PAH1_YEAST
ID PAH1_YEAST Reviewed; 862 AA.
AC P32567; D6VZY7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Phosphatidic acid phosphohydrolase 1;
DE Short=PAP1;
DE EC=3.1.3.4;
DE AltName: Full=Protein SMP2;
GN Name=PAH1; Synonyms=PAP1, SMP2; OrderedLocusNames=YMR165C;
GN ORFNames=YM8520.14C;
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], AND FUNCTION.
RC STRAIN=NBW5;
RX PubMed=8437575; DOI=10.1007/bf00277124;
RA Irie K., Takase M., Araki H., Oshima Y.;
RT "A gene, SMP2, involved in plasmid maintenance and respiration in
RT Saccharomyces cerevisiae encodes a highly charged protein.";
RL Mol. Gen. Genet. 236:283-288(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [5]
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 [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15889145; DOI=10.1038/sj.emboj.7600672;
RA Santos-Rosa H., Leung J., Grimsey N., Peak-Chew S., Siniossoglou S.;
RT "The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane
RT growth.";
RL EMBO J. 24:1931-1941(2005).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION AT SER-110; SER-114; SER-168; SER-602;
RP THR-723; SER-744 AND SER-748.
RX PubMed=16968695; DOI=10.1074/jbc.m606654200;
RA O'Hara L., Han G.S., Peak-Chew S., Grimsey N., Carman G.M.,
RA Siniossoglou S.;
RT "Control of phospholipid synthesis by phosphorylation of the yeast lipin
RT Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase.";
RL J. Biol. Chem. 281:34537-34548(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=16467296; DOI=10.1074/jbc.m600425200;
RA Han G.S., Wu W.I., Carman G.M.;
RT "The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent
RT phosphatidate phosphatase enzyme.";
RL J. Biol. Chem. 281:9210-9218(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-80; ASP-398 AND
RP ASP-400.
RX PubMed=17971454; DOI=10.1074/jbc.m705777200;
RA Han G.S., Siniossoglou S., Carman G.M.;
RT "The cellular functions of the yeast lipin homolog PAH1p are dependent on
RT its phosphatidate phosphatase activity.";
RL J. Biol. Chem. 282:37026-37035(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602; SER-744 AND SER-748, 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 [11]
RP IDENTIFICATION BY 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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=17910939; DOI=10.1016/j.ab.2007.08.037;
RA Havriluk T., Lozy F., Siniossoglou S., Carman G.M.;
RT "Colorimetric determination of pure Mg(2+)-dependent phosphatidate
RT phosphatase activity.";
RL Anal. Biochem. 373:392-394(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602; SER-744; SER-748 AND
RP THR-816, AND 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-602; SER-744;
RP SER-748; SER-773; SER-774; SER-810; SER-814; SER-844 AND SER-847, AND
RP 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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN, AND MUTAGENESIS OF
RP LEU-8; VAL-11 AND TRP-15.
RX PubMed=20876142; DOI=10.1073/pnas.1007974107;
RA Karanasios E., Han G.S., Xu Z., Carman G.M., Siniossoglou S.;
RT "A phosphorylation-regulated amphipathic helix controls the membrane
RT translocation and function of the yeast phosphatidate phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17539-17544(2010).
RN [16]
RP FUNCTION, AND PHOSPHORYLATION AT SER-602; THR-723 AND SER-744.
RX PubMed=21081492; DOI=10.1074/jbc.m110.155598;
RA Choi H.S., Su W.M., Morgan J.M., Han G.S., Xu Z., Karanasios E.,
RA Siniossoglou S., Carman G.M.;
RT "Phosphorylation of phosphatidate phosphatase regulates its membrane
RT association and physiological functions in Saccharomyces cerevisiae:
RT identification of SER(602), THR(723), AND SER(744) as the sites
RT phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase.";
RL J. Biol. Chem. 286:1486-1498(2011).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF GLY-80; ASP-398 AND ASP-400.
RX PubMed=21422231; DOI=10.1083/jcb.201010111;
RA Adeyo O., Horn P.J., Lee S., Binns D.D., Chandrahas A., Chapman K.D.,
RA Goodman J.M.;
RT "The yeast lipin orthologue Pah1p is important for biogenesis of lipid
RT droplets.";
RL J. Cell Biol. 192:1043-1055(2011).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-496 AND LYS-801, AND
RP MUTAGENESIS OF LYS-496 AND LYS-801.
