ID LAC1_YEAST Reviewed; 418 AA. AC P28496; D6VXS8; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 04-NOV-2026, entry version 201. DE RecName: Full=Ceramide synthase LAC1; DE AltName: Full=Very-long-chain ceramide synthase LAC1; DE EC=2.3.1.297 {ECO:0000269|PubMed:11694577, ECO:0000269|PubMed:15692566, ECO:0000269|PubMed:37953642, ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796}; GN Name=LAC1; Synonyms=DGT1; OrderedLocusNames=YKL008C; ORFNames=YKL156; 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]. RX PubMed=8488728; DOI=10.1002/yea.320090307; RA Boyer J., Pascolo S., Richard G.-F., Dujon B.; RT "Sequence of a 7.8 kb segment on the left arm of yeast chromosome XI RT reveals four open reading frames, including the CAP1 gene, an intron- RT containing gene and a gene encoding a homolog to the mammalian UOG-1 RT gene."; RL Yeast 9:279-287(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149. RX PubMed=1447293; DOI=10.1083/jcb.119.5.1151; RA Amatruda J.F., Gattermeir D.J., Karpova T.S., Cooper J.A.; RT "Effects of null mutations and overexpression of capping protein on RT morphogenesis, actin distribution and polarized secretion in yeast."; RL J. Cell Biol. 119:1151-1162(1992). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10198056; DOI=10.1091/mbc.10.4.1043; RA Barz W.P., Walter P.; RT "Two endoplasmic reticulum (ER) membrane proteins that facilitate ER-to- RT Golgi transport of glycosylphosphatidylinositol-anchored proteins."; RL Mol. Biol. Cell 10:1043-1059(1999). RN [6] RP FUNCTION. RX PubMed=11387200; DOI=10.1093/emboj/20.11.2655; RA Guillas I., Kirchman P.A., Chuard R., Pfefferli M., Jiang J.C., RA Jazwinski S.M., Conzelmann A.; RT "C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is RT operated by Lag1p and Lac1p."; RL EMBO J. 20:2655-2665(2001). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=11694577; DOI=10.1091/mbc.12.11.3417; RA Schorling S., Vallee B., Barz W.P., Riezman H., Oesterhelt D.; RT "Lag1p and Lac1p are essential for the acyl-CoA-dependent ceramide synthase RT reaction in Saccharomyces cerevisae."; RL Mol. Biol. Cell 12:3417-3427(2001). RN [8] RP DOMAIN, AND TOPOLOGY. RX PubMed=12151215; DOI=10.1016/s0968-0004(02)02154-0; RA Winter E., Ponting C.P.; RT "TRAM, LAG1 and CLN8: members of a novel family of lipid-sensing domains?"; RL Trends Biochem. Sci. 27:381-383(2002). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [10] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [11] RP INDUCTION. RX PubMed=15302821; DOI=10.1128/ec.3.4.880-892.2004; RA Kolaczkowski M., Kolaczkowska A., Gaigg B., Schneiter R., Moye-Rowley W.S.; RT "Differential regulation of ceramide synthase components LAC1 and LAG1 in RT Saccharomyces cerevisiae."; RL Eukaryot. Cell 3:880-892(2004). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, IDENTIFICATION BY MASS SPECTROMETRY, RP AND INTERACTION WITH LAG1 AND LIP1. RX PubMed=15692566; DOI=10.1038/sj.emboj.7600562; RA Vallee B., Riezman H.; RT "Lip1p: a novel subunit of acyl-CoA ceramide synthase."; RL EMBO J. 24:730-741(2005). RN [13] RP TOPOLOGY. RX PubMed=16756512; DOI=10.1042/bj20060697; RA Kageyama-Yahara N., Riezman H.; RT "Transmembrane topology of ceramide synthase in yeast."; RL Biochem. J. 398:585-593(2006). RN [14] RP TOPOLOGY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 208353 / W303-1A; RX PubMed=16847258; DOI=10.1073/pnas.0604075103; RA Kim H., Melen K., Oesterberg M., von Heijne G.; RT "A global topology map of the Saccharomyces cerevisiae membrane proteome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] {ECO:0000305} RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=26726837; DOI=10.1080/15384101.2015.1127475; RA Villasmil M.L., Francisco J., Gallo-Ebert C., Donigan M., Liu H.Y., RA Brower M., Nickels J.T. Jr.; RT "Ceramide signals for initiation of yeast mating-specific cell cycle RT arrest."; RL Cell Cycle 15:441-454(2016). RN [17] {ECO:0000305} RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=31164445; DOI=10.1242/jcs.228411; RA Megyeri M., Prasad R., Volpert G., Sliwa-Gonzalez A., Haribowo A.G., RA Aguilera-Romero