TGL2_YEAST
ID TGL2_YEAST Reviewed; 326 AA.
AC P54857; D6VS44; E9P8S6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Triacylglycerol lipase 2;
DE EC=3.1.1.3 {ECO:0000269|PubMed:9544243};
DE AltName: Full=Lipase 2;
DE AltName: Full=Neutral lipid hydrolase {ECO:0000303|PubMed:31483742};
GN Name=TGL2; OrderedLocusNames=YDR058C; ORFNames=D4225, YD9609.12C;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=S288c / SNY243;
RX PubMed=9544243;
RX DOI=10.1002/(sici)1097-0061(199802)14:3<225::aid-yea215>3.0.co;2-#;
RA van Heusden G.P.H., Nebohacova M., Overbeeke T.L.A., Steensma H.Y.;
RT "The Saccharomyces cerevisiae TGL2 gene encodes a protein with lipolytic
RT activity and can complement an Escherichia coli diacylglycerol kinase
RT disruptant.";
RL Yeast 14:225-232(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8789263;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA Brandt P., Ramlow S., Otto B., Bloecker H.;
RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT Saccharomyces cerevisiae chromosome IV.";
RL Yeast 12:85-90(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19959834; DOI=10.1074/jbc.m109.046946;
RA Ham H.J., Rho H.J., Shin S.K., Yoon H.J.;
RT "The TGL2 gene of Saccharomyces cerevisiae encodes an active acylglycerol
RT lipase located in the mitochondria.";
RL J. Biol. Chem. 285:3005-3013(2010).
RN [7]
RP LIPASE 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 [8]
RP CATALYTIC ACTIVITY.
RX PubMed=28119444; DOI=10.1194/jlr.d074385;
RA Ham H.J., Seo J., Yoon H.J., Shin S.K.;
RT "Label-free measurement of the yeast short chain TAG lipase activity by
RT ESI-MS after one-step esterification.";
RL J. Lipid Res. 58:625-631(2017).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MIA40.
RX PubMed=31483742; DOI=10.1091/mbc.e19-03-0166;
RA Odendall F., Backes S., Tatsuta T., Weill U., Schuldiner M., Langer T.,
RA Herrmann J.M., Rapaport D., Dimmer K.S.;
RT "The mitochondrial intermembrane space-facing proteins Mcp2 and Tgl2 are
RT involved in yeast lipid metabolism.";
RL Mol. Biol. Cell 30:2681-2694(2019).
CC -!- FUNCTION: Mitochondrial triacylglycerol (TAG) lipase with activity
CC toward long-chain diacylglycerols (DAGs) and triacylglycerols (TAGs)
CC (PubMed:9544243, PubMed:19959834). Involved in mitochondrial lipid
CC metabolism (PubMed:31483742). {ECO:0000269|PubMed:19959834,
CC ECO:0000269|PubMed:31483742, ECO:0000269|PubMed:9544243}.
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:9544243};
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:19959834};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:19959834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:19959834};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:19959834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:19959834,
CC ECO:0000269|PubMed:28119444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000305|PubMed:19959834, ECO:0000305|PubMed:28119444};
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:19959834};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869;
CC Evidence={ECO:0000305|PubMed:19959834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dioctanoylglycerol + H2O = H(+) + octanoate +
CC octanoylglycerol; Xref=Rhea:RHEA:47880, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:88066,
CC ChEBI:CHEBI:88070; Evidence={ECO:0000269|PubMed:19959834,
CC ECO:0000269|PubMed:28119444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47881;
CC Evidence={ECO:0000305|PubMed:19959834, ECO:0000305|PubMed:28119444};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:9544243};
CC -!- SUBUNIT: Interacts with MIA40; forms mixed disulfide intermediates with
CC MIA40. {ECO:0000269|PubMed:31483742}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19959834}.
CC Mitochondrion intermembrane space {ECO:0000269|PubMed:31483742}.
CC Note=Imported into the IMS via the MIA40 disulfide relay system.
CC {ECO:0000269|PubMed:31483742}.
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DR EMBL; X98000; CAA66637.1; -; Genomic_DNA.
DR EMBL; X84162; CAA58974.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89087.1; -; Genomic_DNA.
DR EMBL; Z74354; CAA98876.1; -; Genomic_DNA.
DR EMBL; AY557691; AAS56017.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11904.1; -; Genomic_DNA.
DR PIR; S54042; S54042.
DR RefSeq; NP_010343.1; NM_001180366.1.
DR AlphaFoldDB; P54857; -.
DR SMR; P54857; -.
DR BioGRID; 32111; 164.
DR MINT; P54857; -.
DR STRING; 4932.YDR058C; -.
DR SwissLipids; SLP:000001353; -.
DR ESTHER; yeast-tgl2; PGAP1.
DR MaxQB; P54857; -.
DR PaxDb; P54857; -.
DR PRIDE; P54857; -.
DR EnsemblFungi; YDR058C_mRNA; YDR058C; YDR058C.
DR GeneID; 851628; -.
DR KEGG; sce:YDR058C; -.
DR SGD; S000002465; TGL2.
DR VEuPathDB; FungiDB:YDR058C; -.
DR eggNOG; ENOG502QQNH; Eukaryota.
DR HOGENOM; CLU_015737_0_0_1; -.
DR InParanoid; P54857; -.
DR OMA; RYMISHL; -.
DR BioCyc; YEAST:YDR058C-MON; -.
DR Reactome; R-SCE-1483115; Hydrolysis of LPC.
DR Reactome; R-SCE-8964058; HDL remodeling.
DR PRO; PR:P54857; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P54857; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..326
FT /note="Triacylglycerol lipase 2"
FT /id="PRO_0000090380"
FT MOTIF 142..146
FT /note="(A/G)XSXG lipase motif"
FT /evidence="ECO:0000305|Ref.7"
FT CONFLICT 104
FT /note="K -> N (in Ref. 5; AAS56017)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="R -> H (in Ref. 1; CAA66637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37500 MW; 3D2421611ED72CE9 CRC64;
MKNDNKANDI IIDSVKVPDS YKPPKNPIVF CHGLSGFDKL ILIPSVFHLT NLISNSIVHN
MAENFMQDDE DKSDNKYTNL LEIEYWIGVK KFLQSKGCTV ITTKVPGFGS IEERAMALDA
QLQKEVKKIE SKDKRHSLNL IAHSMGGLDC RYLICNIKNR NYDILSLTTI STPHRGSEMA
DYVVDLFENL NALRVSQKIL PICFYQLTTA YMKYFNLVTP NSPKVSYFSY GCSFVPKWYN
VFCTPWKIVY ERSKGCPNDG LVTINSSKWG EYRGTLKDMD HLDVINWKNK LQDDWSKFFR
TTTVGEKVDI LNFYLKITDD LARKGF