RX PubMed=29765047; DOI=10.1038/s41467-018-04363-w;
RA Li T.Y., Song L., Sun Y., Li J., Yi C., Lam S.M., Xu D., Zhou L., Li X.,
RA Yang Y., Zhang C.S., Xie C., Huang X., Shui G., Lin S.Y., Reue K.,
RA Lin S.C.;
RT "Tip60-mediated lipin 1 acetylation and ER translocation determine
RT triacylglycerol synthesis rate.";
RL Nat. Commun. 9:1916-1916(2018).
CC -!- FUNCTION: Mg(2+)-dependent phosphatidate (PA) phosphatase which
CC catalyzes the dephosphorylation of PA to yield diacylglycerol
CC (PubMed:16467296, PubMed:16968695, PubMed:17910939, PubMed:17971454,
CC PubMed:20876142, PubMed:21081492, PubMed:29765047). Required for de
CC novo lipid synthesis and formation of lipid droplets (PubMed:21422231).
CC Controls transcription of phospholipid biosynthetic genes and nuclear
CC structure by regulating the amount of membrane present at the nuclear
CC envelope (PubMed:15889145). Involved in plasmid maintenance, in
CC respiration and in cell proliferation (PubMed:8437575).
CC {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:16467296,
CC ECO:0000269|PubMed:16968695, ECO:0000269|PubMed:17910939,
CC ECO:0000269|PubMed:17971454, ECO:0000269|PubMed:20876142,
CC ECO:0000269|PubMed:21081492, ECO:0000269|PubMed:21422231,
CC ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:8437575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000269|PubMed:16467296, ECO:0000269|PubMed:17910939,
CC ECO:0000269|PubMed:17971454, ECO:0000269|PubMed:29765047};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16467296};
CC -!- ACTIVITY REGULATION: Phenylglyoxal and propranolol inhibit activity in
CC dose-dependent manners with IC(50) values of 1.3 mM and 0.2 mM,
CC respectively. {ECO:0000269|PubMed:17910939}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Peripheral membrane
CC protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
CC -!- DOMAIN: The N-terminal amphipathic helix (residues 1 to 18) is involved
CC in the membrane recruitment. {ECO:0000269|PubMed:20876142}.
CC -!- DOMAIN: Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC motif essential for phosphatidate phosphatase activity.
CC {ECO:0000269|PubMed:20876142}.
CC -!- PTM: Acetylation at Lys-496 and Lys-801 by ESA1 promotes synthesis of
CC diacylglycerol. {ECO:0000269|PubMed:29765047}.
CC -!- PTM: Phosphorylated by CDC28 at the onset of mitosis, and
CC dephosphorylated by the NEM1-SPO7 complex. Phosphorylation regulates
CC recruitment on promoters of lipid biosynthetic enzymes.
CC {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:16968695,
CC ECO:0000269|PubMed:20876142, ECO:0000269|PubMed:21081492}.
CC -!- MISCELLANEOUS: Present with 3910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
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DR EMBL; D01095; BAA00880.1; -; Genomic_DNA.
DR EMBL; Z49705; CAA89801.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10061.1; -; Genomic_DNA.
DR PIR; S30911; S30911.
DR RefSeq; NP_013888.1; NM_001182669.1.
DR AlphaFoldDB; P32567; -.
DR SMR; P32567; -.
DR BioGRID; 35343; 224.
DR DIP; DIP-1454N; -.
DR IntAct; P32567; 10.
DR MINT; P32567; -.
DR STRING; 4932.YMR165C; -.
DR SwissLipids; SLP:000000045; -.
DR iPTMnet; P32567; -.
DR MaxQB; P32567; -.
DR PaxDb; P32567; -.
DR PRIDE; P32567; -.
DR EnsemblFungi; YMR165C_mRNA; YMR165C; YMR165C.
DR GeneID; 855201; -.
DR KEGG; sce:YMR165C; -.
DR SGD; S000004775; PAH1.
DR VEuPathDB; FungiDB:YMR165C; -.
DR eggNOG; KOG2116; Eukaryota.
DR GeneTree; ENSGT00940000168260; -.
DR HOGENOM; CLU_002546_3_1_1; -.
DR InParanoid; P32567; -.
DR OMA; TWSSINP; -.
DR BioCyc; MetaCyc:G3O-32855-MON; -.
DR BioCyc; YEAST:G3O-32855-MON; -.
DR BRENDA; 3.1.3.4; 984.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR Reactome; R-SCE-1483213; Synthesis of PE.
DR Reactome; R-SCE-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-SCE-75109; Triglyceride biosynthesis.
