ID PDAT_YEAST Reviewed; 661 AA.
AC P40345; D6W1I3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Phospholipid:diacylglycerol acyltransferase {ECO:0000305};
DE Short=PDAT;
DE EC=2.3.1.158 {ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386, ECO:0000269|PubMed:30706417};
DE AltName: Full=LCAT-related open reading frame 1 {ECO:0000303|PubMed:10747858};
DE AltName: Full=Lecithin cholesterol acyl transferase-related open reading frame 1 {ECO:0000303|PubMed:10747858};
DE AltName: Full=Triacylglycerol synthase;
DE Short=TAG synthase;
GN Name=LRO1 {ECO:0000303|PubMed:10747858}; OrderedLocusNames=YNR008W;
GN ORFNames=N2042;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=10747858; DOI=10.1074/jbc.c000144200;
RA Oelkers P., Tinkelenberg A., Erdeniz N., Cromley D., Billheimer J.T.,
RA Sturley S.L.;
RT "A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol
RT esterification in yeast.";
RL J. Biol. Chem. 275:15609-15612(2000).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10829075; DOI=10.1073/pnas.120067297;
RA Dahlqvist A., Stahl U., Lenman M., Banas A., Lee M., Sandager L., Ronne H.,
RA Stymne S.;
RT "Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the
RT acyl-CoA-independent formation of triacylglycerol in yeast and plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6487-6492(2000).
RN [6]
RP CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RX PubMed=18037386; DOI=10.1016/j.bbalip.2007.10.007;
RA Ghosal A., Banas A., Staahl U., Dahlqvist A., Lindqvist Y., Stymne S.;
RT "Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase
RT (PDAT) devoid of its membrane anchor region is a soluble and active enzyme
RT retaining its substrate specificities.";
RL Biochim. Biophys. Acta 1771:1457-1463(2007).
RN [7]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=22446555; DOI=10.4161/cib.17830;
RA Choudhary V., Jacquier N., Schneiter R.;
RT "The topology of the triacylglycerol synthesizing enzyme Lro1 indicates
RT that neutral lipids can be produced within the luminal compartment of the
RT endoplasmatic reticulum: Implications for the biogenesis of lipid
RT droplets.";
RL Commun. Integr. Biol. 4:781-784(2011).
RN [8]
RP FUNCTION.
RX PubMed=22738231; DOI=10.1042/bj20120712;
RA Voynova N.S., Vionnet C., Ejsing C.S., Conzelmann A.;
RT "A novel pathway of ceramide metabolism in Saccharomyces cerevisiae.";
RL Biochem. J. 447:103-114(2012).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=22454508; DOI=10.1242/jcs.100230;
RA Wang C.W., Lee S.C.;
RT "The ubiquitin-like (UBX)-domain-containing protein Ubx2/Ubxd8 regulates
RT lipid droplet homeostasis.";
RL J. Cell Sci. 125:2930-2939(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND GLYCOSYLATION AT
RP ASN-453; ASN-461; ASN-469 AND ASN-594.
RX PubMed=30706417; DOI=10.1007/s12010-019-02954-x;
RA Feng Y., Zhang Y., Ding W., Wu P., Cao X., Xue S.;
RT "Expanding of phospholipid:diacylglycerol acyltransferase (PDAT) from
RT Saccharomyces cerevisiae as multifunctional biocatalyst with broad acyl
RT donor/acceptor selectivity.";
RL Appl. Biochem. Biotechnol. 188:824-835(2019).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-324.
RX PubMed=31422915; DOI=10.1016/j.devcel.2019.07.009;
RA Barbosa A.D., Lim K., Mari M., Edgar J.R., Gal L., Sterk P., Jenkins B.J.,
RA Koulman A., Savage D.B., Schuldiner M., Reggiori F., Wigge P.A.,
RA Siniossoglou S.;
RT "Compartmentalized synthesis of triacylglycerol at the inner nuclear
RT membrane regulates nuclear organization.";
RL Dev. Cell 50:755-766.e6(2019).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-618.
RX PubMed=32349126; DOI=10.1083/jcb.201910177;
RA Choudhary V., El Atab O., Mizzon G., Prinz W.A., Schneiter R.;
RT "Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid
RT droplet biogenesis.";
RL J. Cell Biol. 219:0-0(2020).
