TGL1_YEAST
ID TGL1_YEAST Reviewed; 548 AA.
AC P34163; D6VX56;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Sterol esterase TGL1;
DE EC=3.1.1.13 {ECO:0000269|PubMed:15713625};
DE AltName: Full=Triglyceride lipase-cholesterol esterase 1;
GN Name=TGL1; OrderedLocusNames=YKL140W; ORFNames=YKL5;
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=1574929; DOI=10.1002/yea.320080309;
RA Abraham P.R., Mulder A., Van'T Riet J., Planta R.J., Raue H.A.;
RT "Molecular cloning and physical analysis of an 8.2 kb segment of chromosome
RT XI of Saccharomyces cerevisiae reveals five tightly linked genes.";
RL Yeast 8:227-238(1992).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
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 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 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.
RX PubMed=14640980; DOI=10.1042/bj20031064;
RA Ferreira T., Regnacq M., Alimardani P., Moreau-Vauzelle C., Berges T.;
RT "Lipid dynamics in yeast under haem-induced unsaturated fatty acid and/or
RT sterol depletion.";
RL Biochem. J. 378:899-908(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15922657; DOI=10.1016/j.bbalip.2005.04.005;
RA Jandrositz A., Petschnigg J., Zimmermann R., Natter K., Scholze H.,
RA Hermetter A., Kohlwein S.D., Leber R.;
RT "The lipid droplet enzyme Tgl1p hydrolyzes both steryl esters and
RT triglycerides in the yeast, Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1735:50-58(2005).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND LACK OF
RP GLYCOSYLATION.
RX PubMed=15713625; DOI=10.1128/mcb.25.5.1655-1668.2005;
RA Koeffel R., Tiwari R., Falquet L., Schneiter R.;
RT "The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes
RT encode a novel family of membrane-anchored lipases that are required for
RT steryl ester hydrolysis.";
RL Mol. Cell. Biol. 25:1655-1668(2005).
RN [10]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, 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 [12]
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 [13]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=19111628; DOI=10.1016/j.bbalip.2008.11.004;
RA Wagner A., Grillitsch K., Leitner E., Daum G.;
RT "Mobilization of steryl esters from lipid particles of the yeast
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1791:118-124(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-466; SER-538 AND
RP THR-539, 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 [15]
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 [16]
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 [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [18]
RP ACETYLATION AT MET-1, AND SUBCELLULAR LOCATION.
RX PubMed=23613772; DOI=10.1371/journal.pone.0061012;
RA Aksnes H., Osberg C., Arnesen T.;
RT "N-terminal acetylation by NatC is not a general determinant for substrate
RT subcellular localization in Saccharomyces cerevisiae.";
RL PLoS ONE 8:e61012-e61012(2013).
RN [19]
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).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=28866104; DOI=10.1016/j.bbalip.2017.08.009;
RA Klein I., Korber M., Athenstaedt K., Daum G.;
RT "The impact of nonpolar lipids on the regulation of the steryl ester
RT hydrolases Tgl1p and Yeh1p in the yeast Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1862:1491-1501(2017).
CC -!- FUNCTION: Mediates the hydrolysis of steryl esters (SE)
CC (PubMed:10515935, PubMed:14640980, PubMed:15713625). Preferentially
CC hydrolyzes ergosteryl and zymosteryl esters (PubMed:19111628). Required
CC for mobilization of SEs from lipid particles/droplets, thereby playing
CC a central role in lipid metabolism and sterol homeostasis. Sterol
CC intermediates stored in SE and set free by SE hydrolases are recycled
CC to the sterol biosynthetic pathway and converted to the final product,
CC ergosterol, in the endoplasmic reticulum. Has also weak lipase activity
CC toward triglycerides at neutral pH, however, the physiological
CC relevance of this activity is unclear (PubMed:15922657,
CC PubMed:19111628, PubMed:28866104). {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:14640980, ECO:0000269|PubMed:15713625,
CC ECO:0000269|PubMed:15922657, ECO:0000269|PubMed:19111628,
CC ECO:0000269|PubMed:28866104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+);
CC Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13;
CC Evidence={ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:15922657,
CC ECO:0000269|PubMed:28866104};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:15922657};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:15922657,
CC ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:23613772,
CC ECO:0000269|PubMed:24868093, ECO:0000269|PubMed:28866104}. Membrane
CC {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CC Note=Partially retained in the endoplasmic reticulum in cells lacking
CC triacylglycerols and consequently lipid droplets.
