ALE1_YEAST
ID ALE1_YEAST Reviewed; 619 AA.
AC Q08548; D6W2N1; Q03130;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Lysophospholipid acyltransferase {ECO:0000305};
DE Short=LPLAT;
DE EC=2.3.1.23 {ECO:0000269|PubMed:17890783};
DE EC=2.3.1.51 {ECO:0000269|PubMed:17890783, ECO:0000269|PubMed:18154737};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:17890783};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:17890783};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000303|PubMed:17726007};
DE Short=AGPAT;
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE AltName: Full=Lysophosphatidylcholine acyltransferase {ECO:0000303|PubMed:17726007};
DE Short=LPCAT;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase {ECO:0000303|PubMed:17652094};
DE Short=LPEAT;
DE AltName: Full=Lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE AltName: Full=Sphingolipid compensation protein 4 {ECO:0000303|PubMed:17675291};
GN Name=ALE1 {ECO:0000303|PubMed:17652094};
GN Synonyms=LCA1 {ECO:0000303|PubMed:17996202},
GN LPT1 {ECO:0000303|PubMed:17726007, ECO:0000303|PubMed:17890783},
GN SLC4 {ECO:0000303|PubMed:17675291}; OrderedLocusNames=YOR175C;
GN ORFNames=O3635;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-619.
RC STRAIN=S288c / FY1678;
RX PubMed=8972579;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT cerevisiae chromosome XV.";
RL Yeast 12:1563-1573(1996).
RN [4]
RP SIMILARITY.
RX PubMed=10694878; DOI=10.1016/s0968-0004(99)01539-x;
RA Hofmann K.;
RT "A superfamily of membrane-bound O-acyltransferases with implications for
RT wnt signaling.";
RL Trends Biochem. Sci. 25:111-112(2000).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=17996202; DOI=10.1016/j.febslet.2007.10.061;
RA Chen Q., Kazachkov M., Zheng Z., Zou J.;
RT "The yeast acylglycerol acyltransferase LCA1 is a key component of Lands
RT cycle for phosphatidylcholine turnover.";
RL FEBS Lett. 581:5511-5516(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=17652094; DOI=10.1074/jbc.m705256200;
RA Riekhof W.R., Wu J., Jones J.L., Voelker D.R.;
RT "Identification and characterization of the major
RT lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:28344-28352(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=17726007; DOI=10.1074/jbc.m706326200;
RA Jain S., Stanford N., Bhagwat N., Seiler B., Costanzo M., Boone C.,
RA Oelkers P.;
RT "Identification of a novel lysophospholipid acyltransferase in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:30562-30569(2007).
RN [10]
RP FUNCTION.
RX PubMed=17675291; DOI=10.1074/jbc.m702719200;
RA Benghezal M., Roubaty C., Veepuri V., Knudsen J., Conzelmann A.;
RT "SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-
RT phosphate O-acyltransferases of budding yeast.";
RL J. Biol. Chem. 282:30845-30855(2007).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-382,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=17890783; DOI=10.1074/jbc.m704509200;
RA Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation
RT of lysophospholipids in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:34288-34298(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-605, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP CATALYTIC ACTIVITY.
RX PubMed=18154737; DOI=10.1016/j.febslet.2007.12.020;
RA Stahl U., Stalberg K., Stymne S., Ronne H.;
RT "A family of eukaryotic lysophospholipid acyltransferases with broad
RT specificity.";
RL FEBS Lett. 582:305-309(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-605; SER-610 AND
RP SER-615, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-146 AND GLU-297.
RX PubMed=26382650; DOI=10.1194/jlr.m062141;
RA Renauer P., Nasiri N., Oelkers P.;
RT "Saccharomyces cerevisiae lysophospholipid acyltransferase, Lpt1, requires
RT Asp146 and Glu297 for catalysis.";
RL J. Lipid Res. 56:2143-2150(2015).
RN [18]
RP CATALYTIC ACTIVITY.
