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BOVIN:RPE65

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Species (Taxon ID) Bos taurus (Bovine). (9913)
Gene Name(s) RPE65
Protein Name(s) Retinoid isomerohydrolase

All-trans-retinyl-palmitate hydrolase Retinal pigment epithelium-specific 65 kDa protein Retinol isomerase

External Links
UniProt Q28175
EMBL L11356
X66277
PIR A47143
RefSeq NP_776878.1
UniGene Bt.108
PDB 3FSN
3KVC
4F2Z
4F30
4F3A
4F3D
PDBsum 3FSN
3KVC
4F2Z
4F30
4F3A
4F3D
ProteinModelPortal Q28175
DIP DIP-48993N
PRIDE Q28175
Ensembl ENSBTAT00000043702
GeneID 282043
KEGG bta:282043
CTD 6121
eggNOG COG3670
GeneTree ENSGT00500000044783
HOGENOM HOG000232156
HOVERGEN HBG050679
InParanoid Q28175
KO K11158
OrthoDB EOG7353WB
TreeFam TF314019
BRENDA 5.2.1.7
Reactome REACT_211834
EvolutionaryTrace Q28175
NextBio 20805904
Proteomes UP000009136
GO GO:0005783
GO:0031090
GO:0005886
GO:0052885
GO:0052884
GO:0046872
GO:0004744
GO:0071257
GO:0050908
GO:0008286
GO:0007468
GO:0001895
GO:0060042
GO:0042574
InterPro IPR004294
PANTHER PTHR10543
Pfam PF03055

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004744

retinal isomerase activity

PMID:16096063[1]

ECO:0000314

F

Figure 4,5. Fig. 4 shows the absence of isomerase activity activity in pRPE65-transerase 293T-RC cell homogenates using atROL as substrate and the presence of activity in the same cells using atRP as substrate. pRPE65-transfected likes do show isomerase activity.

complete
CACAO 4450

enables

GO:0052884

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

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q16518

F

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q16518

C

Seeded From UniProt

complete

involved_in

GO:1901827

zeaxanthin biosynthetic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q16518

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:19892706[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0052885

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

PMID:19892706[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:1901612

cardiolipin binding

PMID:19892706[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0031210

phosphatidylcholine binding

PMID:19892706[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001786

phosphatidylserine binding

PMID:19892706[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004744

retinal isomerase activity

PMID:16096063[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:1901827

zeaxanthin biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002576077
UniProtKB:Q16518
UniProtKB:Q9YGX2

P

Seeded From UniProt

complete

enables

GO:0052885

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

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002576077
RGD:621396
UniProtKB:Q28175
UniProtKB:Q9YGX2

F

Seeded From UniProt

complete

enables

GO:0050251

retinol isomerase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002576077
UniProtKB:A9C3R8

F

Seeded From UniProt

complete

involved_in

GO:0042574

retinal metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0002937
MGI:MGI:1926923
MGI:MGI:2177469
MGI:MGI:98001
PANTHER:PTN000057192
RGD:621396
UniProtKB:Q9I993

P

Seeded From UniProt

complete

enables

GO:0004744

retinal isomerase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0002937
MGI:MGI:98001
PANTHER:PTN000830314
UniProtKB:Q28175

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23012475[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q28175

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19805034[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q28175

F

Seeded From UniProt

complete

involved_in

GO:0042572

retinol metabolic process

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0052884

P

Seeded From UniProt

complete

involved_in

GO:0042572

retinol metabolic process

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0052885

P

Seeded From UniProt

complete

involved_in

GO:0042572

retinol metabolic process

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0052885

P

Seeded From UniProt

complete

involved_in

GO:0042572

retinol metabolic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0052884

P

Seeded From UniProt

complete

enables

GO:0016702

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004294

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004294

P

Seeded From UniProt

complete

enables

GO:0052885

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

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.64

F

Seeded From UniProt

complete

enables

GO:0052884

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

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.64

F

Seeded From UniProt

complete

involved_in

GO:0050896

response to stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0716

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

involved_in

GO:0007601

visual perception

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0844

P

Seeded From UniProt

complete

part_of

GO:0043231

intracellular membrane-bounded organelle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0492

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0031090

organelle membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0165

C

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Jin, M et al. (2005) Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium. Cell 122 449-59 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 Yuan, Q et al. (2010) Rpe65 isomerase associates with membranes through an electrostatic interaction with acidic phospholipid headgroups. J. Biol. Chem. 285 988-99 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Kiser, PD et al. (2012) Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis. Proc. Natl. Acad. Sci. U.S.A. 109 E2747-56 PubMed GONUTS page
  5. ↑ Kiser, PD et al. (2009) Crystal structure of native RPE65, the retinoid isomerase of the visual cycle. Proc. Natl. Acad. Sci. U.S.A. 106 17325-30 PubMed GONUTS page
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