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Protein

Retinoid isomerohydrolase

Gene

RPE65

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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.3 Publications

Catalytic activityi

An all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid.3 Publications

Cofactori

Fe2+2 PublicationsNote: Binds 1 Fe2+ ion per subunit.2 Publications

Kineticsi

  1. KM=7.1 µM for all-trans-retinyl palmitate1 Publication
  1. Vmax=26.1 pmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi180Iron; catalytic1
Metal bindingi241Iron; catalytic1
Metal bindingi313Iron; catalytic1
Metal bindingi527Iron; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.64. 908.
SABIO-RKQ28175.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm
  • Cell membrane; Lipid-anchor
  • Microsome membrane

  • Note: Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells (By similarity). Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated.By similarity

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-KW
  • membrane Source: AgBase
  • organelle membrane Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001439402 – 533Retinoid isomerohydrolaseAdd BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei101PhosphothreonineBy similarity1
Modified residuei105PhosphothreonineBy similarity1
Lipidationi112S-palmitoyl cysteine; in membrane form1 Publication1
Modified residuei113N6-acetyllysineBy similarity1
Modified residuei117PhosphoserineBy similarity1
Lipidationi231S-palmitoyl cysteine; in membrane form1 Publication1
Lipidationi329S-palmitoyl cysteine; in membrane form1 Publication1
Lipidationi330S-palmitoyl cysteine; in membrane form1 Publication1

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).3 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ28175.
PRIDEiQ28175.

PTM databases

SwissPalmiQ28175.

Expressioni

Tissue specificityi

Retinal pigment epithelium specific.2 Publications

Gene expression databases

BgeeiENSBTAG00000020494.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48993N.
STRINGi9913.ENSBTAP00000041254.

Structurei

Secondary structure

1533
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 16Combined sources6
Beta strandi29 – 32Combined sources4
Beta strandi40 – 49Combined sources10
Turni60 – 62Combined sources3
Beta strandi63 – 73Combined sources11
Beta strandi76 – 83Combined sources8
Helixi87 – 95Combined sources9
Beta strandi134 – 139Combined sources6
Beta strandi142 – 146Combined sources5
Beta strandi148 – 155Combined sources8
Turni157 – 159Combined sources3
Beta strandi162 – 167Combined sources6
Helixi168 – 170Combined sources3
Beta strandi189 – 195Combined sources7
Helixi198 – 200Combined sources3
Beta strandi203 – 209Combined sources7
Helixi219 – 222Combined sources4
Beta strandi224 – 230Combined sources7
Beta strandi232 – 235Combined sources4
Beta strandi247 – 254Combined sources8
Beta strandi256 – 259Combined sources4
Helixi261 – 264Combined sources4
Helixi268 – 271Combined sources4
Helixi276 – 278Combined sources3
Beta strandi279 – 281Combined sources3
Beta strandi283 – 285Combined sources3
Beta strandi287 – 293Combined sources7
Turni294 – 297Combined sources4
Beta strandi298 – 306Combined sources9
Beta strandi309 – 320Combined sources12
Beta strandi323 – 335Combined sources13
Helixi337 – 340Combined sources4
Helixi343 – 346Combined sources4
Helixi350 – 356Combined sources7
Turni357 – 359Combined sources3
Beta strandi362 – 372Combined sources11
Helixi376 – 378Combined sources3
Beta strandi392 – 395Combined sources4
Beta strandi399 – 404Combined sources6
Beta strandi406 – 409Combined sources4
Beta strandi414 – 420Combined sources7
Helixi423 – 426Combined sources4
Beta strandi433 – 440Combined sources8
Beta strandi443 – 451Combined sources9
Turni452 – 454Combined sources3
Beta strandi457 – 460Combined sources4
Beta strandi471 – 474Combined sources4
Beta strandi480 – 482Combined sources3
Beta strandi484 – 491Combined sources8
Beta strandi494 – 497Combined sources4
Beta strandi499 – 506Combined sources8
Turni507 – 509Combined sources3
Beta strandi512 – 520Combined sources9
Beta strandi527 – 532Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FSNX-ray2.14A/B1-533[»]
3KVCX-ray1.90A/B1-533[»]
4F2ZX-ray3.00A/E1-533[»]
4F30X-ray3.15A1-533[»]
4F3AX-ray2.60A1-533[»]
4F3DX-ray2.50A/B1-533[»]
4RSCX-ray1.80A/B1-533[»]
4RSEX-ray2.39A/B2-533[»]
4RYXX-ray2.00A1-533[»]
4RYYX-ray2.30A/B2-533[»]
4RYZX-ray2.50A/B2-533[»]
4ZHKX-ray2.09A/B2-533[»]
ProteinModelPortaliQ28175.
SMRiQ28175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28175.