DR PRO; PR:P32567; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32567; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IDA:SGD.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:SGD.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0034389; P:lipid droplet organization; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
DR GO; GO:0006276; P:plasmid maintenance; IMP:SGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR026058; LIPIN.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR InterPro; IPR031315; LNS2/PITP.
DR PANTHER; PTHR12181; PTHR12181; 2.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..862
FT /note="Phosphatidic acid phosphohydrolase 1"
FT /id="PRO_0000209887"
FT REGION 19..104
FT /note="N-LIP"
FT REGION 104..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 398..402
FT /note="DXDXT motif"
FT COMPBIAS 104..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16968695"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16968695"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16968695"
FT MOD_RES 496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:29765047"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 602
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16968695,
FT ECO:0000269|PubMed:21081492, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 723
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16968695,
FT ECO:0000269|PubMed:21081492"
FT MOD_RES 744
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16968695,
FT ECO:0000269|PubMed:21081492, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16968695,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 801
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:29765047"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 816
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 8
FT /note="L->A: Impairs membrane recruitiment; when associated
FT with A-11 and A-15."
FT /evidence="ECO:0000269|PubMed:20876142"
FT MUTAGEN 11
FT /note="V->A: Impairs membrane recruitiment; when associated
FT with A-8 and A-15."
FT /evidence="ECO:0000269|PubMed:20876142"
FT MUTAGEN 15
FT /note="W->A: Impairs membrane recruitiment; when associated
FT with A-8 and A-11."
FT /evidence="ECO:0000269|PubMed:20876142"
FT MUTAGEN 80
FT /note="G->R: Impairs phosphatidate phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17971454,
FT ECO:0000269|PubMed:21422231"
FT MUTAGEN 398
FT /note="D->E: Impairs phosphatidate phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17971454,
FT ECO:0000269|PubMed:21422231"
FT MUTAGEN 400
FT /note="D->E: Impairs phosphatidate phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17971454,
FT ECO:0000269|PubMed:21422231"
FT MUTAGEN 496
FT /note="K->R: Abolished acetylation by ESA1, leading to
FT decreased diacylglycerol synthesis; when associated with R-
FT 801."
FT /evidence="ECO:0000269|PubMed:29765047"
FT MUTAGEN 801
FT /note="K->R: Abolished acetylation by ESA1, leading to
FT decreased diacylglycerol synthesis; when associated with R-
FT 496."
FT /evidence="ECO:0000269|PubMed:29765047"
SQ SEQUENCE 862 AA; 95031 MW; 28132EED1906ACBD CRC64;
MQYVGRALGS VSKTWSSINP ATLSGAIDVI VVEHPDGRLS CSPFHVRFGK FQILKPSQKK
VQVFINEKLS NMPMKLSDSG EAYFVFEMGD QVTDVPDELL VSPVMSATSS PPQSPETSIL
EGGTEGEGEG ENENKKKEKK VLEEPDFLDI NDTGDSGSKN SETTGSLSPT ESSTTTPPDS
VEERKLVEQR TKNFQQKLNK KLTEIHIPSK LDNNGDLLLD TEGYKPNKNM MHDTDIQLKQ
LLKDEFGNDS DISSFIKEDK NGNIKIVNPY EHLTDLSPPG TPPTMATSGS VLGLDAMESG
STLNSLSSSP SGSDTEDETS FSKEQSSKSE KTSKKGTAGS GETEKRYIRT IRLTNDQLKC
LNLTYGENDL KFSVDHGKAI VTSKLFVWRW DVPIVISDID GTITKSDALG HVLAMIGKDW
THLGVAKLFS EISRNGYNIL YLTARSAGQA DSTRSYLRSI EQNGSKLPNG PVILSPDRTM
AALRREVILK KPEVFKIACL NDIRSLYFED SDNEVDTEEK STPFFAGFGN RITDALSYRT
VGIPSSRIFT INTEGEVHME LLELAGYRSS YIHINELVDH FFPPVSLDSV DLRTNTSMVP
GSPPNRTLDN FDSEITSGRK TLFRGNQEEK FTDVNFWRDP LVDIDNLSDI SNDDSDNIDE
DTDVSQQSNI SRNRANSVKT AKVTKAPQRN VSGSTNNNEV LAASSDVENA SDLVSSHSSS
GSTPNKSTMS KGDIGKQIYL ELGSPLASPK LRYLDDMDDE DSNYNRTKSR RASSAAATSI
DKEFKKLSVS KAGAPTRIVS KINVSNDVHS LGNSDTESRR EQSVNETGRN QLPHNSMDDK
DLDSRVSDEF DDDEFDEDEF ED
