM_RPE65.
GenevestigatorQ91ZQ5.

Family and domain databases

InterProIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERPTHR10543. PTHR10543. 1 hit.
PfamPF03055. RPE65. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio297412.
PROQ91ZQ5.
SOURCESearch...

Entry information

Entry nameRPE65_MOUSE
AccessionPrimary (citable) accession number: Q91ZQ5
Secondary accession number(s): A1L3D1 expand/collapse secondary AC list , E9QNS6, H9KUX9, Q8VHP2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 11, 2013
Last modified: July 9, 2014
This is version 86 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot