Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods
Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1).
-
RDH11 (RalR1/PSDR1) is an NADP-preferring retinoid oxidoreductase with no steroid activity; ~50-fold more efficient at reducing all-trans-retinal than oxidizing all-trans-retinol, and localizes to the ER.
"The enzyme is approximately 50-fold more efficient for the reduction of all-trans-retinal than for the oxidation of all-trans-retinol."
Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina.
-
RDH11 is one of a novel subfamily (RDH11-14) of dual-specificity retinol dehydrogenases metabolizing all-trans- and cis-retinols with C15 pro-R specificity, positioned in the RPE for the visual retinoid cycle.
"display dual-substrate specificity, uniquely metabolizing all-trans- and cis-retinols with C(15) pro-R specificity"
Characterization of mouse short-chain aldehyde reductase (SCALD), an enzyme regulated by sterol regulatory element-binding proteins.
-
The mouse ortholog SCALD is an NADPH-dependent reductase of short-chain aldehydes and retinaldehydes; it is the mouse ortholog of human PSDR1/RalR1/RDH11. Human RDH11 differs in having little activity toward toxic lipid-peroxidation aldehydes.
"SCALD appears to be the mouse ortholog of the human protein"
Architecture of the human interactome defines protein communities and disease networks.
The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism.
-
SELENOF physically interacts with RDH11 and inhibits its NADPH-dependent reduction of all-trans-retinaldehyde to all-trans-retinol, implicating this interaction in regulation of vitamin A metabolism.
"SELENOF interacts with RDH11 and blocks its enzyme activity to reduce all-trans-retinaldehyde."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
-
Proteome-scale AP-MS interactome (BioPlex 3.0); source of a bare protein-binding IPI for RDH11 (WITH/FROM UBAC1).
"118,162 interactions among 14,586 proteins"
The canonical retinoid cycle in rods (twilight vision)
RDH5,RDH11 oxidise 11cROL to 11cRAL
RDH11,14,DHRS3,DRHS4 reduce atRAL to atROL
RDH10,11 oxidise 11cROL to 11cRAL
RDH11 reduces RBP2:atRAL to RBP2:atROL
Retinoid metabolism and transport