Literature summary for 1.1.1.315 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.

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Protein Variants

Protein Variants	Comment	Organism
DELTA289-318	results show that the N-terminal hydrophobic domain is a membrane-anchoring domain	Bos taurus
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

Localization	Comment	Organism	GeneOntology No.	Textmining
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	-

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	Q27979	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
retinal pigment epithelial cell	-	Bos taurus	-

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Release 2023.1 (January 2023)