RX PubMed=26643989; DOI=10.1007/s11745-015-4102-0;
RA Jasieniecka-Gazarkiewicz K., Demski K., Lager I., Stymne S., Banas A.;
RT "Possible role of different yeast and plant lysophospholipid:acyl-CoA
RT acyltransferases (LPLATs) in acyl remodelling of phospholipids.";
RL Lipids 51:15-23(2016).
RN [19]
RP FUNCTION.
RX PubMed=29782033; DOI=10.1002/1873-3468.13103;
RA Morisada S., Ono Y., Kodaira T., Kishino H., Ninomiya R., Mori N.,
RA Watanabe H., Ohta A., Horiuchi H., Fukuda R.;
RT "The membrane-bound O-acyltransferase Ale1 transfers an acyl moiety to
RT newly synthesized 2-alkyl-sn-glycero-3-phosphocholine in yeast.";
RL FEBS Lett. 592:1829-1836(2018).
CC -!- FUNCTION: Broad specificity membrane-bound O-acyltransferase that
CC mediates the incorporation of unsaturated acyl chains into the sn-2
CC position of various lysophospholipids. Preferentially acylates
CC lysophosphocholine (LPC), but also lysophosphoethanolamine (LPE),
CC lysophosphatidylglycerol (LPG), lysophosphatidic acid (LPA),
CC lysophosphoethanolamine (LPE), lysophosphoinositol (LPI), and
CC lysophosphoserine (LPS) (PubMed:17996202, PubMed:17652094,
CC PubMed:17726007, PubMed:17675291, PubMed:17890783). Prefers an acyl
CC residue to an alkyl residue at the sn-1 position of lysophospholipid
CC acceptors. Accepts acyl chains in acyl-CoA from C-2 to C-20, and shows
CC strong preference for unsaturated acyl-CoAs with 16-20 carbons
CC (PubMed:17890783). Together with SLC1, plays a central role in
CC phosphatidic acid (PA) biosynthesis. PA is the intermediate, from which
CC all glycerophospholipids are synthesized (PubMed:17890783). Can also
CC introduce an acyl chain at the sn-1 position of the
CC lysophosphatidylcholine analog 1-hydroxy-2-hexadecyl-sn-glycero-3-
CC phosphocholine (HHPC) (PubMed:29782033). {ECO:0000269|PubMed:17652094,
CC ECO:0000269|PubMed:17675291, ECO:0000269|PubMed:17726007,
CC ECO:0000269|PubMed:17890783, ECO:0000269|PubMed:17996202,
CC ECO:0000269|PubMed:29782033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:17890783, ECO:0000269|PubMed:18154737,
CC ECO:0000269|PubMed:26643989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000269|PubMed:26643989, ECO:0000305|PubMed:17890783,
CC ECO:0000305|PubMed:18154737};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:17890783, ECO:0000269|PubMed:26643989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:26643989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA =
CC 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC Evidence={ECO:0000269|PubMed:17890783};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) + an acyl-CoA
CC = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:33195, ChEBI:CHEBI:57287, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64771;
CC Evidence={ECO:0000269|PubMed:17890783};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:17890783};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:17890783, ECO:0000269|PubMed:26643989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:26643989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000269|PubMed:17652094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000305|PubMed:17652094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1-(9Z)-octadecenoyl-2-(9Z)-hexadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:42232,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:74971,
CC ChEBI:CHEBI:78810; Evidence={ECO:0000269|PubMed:17652094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42233;
CC Evidence={ECO:0000305|PubMed:17652094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:42236, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:74971, ChEBI:CHEBI:78813;
CC Evidence={ECO:0000269|PubMed:17652094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42237;
CC Evidence={ECO:0000305|PubMed:17652094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC tetradecanoyl-CoA = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:42240, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:74971, ChEBI:CHEBI:78814;
CC Evidence={ECO:0000269|PubMed:17652094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42241;
