TGL3_YEAST
ID TGL3_YEAST Reviewed; 642 AA.
AC P40308; D6W0E0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Triacylglycerol lipase 3;
DE EC=3.1.1.3 {ECO:0000269|PubMed:12682047};
DE AltName: Full=Lipase 3;
GN Name=TGL3; OrderedLocusNames=YMR313C; ORFNames=YM9924.05C;
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=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 [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 1-174.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7918444; DOI=10.1021/bi00206a028;
RA Heinemeyer W., Troendle N., Albrecht G., Wolf D.H.;
RT "PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits
RT from yeast? Indication for a set of 14 different subunits in the eukaryotic
RT proteasome core.";
RL Biochemistry 33:12229-12237(1994).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10515935; DOI=10.1128/jb.181.20.6441-6448.1999;
RA Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.;
RT "Identification and characterization of major lipid particle proteins of
RT the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:6441-6448(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12682047; DOI=10.1074/jbc.m302577200;
RA Athenstaedt K., Daum G.;
RT "YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid
RT particles of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:23317-23323(2003).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP SER-237.
RX PubMed=16267052; DOI=10.1074/jbc.m508414200;
RA Kurat C.F., Natter K., Petschnigg J., Wolinski H., Scheuringer K.,
RA Scholz H., Zimmermann R., Leber R., Zechner R., Kohlwein S.D.;
RT "Obese yeast: triglyceride lipolysis is functionally conserved from mammals
RT to yeast.";
RL J. Biol. Chem. 281:491-500(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20016004; DOI=10.1091/mbc.e09-09-0775;
RA Rajakumari S., Daum G.;
RT "Janus-faced enzymes yeast Tgl3p and Tgl5p catalyze lipase and
RT acyltransferase reactions.";
RL Mol. Biol. Cell 21:501-510(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015;
RA Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B.,
RA Wagner B., Karas M., Daum G.;
RT "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited:
RT lipidome meets proteome.";
RL Biochim. Biophys. Acta 1811:1165-1176(2011).
RN [10]
RP ACYLTRANSFERASE MOTIF.
RX DOI=10.1007/s11515-011-1142-6;
RA Grillitsch K., Daum G.;
RT "Triacylglycerol lipases of the yeast.";
RL Front. Biol. 6:219-230(2011).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=23673660; DOI=10.1074/jbc.m113.459610;
RA Schmidt C., Athenstaedt K., Koch B., Ploier B., Daum G.;
RT "Regulation of the yeast triacylglycerol lipase Tgl3p by formation of
RT nonpolar lipids.";
RL J. Biol. Chem. 288:19939-19948(2013).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=24868093; DOI=10.1194/jlr.m050229;
RA Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA Haas J., Walther T.C., Farese R.V. Jr.;
RT "High-confidence proteomic analysis of yeast lipid droplets identifies
RT additional droplet proteins and reveals connections to dolichol synthesis
RT and sterol acetylation.";
RL J. Lipid Res. 55:1465-1477(2014).
CC -!- FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The
CC lipid droplet/particle is a lipid storage compartment which serves as a
CC depot of energy and building blocks for membrane lipid biosynthesis.
CC Involved in the mobilization of the non-polar storage lipids
CC triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs,
CC releasing and supplying specific fatty acids to the appropriate
CC metabolic pathways (PubMed:10515935, PubMed:12682047, PubMed:16267052).
CC Also catalyzes the acylation of lysophosphatidic acid (LPA). Important
CC for efficient sporulation, but rather through its acyltransferase than
CC lipase activity (PubMed:20016004). {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:12682047, ECO:0000269|PubMed:16267052,
CC ECO:0000269|PubMed:20016004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:12682047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:12682047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:20016004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:16267052, ECO:0000305|PubMed:20016004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-
CC octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:16267052};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869;
CC Evidence={ECO:0000305|PubMed:16267052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37731, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64381, ChEBI:CHEBI:75238;
CC Evidence={ECO:0000269|PubMed:20016004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37732;
CC Evidence={ECO:0000305|PubMed:20016004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA =
CC 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37767, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75265;
CC Evidence={ECO:0000269|PubMed:20016004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37768;
CC Evidence={ECO:0000305|PubMed:20016004};
CC -!- ACTIVITY REGULATION: Loses its lipolytic activity in cells lacking
CC nonpolar lipids. {ECO:0000269|PubMed:23673660}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for 1-acyl-sn-glycero-3-phosphoethanolamine
CC {ECO:0000269|PubMed:20016004};
CC KM=18 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20016004};
CC Vmax=46.26 nmol/min/mg enzyme towards 1-acyl-sn-glycero-3-
CC phosphoethanolamine {ECO:0000269|PubMed:20016004};
CC Vmax=44.25 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA
CC {ECO:0000269|PubMed:20016004};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:12682047, ECO:0000269|PubMed:21820081,
CC ECO:0000269|PubMed:23673660, ECO:0000269|PubMed:24868093}.
