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Literature summary extracted from

  • Simon, A.; Romert, A.; Gustafson, A.; McCaffery, J.; Eriksson, U.
    Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde (1999), J. Cell Sci., 112, 549-558.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.315 DELTA289-318 results show that the N-terminal hydrophobic domain is a membrane-anchoring domain Bos taurus
1.1.1.315 additional information introduction of a glycosylation site in mutant 11-cis RDH GM71-73 at positions 71-73, residues NIS. Construction of a mutant protein, 11-cis RDH-HA, with a C-terminal extension of 12 amino acid residues consisting of the hemagglutinin antigenic epitope and a glycosylation site. Results suggest that residues 289-310 of 11-cis RDH are a transmembrane domain and that amino acid residues 311-318 are located in the cytosol Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.315 endoplasmic reticulum the majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells. The enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes Bos taurus 5783
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Organism

EC Number Organism UniProt Comment Textmining
1.1.1.315 Bos taurus Q27979
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.315 retinal pigment epithelial cell
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Bos taurus
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