CC Evidence={ECO:0000305|PubMed:17652094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000269|PubMed:17652094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:17652094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000269|PubMed:17726007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000305|PubMed:17726007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:17726007, ECO:0000269|PubMed:26382650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000305|PubMed:17726007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-tetradecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:44308, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:84299, ChEBI:CHEBI:84300;
CC Evidence={ECO:0000269|PubMed:17726007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44309;
CC Evidence={ECO:0000305|PubMed:17726007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000269|PubMed:17726007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000305|PubMed:17726007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) = a 1-acyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-
CC myo-inositol) + CoA; Xref=Rhea:RHEA:37623, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64771, ChEBI:CHEBI:75116;
CC Evidence={ECO:0000269|PubMed:17726007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37624;
CC Evidence={ECO:0000305|PubMed:17726007};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for oleoyl-CoA (with lysophosphoethanolamine as cosubstrate)
CC {ECO:0000269|PubMed:17652094};
CC KM=17 uM for palmitoleoyl-CoA (with lysophosphoethanolamine as
CC cosubstrate) {ECO:0000269|PubMed:17652094};
CC KM=0.9 uM for palmitoyl-CoA (with lysophosphoethanolamine as
CC cosubstrate) {ECO:0000269|PubMed:17652094};
CC KM=0.4 uM for myristoyl-CoA (with lysophosphoethanolamine as
CC cosubstrate) {ECO:0000269|PubMed:17652094};
CC KM=49 uM for oleoyl-CoA (with lysophosphocholine as cosubstrate)
CC {ECO:0000269|PubMed:17726007};
CC KM=21 uM for palmitoleoyl-CoA (with lysophosphocholine as
CC cosubstrate) {ECO:0000269|PubMed:17726007};
CC KM=1.8 uM for palmitoyl-CoA (with lysophosphocholine as cosubstrate)
CC {ECO:0000269|PubMed:17726007};
CC KM=5.9 uM for stearoyl-CoA (with lysophosphocholine as cosubstrate)
CC {ECO:0000269|PubMed:17726007};
CC KM=11 uM for arachidonyl-CoA (with lysophosphocholine as cosubstrate)
CC {ECO:0000269|PubMed:17726007};
CC KM=23.8 uM for acetyl-CoA (with 1-palmitoyl-lysophosphocholine as
CC cosubstrate) {ECO:0000269|PubMed:17890783};
CC KM=8.7 uM for linoleoyl-CoA (with 1-palmitoyl-lysophosphocholine as
CC cosubstrate) {ECO:0000269|PubMed:17890783};
CC KM=0.467 uM for 1-palmitoyl-lysophosphocholine (with linoleoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17890783};
CC Vmax=38 nmol/min/mg enzyme with oleoyl-CoA as substrate (with
CC lysophosphoethanolamine as cosubstrate)
CC {ECO:0000269|PubMed:17652094};
CC Vmax=44 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with
CC lysophosphoethanolamine as cosubstrate)
CC {ECO:0000269|PubMed:17652094};
CC Vmax=3.7 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with
CC lysophosphoethanolamine as cosubstrate)
CC {ECO:0000269|PubMed:17652094};
CC Vmax=1.2 nmol/min/mg enzyme with myristoyl-CoA as substrate (with
CC lysophosphoethanolamine as cosubstrate)
CC {ECO:0000269|PubMed:17652094};
CC Vmax=125 nmol/min/mg enzyme with oleoyl-CoA as substrate (with
CC lysophosphocholine as cosubstrate) {ECO:0000269|PubMed:17726007};
CC Vmax=142 nmol/min/mg enzyme with palmitoleoyl-CoA as substrate (with
CC lysophosphocholine as cosubstrate) {ECO:0000269|PubMed:17726007};
CC Vmax=7.8 nmol/min/mg enzyme with palmitoyl-CoA as substrate (with
CC lysophosphocholine as cosubstrate) {ECO:0000269|PubMed:17726007};
CC Vmax=12 nmol/min/mg enzyme with stearoyl-CoA as substrate (with
CC lysophosphocholine as cosubstrate) {ECO:0000269|PubMed:17726007};
CC Vmax=58 nmol/min/mg enzyme with arachidonyl-CoA as substrate (with
CC lysophosphocholine as cosubstrate) {ECO:0000269|PubMed:17726007};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:17652094};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000305|PubMed:17890783}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17890783}; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z75083; CAA99384.1; -; Genomic_DNA.