A., Riezman H., Barral Y., Futerman A.H., Schuldiner M.; RT "Yeast ceramide synthases, Lag1 and Lac1, have distinct substrate RT specificity."; RL J. Cell Sci. 132:0-0(2019). RN [18] {ECO:0000305} RP PHOSPHORYLATION. RX PubMed=39490931; DOI=10.1016/j.jlr.2024.100683; RA Ren J., Rieger R., Pereira de Sa N., Kelapire D., Del Poeta M., RA Hannun Y.A.; RT "Orm proteins control ceramide synthesis and endocytosis via LCB-mediated RT Ypk1 regulation."; RL J. Lipid Res. 65:100683-100683(2024). RN [19] {ECO:0007744|PDB:8IZD, ECO:0007744|PDB:8IZF} RP STRUCTURE BY ELECTRON MICROSCOPYIN COMPLEX WITH LIP1; HEXACOSANOYL-COA AND RP 1-PALMITOYL-2-STEAROYL-SN-GLYCERO-3-PHOSPHOCHOLINE, FUNCTION, CATALYTIC RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF SER-186; GLN-227; TRP-231; HIS-255; RP HIS-256; PHE-269; PHE-271; MET-274; TYR-279; MET-282; ASP-283; ASP-286; RP LYS-293; ASN-296; ARG-318; LEU-341; PHE-343; TYR-348 AND ILE-352. RX PubMed=37953642; DOI=10.15252/embj.2023114889; RA Xie T., Fang Q., Zhang Z., Wang Y., Dong F., Gong X.; RT "Structure and mechanism of a eukaryotic ceramide synthase complex."; RL EMBO J. 42:e114889-e114889(2023). RN [20] {ECO:0007744|PDB:8QTN, ECO:0007744|PDB:8QTR} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH LAG1; LIP1; HEXACOSANOIC RP ACID; 1,2-DISTEAROYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE AND FUMONISIN B1, RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF ARG-172; SER-265; SER-266; GLY-275; LEU-289; LYS-293; RP ASN-296; ARG-318; SER-353; ILE-375; ARG-381; LYS-389 AND ARG-392. RX PubMed=39528796; DOI=10.1038/s41594-024-01415-2; RA Schafer J.H., Clausmeyer L., Korner C., Esch B.M., Wolf V.N., Sapia J., RA Ahmed Y., Walter S., Vanni S., Januliene D., Moeller A., Frohlich F.; RT "Structure of the yeast ceramide synthase."; RL Nat. Struct. Mol. Biol. 0:0-0(2024). RN [21] {ECO:0007744|PDB:8Y2M, ECO:0007744|PDB:8Y2N, ECO:0007744|PDB:8ZB1} RP STRUCTURE BY ELECTRON MICROSCOPY OF LAC1 AND LIP1 IN APO FORM AND IN RP COMPLEX WITH HEXACOSANOIC ACID; FUMONISIN B1 AND N-ACYL FUMONISIN B1, RP SUBUNIT, AND MUTAGENESIS OF HIS-255 AND HIS-256. RX PubMed=38964337; DOI=10.1016/j.str.2024.06.002; RA Zhang Z., Fang Q., Xie T., Gong X.; RT "Mechanism of ceramide synthase inhibition by fumonisin B1."; RL Structure 32:1419-1428.e4(2024). CC -!- FUNCTION: Component of the ceramide synthase complex that catalyzes the CC transfer of the acyl chain from acyl-CoA to a sphingoid base, with high CC selectivity toward hexacosanoyl-CoA (C26:0-CoA) (PubMed:11694577, CC PubMed:15692566, PubMed:37953642, PubMed:39528796). N-acylates CC sphinganine and phytosphingosine bases to form dihydroceramides and CC phytoceramides, respectively (PubMed:11694577, PubMed:15692566). CC Redundant with LAG1 (PubMed:39528796). Facilitates ER-to-Golgi CC transport of GPI-anchored proteins. Has a lower affinity for CC phytosphingosine (PHS) than dihydrosphingosine (DHS); PHS is required CC for the synthesis of phytoceramides and the formation of nuclear CC envelopes (PubMed:31164445). Along with LAG1, plays a role in CC pheromone-induced MAP kinase-activation of mating and formation of CC diploid cells (PubMed:26726837). May also play a role, together with CC LAG1, in the polarized membrane distribution of phosphatidylinositol CC 4,5 biphosphate required for STE5 localization to the plasma membrane CC (PubMed:26726837). {ECO:0000269|PubMed:10198056, CC ECO:0000269|PubMed:11387200, ECO:0000269|PubMed:11694577, CC ECO:0000269|PubMed:15692566, ECO:0000269|PubMed:26726837, CC ECO:0000269|PubMed:31164445, ECO:0000269|PubMed:37953642, CC ECO:0000269|PubMed:39528796}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a very long-chain fatty acyl-CoA + a sphingoid base = an N- CC (very-long-chain fatty acyl)-sphingoid base + CoA + H(+); CC Xref=Rhea:RHEA:61480, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:84410, ChEBI:CHEBI:138261, ChEBI:CHEBI:144712; CC EC=2.3.1.297; Evidence={ECO:0000269|PubMed:11694577, CC ECO:0000269|PubMed:15692566, ECO:0000269|PubMed:37953642, CC ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61481; CC Evidence={ECO:0000269|PubMed:11694577, ECO:0000269|PubMed:15692566, CC ECO:0000269|PubMed:37953642, ECO:0000269|PubMed:38964337, CC ECO:0000269|PubMed:39528796}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexacosanoyl-CoA + sphinganine = N-hexacosanoylsphinganine + CC CoA + H(+); Xref=Rhea:RHEA:33351, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:52962, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, CC ChEBI:CHEBI:64868; Evidence={ECO:0000269|PubMed:15692566}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33352; CC Evidence={ECO:0000269|PubMed:15692566}; CC -!