2.3.1.135 endoplasmic reticulum before initiation of retinyl ester biosynthesis, LRAT distributes throughout the endoplasmic reticulum, and Crpb1 localizes with mitochondria associated membranes, surrounded by LRAT. Upon initiating retinyl ester biosynthesis in cells, Crpb1 remains with MAM, and both Crbp1 and MAM re-localize with LRAT. LRAT formed rings around the growing lipid droplets 5783 718992 2.3.1.135 endoplasmic reticulum membrane LRAT is localized to the membrane of the LRAT is localized to the membrane of the endoplasmic reticulum. Single membrane-spanning protein with an N-terminal domain that faces the cytoplasm 5789 674832 2.3.1.135 endoplasmic reticulum membrane LRATis a single membrane-spanning protein with an N-terminal domain that faces the cytoplasm, C-terminal luminal orientation, membrane topology, overview 5789 674832 2.3.1.135 lipid droplet upon initiating retinyl ester biosynthesis in cells, Crpb1 remains with MAM, and both Crbp1 and MAM re-localize with LRAT. LRAT formed rings around the growing lipid droplets. LRAT-containing rings colocalize with the lipid-droplet surface proteins, desnutrin/adipose triglyceride lipase and perilipin 2. Colocalization with lipid droplets requires the 38 N-terminal amino acid residues of LRAT, and specifically K36 and R38. Formation of rings around the growing lipid droplets does not require functional microtubules 5811 718992 2.3.1.135 membrane - 16020 658661, 658662, 672075 2.3.1.135 membrane boound 16020 719417 2.3.1.135 membrane bound, membrane topology model of LRAT using I-TASSER, membrane interaction probes of LRAT and truncated LRAT with phospholipid monolayers, circular dichroism, overview 16020 720353 2.3.1.135 membrane integral 16020 658001 2.3.1.135 membrane membrane-associated protein 16020 685367 2.3.1.135 microsome - - 487491, 638608, 638613, 638625, 658662, 674487, 758200