CC Note=Partially retained in the endoplasmic reticulum in cells lacking
CC triacylglycerols. {ECO:0000269|PubMed:23673660}.
CC -!- DISRUPTION PHENOTYPE: A double deletion of TGL3 and TGL4, the 2 major
CC TGA lipases, leads to fat yeast, rendering growing cells unable to
CC degrade triglycerides. {ECO:0000269|PubMed:16267052}.
CC -!- MISCELLANEOUS: Present with 3210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z54141; CAA90831.1; -; Genomic_DNA.
DR EMBL; L34347; AAA53543.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10214.1; -; Genomic_DNA.
DR PIR; S59306; S59306.
DR RefSeq; NP_014044.1; NM_001182824.1.
DR AlphaFoldDB; P40308; -.
DR BioGRID; 35493; 88.
DR DIP; DIP-5641N; -.
DR IntAct; P40308; 3.
DR MINT; P40308; -.
DR STRING; 4932.YMR313C; -.
DR SwissLipids; SLP:000000052; -.
DR SwissLipids; SLP:000000671; -.
DR SwissLipids; SLP:000000678; -.
DR iPTMnet; P40308; -.
DR MaxQB; P40308; -.
DR PaxDb; P40308; -.
DR PRIDE; P40308; -.
DR EnsemblFungi; YMR313C_mRNA; YMR313C; YMR313C.
DR GeneID; 855361; -.
DR KEGG; sce:YMR313C; -.
DR SGD; S000004930; TGL3.
DR VEuPathDB; FungiDB:YMR313C; -.
DR eggNOG; KOG2214; Eukaryota.
DR GeneTree; ENSGT00940000176365; -.
DR HOGENOM; CLU_009031_5_0_1; -.
DR InParanoid; P40308; -.
DR BioCyc; MetaCyc:G3O-32977-MON; -.
DR BioCyc; YEAST:G3O-32977-MON; -.
DR PRO; PR:P40308; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40308; protein.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0071618; F:lysophosphatidylethanolamine acyltransferase activity; IDA:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0007114; P:cell budding; IMP:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:SGD.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..642
FT /note="Triacylglycerol lipase 3"
FT /id="PRO_0000203356"
FT DOMAIN 204..392
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 471..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 235..239
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 298..303
FT /note="HXXXXD acyltransferase motif"
FT /evidence="ECO:0000305|PubMed:20016004, ECO:0000305|Ref.10"
FT ACT_SITE 237
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 403
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12043"
FT MUTAGEN 237
FT /note="S->A: Abolishes TAG lipolytic activity."
FT /evidence="ECO:0000269|PubMed:16267052"
FT CONFLICT 96
FT /note="A -> P (in Ref. 3; AAA53543)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="R -> P (in Ref. 3; AAA53543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 73613 MW; A5AE059EF65465D1 CRC64;
MKETAQEYKV SAVIPTLLKN WILRVVYATL DHIPPFVWEI LHVITDIYFF WVQKLINYVR
PHSRVIYYNA IKKLDECDTY QMWCQQASVV DEITGANLWR RNFFSRRYDF NSVIEQYSIL
ENMLREEKYD VVKEKFSTTG PCMLRNFAGI GDKKLFTKSL MGTKLLIEQY LTRILEGLDI
LNNQTLTPTS FFQRCKLSLG TTALILQGGS LFGLFHLGVI RGLLLQDLMP NIISGSSMGA
CVASLFGCLS NEQLKQLLTD DNLLNIIKND VDLLKSCGYG NLEQHLNLGT LIQNLIHHGY
SQDVYLFIRF VMKYIVKEKT FEEVYQITGK VFNIVIHPTD KSCPNLLNYV TTPNVLIKSA
IECSLGSGVI SEDTSLLCKN LENEIEPFLN INKNKQVKFL TPENANNPSI TESPYTRLTE
LFNVNNFIVS LARPYLAPLV VNDLKHEIKT SKYYYYKHYP NMPPINANTV RKTQRSSSQS
PIKAGTVEDL EPEPLMSPVP PSSAVNDSAE YIIPELGIPQ LNFTEMEPLA FKFKYHLERK
LKNIATMEFR HRMEVLDNLG LLCSLIKRLI IDEKTPRSAT EIAVVPRMKS LSLTRIIEGQ
LNNIPYWIKS GERSTWPALA LIKTRCAVEF KLDDIIRARR SR