- CATALYTIC ACTIVITY: CC Reaction=eicosanoyl-CoA + sphinganine = N-eicosanoylsphinganine + CoA + CC H(+); Xref=Rhea:RHEA:36555, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57380, ChEBI:CHEBI:57817, ChEBI:CHEBI:67027; CC Evidence={ECO:0000269|PubMed:15692566}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36556; CC Evidence={ECO:0000269|PubMed:15692566}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sphinganine + a fatty acyl-CoA = an N-acylsphinganine + CoA + CC H(+); Xref=Rhea:RHEA:34735, ChEBI:CHEBI:15378, ChEBI:CHEBI:31488, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:77636; CC Evidence={ECO:0000269|PubMed:11694577}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34736; CC Evidence={ECO:0000269|PubMed:11694577}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4R)-hydroxysphinganine + a fatty acyl-CoA = an N-acyl-(4R)-4- CC hydroxysphinganine + CoA + H(+); Xref=Rhea:RHEA:35651, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:31998, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:64124, ChEBI:CHEBI:77636; CC Evidence={ECO:0000269|PubMed:11694577}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35652; CC Evidence={ECO:0000269|PubMed:11694577}; CC -!- ACTIVITY REGULATION: As part of the ceramide synthase complex, CC inhibited by the sphinganine analog mycotoxin, fumonisin B1 (FB1) CC (PubMed:38964337, PubMed:39528796). Activated by ACB1, as part of the CC ceramide synthase complex (PubMed:39528796). CC {ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796}. CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC {ECO:0000269|PubMed:11694577, ECO:0000269|PubMed:15692566}. CC -!- SUBUNIT: Component of the ceramide synthase complex composed of at CC least LAC1, LAG1 and LIP1 (PubMed:37953642, PubMed:39528796). Forms a CC heterotetrameric complex, where one unit of the LIP1 homodimer CC interacts with LAC1 and the other with either LAC1 or LAG1 CC (PubMed:37953642, PubMed:38964337, PubMed:39528796). CC {ECO:0000269|PubMed:37953642, ECO:0000269|PubMed:38964337, CC ECO:0000269|PubMed:39528796}. CC -!- INTERACTION: CC P28496; P38703: LAG1; NbExp=7; IntAct=EBI-26585, EBI-10035; CC P28496; Q03579: LIP1; NbExp=6; IntAct=EBI-26585, EBI-27640; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:10198056, ECO:0000269|PubMed:14562095}; Multi-pass CC membrane protein {ECO:0000269|PubMed:10198056, CC ECO:0000269|PubMed:14562095}. Note=The specific interaction of LAC1 and CC LIP1 at the lumen of the ER may be important for the enzymatic activity CC of the complex. {ECO:0000269|PubMed:37953642}. CC -!- INDUCTION: Expression is controlled by PDR1 and PDR3 which bind its CC promoter PDRE element, and by ROX1 and CBF1. CC {ECO:0000269|PubMed:15302821}. CC -!- PTM: Phosphorylated; phosphorylation is induced upon disruption of CC sphingolipid synthesis (By similarity). Phosphorylation is inhibited by CC exogenous addition of phytosphingosine (PubMed:39490931). CC {ECO:0000250|UniProtKB:P38703, ECO:0000269|PubMed:39490931}. CC -!