Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
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
Combined Automated Annotation using Multiple IEA Methods
Lecithin retinol acyltransferase contains cysteine residues essential for catalysis.
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LRAT is a membrane-bound thiol acyltransferase that transfers an acyl group from the sn-1 position of lecithin to retinol to form retinyl esters; site-directed mutagenesis identifies Cys161 as the essential catalytic nucleophile (C161A/C168A inactive), consistent with an acyl-thioester intermediate.
"an acyl group from the sn-1 position of lecithin to vitamin A to generate"
Molecular and biochemical characterization of lecithin retinol acyltransferase.
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Molecular cloning and biochemical characterization of human LRAT (230-aa, ~25 kDa protein); LRAT-transfected HEK-293 cells convert all-trans-retinol into all-trans-retinyl palmitate, and the transcript is expressed in human retinal pigment epithelium and other vitamin A-processing tissues.
"The enzyme responsible for conversion of all-trans-retinol into retinyl esters,"
A reference map of the human binary protein interactome.
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HuRI systematic binary interactome map; the source of the three IntAct "protein binding" (GO:0005515) IPI annotations for LRAT (interactors BLCAP, HSD17B13, TMX2). These are high-throughput binary hits without LRAT-specific functional follow-up.
"reference interactome map of human binary protein interactions, or 'HuRI'."
Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy.
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Biallelic LRAT mutations (including the S175R loss-of-function variant) cause early-onset severe retinal dystrophy / Leber congenital amaurosis (LCA14), establishing LRAT's essential role in vision.
"Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy."
LRAT esterifies RBP1:atROL and FACYLs to atREs
LRAT esterifies RBP1:atROL and FACYLs to atREs
The canonical retinoid cycle in rods (twilight vision)
Defective LRAT does not esterify RBP1:atROL and FACYLs to atREs
LRAT esterifies RBP2:atROL and FACYLs to atREs
Retinoid metabolism and transport
UniProt entry O95237 (LRAT_HUMAN), Lecithin retinol acyltransferase
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LRAT transfers the acyl group from the sn-1 position of phosphatidylcholine (lecithin) to all-trans-retinol to produce all-trans-retinyl esters (the vitamin A storage form and RPE65 substrate); it is an endoplasmic reticulum membrane, single-pass membrane protein, and its loss of function causes Leber congenital amaurosis 14 (LCA14).
"Transfers the acyl group from the sn-1 position of"