ID  P40345;
PN  Phospholipid:diacylglycerol acyltransferase;
GN  LRO1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22446555, ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}; Single-pass type II membrane protein {ECO:0000269|PubMed:22446555}. Nucleus inner membrane {ECO:0000269|PubMed:31422915}; Single-pass type II membrane protein {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum (PubMed:22454508, PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane that associates with the nucleolus upon nutrient starvation (PubMed:31422915). {ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}.
DR  UNIPROT: P40345;
DR  UNIPROT: D6W1I3;
DR  Pfam: PF02450;
DE  Function: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid (PubMed:10747858, PubMed:10829075, PubMed:32349126). The preferred acyl donors are phosphatidylethanolamine (PE) and phosphatidylcholine (PC). Also capable of using broad acyl donors such as phosphatidic acid (PA), phosphatidylserine (PS), phosphatidylglycerol (PG) and phosphatidylinositol (PI), as well as monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), and acyl-CoA, and it is more likely to use unsaturated acyl donors. As acyl acceptors, it prefers 1,2- over 1,3-diacylglycerol (DAG). Additionally, has esterification activity that can utilize methanol as acyl acceptor to generate fatty acid methyl esters (FAME) (PubMed:30706417). Can also utilize ceramide instead of DAG, acylating the ceramides by attaching a fatty acid to the hydroxy group on the first carbon atom of the long-chain base to produce 1-O-acylceramides (PubMed:22738231). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane upon nutrient starvation, where it provides a site of TAG synthesis, which is coupled with nuclear membrane remodeling (PubMed:31422915). {ECO:0000269|PubMed:10747858, ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:22738231, ECO:0000269|PubMed:30706417, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}.
DE  Reference Proteome: Yes;
DE  Interaction: P53919; IntAct: EBI-858436; Score: 0.00
DE  Interaction: P25294; IntAct: EBI-3661091; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3672140; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3690189; Score: 0.35
DE  Interaction: Q04675; IntAct: EBI-16281991; Score: 0.35
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005637;
GO  GO:0097038;
GO  GO:0003824;
GO  GO:0008374;
GO  GO:0046027;
GO  GO:0006672;
GO  GO:0006629;
GO  GO:0019915;
GO  GO:0055091;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGTLFRRNVQNQKSDSDENNKGGSVHNKRESRNHIHHQQGLGHKRRRGISGSAKRNERGKDFDRKRDGNGRKRWRDSRRL
SQ  IFILGAFLGVLLPFSFGAYHVHNSDSDLFDNFVNFDSLKVYLDDWKDVLPQGISSFIDDIQAGNYSTSSLDDLSENFAVG
SQ  KQLLRDYNIEAKHPVVMVPGVISTGIESWGVIGDDECDSSAHFRKRLWGSFYMLRTMVMDKVCWLKHVMLDPETGLDPPN
SQ  FTLRAAQGFESTDYFIAGYWIWNKVFQNLGVIGYEPNKMTSAAYDWRLAYLDLERRDRYFTKLKEQIELFHQLSGEKVCL
SQ  IGHSMGSQIIFYFMKWVEAEGPLYGNGGRGWVNEHIDSFINAAGTLLGAPKAVPALISGEMKDTIQLNTLAMYGLEKFFS
SQ  RIERVKMLQTWGGIPSMLPKGEEVIWGDMKSSSEDALNNNTDTYGNFIRFERNTSDAFNKNLTMKDAINMTLSISPEWLQ
SQ  RRVHEQYSFGYSKNEEELRKNELHHKHWSNPMEVPLPEAPHMKIYCIYGVNNPTERAYVYKEEDDSSALNLTIDYESKQP
SQ  VFLTEGDGTVPLVAHSMCHKWAQGASPYNPAGINVTIVEMKHQPDRFDIRGGAKSAEHVDILGSAELNDYILKIASGNGD
SQ  LVEPRQLSNLSQWVSQMPFPM
//