- DISRUPTION PHENOTYPE: Does not affect the level of total sphingolipids CC (PubMed:31164445). Exhibits weak diffusion barriers only in cortical ER CC and not in the nuclear envelope (PubMed:31164445). Double knockout of CC LAC1 and LAG1 abolishes growth and leads to mating defects including CC defects in diploid cell formation, pheromone-induced shmoo formation, CC induction of cell cycle arrest and activation of mating-specific MAP CC kinase (PubMed:26726837, PubMed:39528796). Also defective in the CC localization of STE5 to the plasma membrane (PubMed:26726837). Double CC knockout of LAC1 and SUR2 reduces the ability to synthesize CC dihydrosphingosines and other complex sphingolipids and increases CC sensitivity to thermal stress (PubMed:31164445). CC {ECO:0000269|PubMed:26726837, ECO:0000269|PubMed:31164445, CC ECO:0000269|PubMed:39528796}. CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the sphingosine N-acyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X61398; CAA43670.1; -; Genomic_DNA. DR EMBL; S59773; AAC60549.1; -; Genomic_DNA. DR EMBL; Z28008; CAA81843.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09148.1; -; Genomic_DNA. DR PIR; S30134; S30134. DR RefSeq; NP_012917.3; NM_001179574.3. DR PDB; 8IZD; EM; 3.09 A; A/C=1-418. DR PDB; 8IZF; EM; 3.85 A; A/C=1-418. DR PDB; 8QTN; EM; 3.00 A; B=75-379. DR PDB; 8QTR; EM; 3.20 A; B=78-379. DR PDB; 8Y2M; EM; 3.07 A; A/C=1-418. DR PDB; 8Y2N; EM; 3.19 A; A/C=1-418. DR PDB; 8ZB1; EM; 2.86 A; A/C=1-418. DR PDB; 9W3Z; EM; 3.36 A; A/C/E/G=1-418. DR AlphaFoldDB; P28496; -. DR EMDB; EMD-18652; -. DR EMDB; EMD-18653; -. DR EMDB; EMD-35862; -. DR EMDB; EMD-35863; -. DR EMDB; EMD-38857; -. DR EMDB; EMD-38858; -. DR EMDB; EMD-39894; -. DR EMDB; EMD-65613; -. DR SMR; P28496; -. DR BioGRID; 34124; 114. DR ComplexPortal; CPX-1706; Acyl-CoA ceramide synthase complex. DR DIP; DIP-4348N; -. DR FunCoup; P28496; 591. DR IntAct; P28496; 67. DR MINT; P28496; -. DR STRING; 4932.YKL008C; -. DR SwissLipids; SLP:000000277; -. DR GlyCosmos; P28496; 1 site, No reported glycans. DR GlyGen; P28496; 1 site. DR iPTMnet; P28496; -. DR PaxDb; 4932-YKL008C; -. DR PeptideAtlas; P28496; -. DR EnsemblFungi; YKL008C_mRNA; YKL008C; YKL008C. DR GeneID; 853861; -. DR KEGG; sce:YKL008C; -. DR AGR; SGD:S000001491; -. DR SGD; S000001491; LAC1. DR VEuPathDB; FungiDB:YKL008C; -. DR eggNOG; KOG1607; Eukaryota. DR HOGENOM; CLU_028277_4_0_1; -. DR InParanoid; P28496; -. DR OMA; AAMYEGF; -. DR OrthoDB; 3053196at2759; -. DR BioCyc; MetaCyc:MONOMER3O-373; -. DR BioCyc; YEAST:MONOMER3O-373; -. DR BRENDA; 2.3.1.297; 984. DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis. DR UniPathway; UPA00222; -. DR BioGRID-ORCS; 853861; 1 hit in 10 CRISPR screens. DR PRO; PR:P28496; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P28496; protein. DR GO; GO:0061576; C:acyl-CoA ceramide synthase complex; IDA:SGD. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0034399; C:nuclear periphery; HDA:SGD. DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IDA:SGD. DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:ComplexPortal. DR InterPro; IPR016439; Lag1/Lac1-like. DR InterPro; IPR006634; TLC-dom. DR PANTHER; PTHR12560:SF11; CERAMIDE SYNTHASE LAC1-RELATED; 1. DR PANTHER; PTHR12560; LONGEVITY ASSURANCE FACTOR 1 LAG1; 1. DR Pfam; PF03798; TRAM_LAG1_CLN8; 1. DR PIRSF; PIRSF005225; LAG1_LAC1; 1. DR SMART; SM00724; TLC; 1. DR PROSITE; PS50922; TLC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Endoplasmic reticulum; Glycoprotein; KW Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..418 FT /note="Ceramide synthase LAC1" FT /id="PRO_0000185535" FT TOPO_DOM 2..81 FT /note="Cytoplasmic" FT /evidence="ECO:0000255, ECO:0000269|PubMed:38964337" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 103..130 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 131..155 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 156..172 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 173..194 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 195..217 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 218..240 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 241..249 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 250..268 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 269..273 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 274..295 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 296..305 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 306..334 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 335..353 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TRANSMEM 354..382 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT TOPO_DOM 383..418 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337, ECO:0000269|PubMed:39528796" FT DOMAIN 168..385 FT /note="TLC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205, FT ECO:0000269|PubMed:38964337" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 390..418 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..14 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..24 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 169 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTR" FT BINDING 172 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 182 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0007744|PDB:8Y2M" FT BINDING 224 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0007744|PDB:8Y2M" FT BINDING 231 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0007744|PDB:8Y2M" FT BINDING 231 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8Y2M" FT BINDING 231 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 255 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 255 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 255 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 259 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTN, ECO:0007744|PDB:8QTR" FT BINDING 259 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 262 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 262 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 263 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTN, ECO:0007744|PDB:8QTR" FT BINDING 265 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 265 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 266 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 266 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 269 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 271 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8Y2M" FT BINDING 271 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 274 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 274 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 275 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 275 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 278 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTN, ECO:0007744|PDB:8QTR" FT BINDING 278 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 279 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 279 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 282 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 282 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 283 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8Y2M" FT BINDING 286 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 286 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8Y2M" FT BINDING 286 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 289 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 289 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 293 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 293 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 296 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 296 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 297 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 303 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 304 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 307 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 307 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 314 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTR" FT BINDING 318 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTN, ECO:0007744|PDB:8QTR" FT BINDING 318 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 343 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTR" FT BINDING 348 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 348 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 352 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 352 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 353 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 353 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 356 