DR EMBL; U55021; AAB47420.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10947.1; -; Genomic_DNA.
DR PIR; S67067; S67067.
DR RefSeq; NP_014818.1; NM_001183594.1.
DR AlphaFoldDB; Q08548; -.
DR SMR; Q08548; -.
DR BioGRID; 34569; 53.
DR DIP; DIP-5617N; -.
DR STRING; 4932.YOR175C; -.
DR SwissLipids; SLP:000000083; -.
DR iPTMnet; Q08548; -.
DR MaxQB; Q08548; -.
DR PaxDb; Q08548; -.
DR PRIDE; Q08548; -.
DR EnsemblFungi; YOR175C_mRNA; YOR175C; YOR175C.
DR GeneID; 854346; -.
DR KEGG; sce:YOR175C; -.
DR SGD; S000005701; ALE1.
DR VEuPathDB; FungiDB:YOR175C; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_5_0_1; -.
DR InParanoid; Q08548; -.
DR OMA; WHGTRPG; -.
DR BioCyc; MetaCyc:G3O-33688-MON; -.
DR BioCyc; YEAST:G3O-33688-MON; -.
DR BRENDA; 2.3.1.23; 984.
DR BRENDA; 2.3.1.51; 984.
DR Reactome; R-SCE-1482788; Acyl chain remodelling of PC.
DR Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
DR Reactome; R-SCE-1482839; Acyl chain remodelling of PE.
DR Reactome; R-SCE-1482922; Acyl chain remodelling of PI.
DR SABIO-RK; Q08548; -.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q08548; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08548; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IMP:SGD.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IMP:SGD.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:SGD.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IMP:SGD.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Coiled coil; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..619
FT /note="Lysophospholipid acyltransferase"
FT /id="PRO_0000245257"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..92
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..274
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..456
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 592..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 545..593
FT /evidence="ECO:0000255"
FT ACT_SITE 146
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:26382650"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:26382650"
FT ACT_SITE 382
FT /evidence="ECO:0000305|PubMed:17890783"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 146
FT /note="D->L: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26382650"
FT MUTAGEN 297
FT /note="E->L: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26382650"
FT MUTAGEN 382
FT /note="H->D: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:17890783"
SQ SEQUENCE 619 AA; 72228 MW; 87C74C9194BE0BC5 CRC64;
MYNPVDAVLT KIITNYGIDS FTLRYAICLL GSFPLNAILK RIPEKRIGLK CCFIISMSMF
YLFGVLNLVS GFRTLFISTM FTYLISRFYR SKFMPHLNFM FVMGHLAINH IHAQFLNEQT
QTTVDITSSQ MVLAMKLTSF AWSYYDGSCT SESDFKDLTE HQKSRAVRGH PPLLKFLAYA
FFYSTLLTGP SFDYADFDSW LNCEMFRDLP ESKKPMRRHH PGERRQIPKN GKLALWKVVQ
GLAWMILSTL GMKHFPVKYV LDKDGFPTRS FIFRIHYLFL LGFIHRFKYY AAWTISEGSC
ILCGLGYNGY DSKTQKIRWD RVRNIDIWTV ETAQNTREML EAWNMNTNKW LKYSVYLRVT
KKGKKPGFRS TLFTFLTSAF WHGTRPGYYL TFATGALYQT CGKIYRRNFR PIFLREDGVT
PLPSKKIYDL VGIYAIKLAF GYMVQPFIIL DLKPSLMVWG SVYFYVHIIV AFSFFLFRGP
YAKQVTEFFK SKQPKEIFIR KQKKLEKDIS ASSPNLGGIL KAKIEHEKGK TAEEEEMNLG
IPPIELEKWD NAKEDWEDFC KDYKEWRNKN GLEIEEENLS KAFERFKQEF SNAASGSGER
VRKMSFSGYS PKPISKKEE