Family & Domainsi

Sequence similaritiesi

Belongs to the carotenoid oxygenase family.Curated

Phylogenomic databases

eggNOGiKOG1285. Eukaryota.
COG3670. LUCA.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ28175.
KOiK11158.
TreeFamiTF314019.

Family and domain databases

InterProiIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERiPTHR10543. PTHR10543. 2 hits.
PfamiPF03055. RPE65. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q28175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQVEHPAG GYKKLFETVE ELSSPLTAHV TGRIPLWLTG SLLRCGPGLF
60 70 80 90 100
EVGSEPFYHL FDGQALLHKF DFKEGHVTYH RRFIRTDAYV RAMTEKRIVI
110 120 130 140 150
TEFGTCAFPD PCKNIFSRFF SYFRGVEVTD NALVNIYPVG EDYYACTETN
160 170 180 190 200
FITKVNPETL ETIKQVDLCN YVSVNGATAH PHIENDGTVY NIGNCFGKNF
210 220 230 240 250
SIAYNIVKIP PLQADKEDPI SKSEIVVQFP CSDRFKPSYV HSFGLTPNYI
260 270 280 290 300
VFVETPVKIN LFKFLSSWSL WGANYMDCFE SNETMGVWLH IADKKRKKYI
310 320 330 340 350
NNKYRTSPFN LFHHINTYED HEFLIVDLCC WKGFEFVYNY SYLANLRENW
360 370 380 390 400
EEVKKNARKA PQPEVRRYVL PLNIDKADTG KNLVTLPNTT ATAILCSDET
410 420 430 440 450
IWLEPEVLFS GPRQAFEFPQ INYQKYGGKP YTYAYGLGLN HFVPDRLCKL
460 470 480 490 500
NVKTKETWVW QEPDSYPSEP IFVSHPDALE EDDGVVLSVV VSPGAGQKPA
510 520 530
YLLILNAKDL SEVARAEVEI NIPVTFHGLF KKS
Length:533
Mass (Da):60,944
Last modified:January 23, 2007 - v3
Checksum:i28B5E4B15ACD8087
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti341S → L in CAA46988 (PubMed:8397208).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11356 mRNA. Translation: AAC37306.1.
X66277 mRNA. Translation: CAA46988.1.
PIRiA47143.
RefSeqiNP_776878.1. NM_174453.2.
UniGeneiBt.108.

Genome annotation databases

GeneIDi282043.
KEGGibta:282043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11356 mRNA. Translation: AAC37306.1.
X66277 mRNA. Translation: CAA46988.1.
PIRiA47143.
RefSeqiNP_776878.1. NM_174453.2.
UniGeneiBt.108.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FSNX-ray2.14A/B1-533[»]
3KVCX-ray1.90A/B1-533[»]
4F2ZX-ray3.00A/E1-533[»]
4F30X-ray3.15A1-533[»]
4F3AX-ray2.60A1-533[»]
4F3DX-ray2.50A/B1-533[»]
4RSCX-ray1.80A/B1-533[»]
4RSEX-ray2.39A/B2-533[»]
4RYXX-ray2.00A1-533[»]
4RYYX-ray2.30A/B2-533[»]
4RYZX-ray2.50A/B2-533[»]
4ZHKX-ray2.09A/B2-533[»]
ProteinModelPortaliQ28175.
SMRiQ28175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48993N.
STRINGi9913.ENSBTAP00000041254.

PTM databases

SwissPalmiQ28175.

Proteomic databases

PaxDbiQ28175.
PRIDEiQ28175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282043.
KEGGibta:282043.

Organism-specific databases

CTDi6121.

Phylogenomic databases

eggNOGiKOG1285. Eukaryota.
COG3670. LUCA.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ28175.
KOiK11158.
TreeFamiTF314019.

Enzyme and pathway databases

BRENDAi3.1.1.64. 908.
SABIO-RKQ28175.

Miscellaneous databases

EvolutionaryTraceiQ28175.

Gene expression databases

BgeeiENSBTAG00000020494.

Family and domain databases

InterProiIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERiPTHR10543. PTHR10543. 2 hits.
PfamiPF03055. RPE65. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPE65_BOVIN
AccessioniPrimary (citable) accession number: Q28175
Secondary accession number(s): Q05661
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.