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 356 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 357 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 357 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 360 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTN, FT ECO:0007744|PDB:8QTR, ECO:0007744|PDB:8Y2M" FT BINDING 360 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 361 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTN" FT BINDING 371 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 371 FT /ligand="hexacosanoate" FT /ligand_id="ChEBI:CHEBI:31013" FT /evidence="ECO:0000269|PubMed:39528796, FT ECO:0007744|PDB:8QTR" FT BINDING 371 FT /ligand="hexacosanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:64868" FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0007744|PDB:8IZD" FT BINDING 375 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 378 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0000269|PubMed:39528796, ECO:0007744|PDB:8QTR, FT ECO:0007744|PDB:8Y2M" FT BINDING 382 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0007744|PDB:8Y2M" FT BINDING 385 FT /ligand="fumonisin B1" FT /ligand_id="ChEBI:CHEBI:62554" FT /evidence="ECO:0000269|PubMed:38964337, FT ECO:0007744|PDB:8Y2M" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38703" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38703" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT MUTAGEN 172 FT /note="R->A: Abolishes the enzymatic activity of the FT ceramide synthase complex. Does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with A-293, A-296, A-318 and A-381." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 186 FT /note="S->A: Does not affect the enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 227 FT /note="Q->A: About 80% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 231 FT /note="W->A: About 85% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 255 FT /note="H->A: Abolishes the enzymatic activity of the FT LAC1-LIP1 complex; alone or when associated with A-256. FT Does not catalyze the reaction between hexacosanoyl-CoA and FT fumonisin B1; when associated with A-256." FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337" FT MUTAGEN 256 FT /note="H->A: Abolishes the enzymatic activity of the FT LAC1-LIP1 complex; alone or when associated with A-255. FT Does not catalyze the reaction between hexacosanoyl-CoA and FT fumonisin B1; when associated with A-255." FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:38964337" FT MUTAGEN 265 FT /note="S->F: Abolishes the enzymatic activity of the FT ceramide synthase complex and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with F-266, F-275, F-353 and F-375." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 266 FT /note="S->F: Abolishes the enzymatic activity of the FT ceramide synthase complex and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with F-265, F-275, F-353 and F-375." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 269 FT /note="F->A: About 75% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 271 FT /note="F->A: More than 90% loss in enzymatic activity of FT the LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 274 FT /note="M->A: About 80% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 275 FT /note="G->F: Abolishes the enzymatic activity of the FT ceramide synthase complex and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with F-265, F-266, F-353 and F-375." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 279 FT /note="Y->A: About 90% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 282 FT /note="M->A: About 60% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 283 FT /note="D->A: Reduces the enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 286 FT /note="D->A: Abolishes the enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 293 FT /note="K->A: About 80% loss in enzymatic activity of the FT LAC1-LIP1 complex. Does not rescue the growth defect of FT LAC1-LAG1 double deletion mutant; when associated with FT A-172, A-296, A-318 and