CC {ECO:0000269|PubMed:28866104}.
CC -!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:15713625}.
CC -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; Z25464; CAA80958.1; -; Genomic_DNA.
DR EMBL; Z28140; CAA81981.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09022.1; -; Genomic_DNA.
DR PIR; S37969; S37969.
DR RefSeq; NP_012782.1; NM_001179706.1.
DR AlphaFoldDB; P34163; -.
DR SMR; P34163; -.
DR BioGRID; 33996; 72.
DR DIP; DIP-6306N; -.
DR IntAct; P34163; 12.
DR MINT; P34163; -.
DR STRING; 4932.YKL140W; -.
DR ESTHER; yeast-tgl1; Acidic_Lipase.
DR iPTMnet; P34163; -.
DR MaxQB; P34163; -.
DR PaxDb; P34163; -.
DR PRIDE; P34163; -.
DR TopDownProteomics; P34163; -.
DR EnsemblFungi; YKL140W_mRNA; YKL140W; YKL140W.
DR GeneID; 853717; -.
DR KEGG; sce:YKL140W; -.
DR SGD; S000001623; TGL1.
DR VEuPathDB; FungiDB:YKL140W; -.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_5_0_1; -.
DR InParanoid; P34163; -.
DR OMA; DGEHVDC; -.
DR BioCyc; MetaCyc:YKL140W-MON; -.
DR BioCyc; YEAST:YKL140W-MON; -.
DR BRENDA; 3.1.1.13; 984.
DR PRO; PR:P34163; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34163; protein.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0004771; F:sterol esterase activity; IDA:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Isopeptide bond; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..548
FT /note="Sterol esterase TGL1"
FT /id="PRO_0000090379"
FT TOPO_DOM 1..13
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15713625"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15713625"
FT DOMAIN 107..402
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 449..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 199..203
FT /note="GXSXG"
FT /evidence="ECO:0000305|Ref.16"
FT COMPBIAS 449..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT ACT_SITE 396
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P80035"
FT MOD_RES 1
FT /note="N-acetylmethionine; partial"
FT /evidence="ECO:0000305|PubMed:23613772"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 539
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 548 AA; 62979 MW; 32D1F230701CB083 CRC64;
MYFPFLGRLS ITDYIIVVLV YIESIISSVL KLIPQPMINL FEWLINFSTS SDDNTIEEKL
RSAPTIHEMC AIFDISVEDH LVRTEDNYIL TLHRIPPISK NRFNNKVVYL HHGLLMCSDV
WCCNIERHKN LPFVLHDLGY DVWMGNNRGN KYSTAHLNKP PKSNKFWDFS IDEFAFFDIP
NSIEFILDIT KVDKVICIGF SQGSAQMFAA FSLSEKLNRK VSHFIAIAPA MTPKGLHNRI
VDTLAKSSPG FMYLFFGRKI VLPSAVIWQR TLHPTLFNLC IDIANKILFN WKSFNILPRQ
KIASYAKLYS TTSVKSIVHW FQILRSQKFQ MFEESDNMLN SLTRPYQIAN FPTRTNIKIP
ILLIYGGIDS LVDIDVMKKN LPFNSVFDVK VDNYEHLDLI WGKDADTLVI AKVLRFIEFF
NPGNVSVKTN QLLPSASLVE ELPSTTWKTT HPTHGLSYRT HSADRSPLSV QADEADEVHN
ADNSRFLRRV FSTSAIDEDN ENEHQDDTED QIHKEQQRRL SAYLESSKDL RQLDANSSTT
ALDALNKE