CC -!- FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA
CC independent pathway. The enzyme specifically transfers acyl groups from
CC the sn-2 position of a phospholipid to diacylglycerol (DAG), thus
CC forming an sn-1-lysophospholipid (PubMed:10747858, PubMed:10829075,
CC PubMed:32349126). The preferred acyl donors are
CC phosphatidylethanolamine (PE) and phosphatidylcholine (PC). Also
CC capable of using broad acyl donors such as phosphatidic acid (PA),
CC phosphatidylserine (PS), phosphatidylglycerol (PG) and
CC phosphatidylinositol (PI), as well as monogalactosyldiacylglycerol
CC (MGDG), digalactosyldiacylglycerol (DGDG), and acyl-CoA, and it is more
CC likely to use unsaturated acyl donors. As acyl acceptors, it prefers
CC 1,2- over 1,3-diacylglycerol (DAG). Additionally, has esterification
CC activity that can utilize methanol as acyl acceptor to generate fatty
CC acid methyl esters (FAME) (PubMed:30706417). Can also utilize ceramide
CC instead of DAG, acylating the ceramides by attaching a fatty acid to
CC the hydroxy group on the first carbon atom of the long-chain base to
CC produce 1-O-acylceramides (PubMed:22738231). Involved in lipid particle
CC synthesis from the endoplasmic reticulum, promoting localized TAG
CC production at discrete ER subdomains (PubMed:32349126). Relocates from
CC the endoplasmic reticulum to a subdomain of the inner nuclear membrane
CC upon nutrient starvation, where it provides a site of TAG synthesis,
CC which is coupled with nuclear membrane remodeling (PubMed:31422915).
CC {ECO:0000269|PubMed:10747858, ECO:0000269|PubMed:10829075,
CC ECO:0000269|PubMed:22738231, ECO:0000269|PubMed:30706417,
CC ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a
CC monoacylglycerophospholipid + a triacyl-sn-glycerol;
CC Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615,
CC ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158;
CC Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386,
CC ECO:0000269|PubMed:30706417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-
CC glycerol = a 1,2-diacyl-sn-glycerol + a 1-acyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:32859, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:64683;
CC Evidence={ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32860;
CC Evidence={ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-
CC glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:44232, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44233;
CC Evidence={ECO:0000305|PubMed:10829075, ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1,2-di-
CC (9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol
CC + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:44236, ChEBI:CHEBI:28610, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44237;
CC Evidence={ECO:0000305|PubMed:10829075, ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z-
CC octadecenoyl)-sn-glycerol = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + di-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:44240,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:74669, ChEBI:CHEBI:75757,
CC ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44241;
CC Evidence={ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-(9Z-
CC octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:44244,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:52323, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:74669; Evidence={ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44245;
CC Evidence={ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z-octadecenoyl)-2-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-
CC octadecenoyl-3-hexadecanoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44248,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:75583,
CC ChEBI:CHEBI:78813; Evidence={ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44249;
CC Evidence={ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z-octadecenoyl)-2-
CC octadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-
CC octadecenoyl-3-octadecanoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44252,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:77686,
CC ChEBI:CHEBI:84234; Evidence={ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44253;
CC Evidence={ECO:0000305|PubMed:18037386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z)-octadecenoyl-2-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-
CC (9Z)-octadecenoyl-3-(9Z,12Z)-octadecadienoyl-sn-glycerol + 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44256,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:74977,
CC ChEBI:CHEBI:77683; Evidence={ECO:0000269|PubMed:18037386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44257;
CC Evidence={ECO:0000305|PubMed:18037386};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22446555, ECO:0000269|PubMed:22454508,
CC ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:22446555}. Nucleus inner
CC membrane {ECO:0000269|PubMed:31422915}; Single-pass type II membrane
CC protein {ECO:0000255}. Note=Localizes to sites of lipid droplet
CC biogenesis in the endoplasmic reticulum (PubMed:22454508,
CC PubMed:32349126). Relocates from the endoplasmic reticulum to a
CC subdomain of the inner nuclear membrane that associates with the
CC nucleolus upon nutrient starvation (PubMed:31422915).
CC {ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915,
CC ECO:0000269|PubMed:32349126}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X77395; CAA54576.1; -; Genomic_DNA.
DR EMBL; Z71623; CAA96285.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10549.1; -; Genomic_DNA.
DR PIR; S45131; S45131.