A-381." FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:39528796" FT MUTAGEN 296 FT /note="N->A: About 60% loss in enzymatic activity of the FT LAC1-LIP1 complex. Does not rescue the growth defect of FT LAC1-LAG1 double deletion mutant; when associated with FT A-172, A-293, A-318 and A-381." FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:39528796" FT MUTAGEN 318 FT /note="R->A: Abolishes the enzymatic activity of the FT LAC1-LIP1 complex. Does not rescue the growth defect of FT LAC1-LAG1 double deletion mutant; when associated with FT A-172, A-293, A-296 and A-381." FT /evidence="ECO:0000269|PubMed:37953642, FT ECO:0000269|PubMed:39528796" FT MUTAGEN 341 FT /note="L->A: About 90% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 343 FT /note="F->A: More than 90% loss in enzymatic activity of FT the LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 348 FT /note="Y->A: More than 90% loss in enzymatic activity of FT the LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 352 FT /note="I->A: About 60% loss in enzymatic activity of the FT LAC1-LIP1 complex." FT /evidence="ECO:0000269|PubMed:37953642" FT MUTAGEN 353 FT /note="S->F: Abolishes the enzymatic activity of the FT ceramide synthase complex and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with F-265, F-266, F-275 and F-375." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 375 FT /note="I->F: Abolishes the enzymatic activity of the FT ceramide synthase complex and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with F-265, F-266, F-275 and F-353." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 381 FT /note="R->A: Abolishes the enzymatic activity of the FT ceramide synthase complex. Does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with A-172, A-293, A-296 and A-318." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 389 FT /note="K->A: Reduces the in vitro activity of LAC1-LIP1 FT complex in the presence of ACB1, increases the levels of FT phytosphingosine in vivo and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with A-392." FT /evidence="ECO:0000269|PubMed:39528796" FT MUTAGEN 392 FT /note="R->A: Reduces the in vitro activity of LAC1-LIP1 FT complex in the presence of ACB1, increases the levels of FT phytosphingosine in vivo and does not rescue the growth FT defect of LAC1-LAG1 double deletion mutant; when associated FT with A-389." FT /evidence="ECO:0000269|PubMed:39528796" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 85..99 FT /evidence="ECO:0007829|PDB:8ZB1" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:8ZB1" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:8Y2M" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 131..150 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 151..155 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:8ZB1" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 168..195 FT /evidence="ECO:0007829|PDB:8ZB1" FT TURN 198..202 FT /evidence="ECO:0007829|PDB:8ZB1" FT TURN 206..210 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 218..239 FT /evidence="ECO:0007829|PDB:8ZB1" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:8QTN" FT HELIX 251..268 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 272..297 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 303..314 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 315..320 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 321..332 FT /evidence="ECO:0007829|PDB:8ZB1" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:8ZB1" FT TURN 343..346 FT /evidence="ECO:0007829|PDB:8ZB1" FT HELIX 353..384 FT /evidence="ECO:0007829|PDB:8ZB1" SQ SEQUENCE 418 AA; 48992 MW; 7691BA623AC0460A CRC64; MSTIKPSPSN NNLKVRSRPR RKSSIGKIDL GDTVPSLGTM FETKESKTAA KRRMQRLSEA TKNDSDLVKK IWFSFREISY RHAWIAPLMI LIAVYSAYFT SGNTTKTNVL HRFVAVSYQI GDTNAYGKGI NDLCFVFYYM IFFTFLREFL MDVVIRPFAI RLHVTSKHRI KRIMEQMYAI FYTGVSGPFG IYCMYHSDLW FFNTKAMYRT YPDFTNPFLF KVFYLGQAAF WAQQACILVL QLEKPRKDHN ELTFHHIVTL LLIWSSYVFH FTKMGLPIYI TMDVSDFLLS FSKTLNYLDS GLAFFSFAIF VVAWIYLRHY INLKILWSVL TQFRTEGNYV LNFATQQYKC WISLPIVFVL IGALQLVNLY WLFLIFRVLY RILWRGILKD DRSDSESDEE SDESSTTPTD STPTKKDI //