DR RefSeq; NP_014405.1; NM_001183185.1.
DR AlphaFoldDB; P40345; -.
DR BioGRID; 35833; 146.
DR DIP; DIP-6403N; -.
DR IntAct; P40345; 2.
DR STRING; 4932.YNR008W; -.
DR SwissLipids; SLP:000000059; -.
DR ESTHER; yeast-pdat; PC-sterol_acyltransferase.
DR GlyCosmos; P40345; 4 sites, No reported glycans.
DR GlyGen; P40345; 4 sites.
DR iPTMnet; P40345; -.
DR MaxQB; P40345; -.
DR PaxDb; 4932-YNR008W; -.
DR PeptideAtlas; P40345; -.
DR EnsemblFungi; YNR008W_mRNA; YNR008W; YNR008W.
DR GeneID; 855742; -.
DR KEGG; sce:YNR008W; -.
DR AGR; SGD:S000005291; -.
DR SGD; S000005291; LRO1.
DR VEuPathDB; FungiDB:YNR008W; -.
DR eggNOG; KOG2369; Eukaryota.
DR HOGENOM; CLU_016065_1_0_1; -.
DR InParanoid; P40345; -.
DR OMA; SMGSQVI; -.
DR OrthoDB; 589269at2759; -.
DR BioCyc; YEAST:YNR008W-MONOMER; -.
DR BRENDA; 2.3.1.158; 984.
DR BioGRID-ORCS; 855742; 1 hit in 10 CRISPR screens.
DR PRO; PR:P40345; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40345; Protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:SGD.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0046027; F:phospholipid:diacylglycerol acyltransferase activity; IDA:SGD.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:SGD.
DR GO; GO:0019915; P:lipid storage; IDA:SGD.
DR GO; GO:0055091; P:phospholipid homeostasis; IDA:SGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:SGD.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF02450; LCAT; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..661
FT /note="Phospholipid:diacylglycerol acyltransferase"
FT /id="PRO_0000058268"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22446555"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..661
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:22446555"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..50
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 64..71
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 322..326
FT /note="GHSXG lipase motif"
FT /evidence="ECO:0000305|PubMed:31422915"
FT COMPBIAS 11..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT ACT_SITE 567
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT ACT_SITE 618
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3,
FT ECO:0000305|PubMed:32349126"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30706417"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30706417"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30706417"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30706417"
FT MUTAGEN 324
FT /note="S->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:31422915"
FT MUTAGEN 618
FT /note="H->A: Abolishes catalytic activity. Fails to
FT localize to lipid droplet biogenesis sites on the ER."
FT /evidence="ECO:0000269|PubMed:32349126"
SQ SEQUENCE 661 AA; 75393 MW; 01C043319A836F44 CRC64;
MGTLFRRNVQ NQKSDSDENN KGGSVHNKRE SRNHIHHQQG LGHKRRRGIS GSAKRNERGK
DFDRKRDGNG RKRWRDSRRL IFILGAFLGV LLPFSFGAYH VHNSDSDLFD NFVNFDSLKV
YLDDWKDVLP QGISSFIDDI QAGNYSTSSL DDLSENFAVG KQLLRDYNIE AKHPVVMVPG
VISTGIESWG VIGDDECDSS AHFRKRLWGS FYMLRTMVMD KVCWLKHVML DPETGLDPPN
FTLRAAQGFE STDYFIAGYW IWNKVFQNLG VIGYEPNKMT SAAYDWRLAY LDLERRDRYF
TKLKEQIELF HQLSGEKVCL IGHSMGSQII FYFMKWVEAE GPLYGNGGRG WVNEHIDSFI
NAAGTLLGAP KAVPALISGE MKDTIQLNTL AMYGLEKFFS RIERVKMLQT WGGIPSMLPK
GEEVIWGDMK SSSEDALNNN TDTYGNFIRF ERNTSDAFNK NLTMKDAINM TLSISPEWLQ
RRVHEQYSFG YSKNEEELRK NELHHKHWSN PMEVPLPEAP HMKIYCIYGV NNPTERAYVY
KEEDDSSALN LTIDYESKQP VFLTEGDGTV PLVAHSMCHK WAQGASPYNP AGINVTIVEM
KHQPDRFDIR GGAKSAEHVD ILGSAELNDY ILKIASGNGD LVEPRQLSNL SQWVSQMPFP
M
//
