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 11-DEC-2019, entry version 164. DE RecName: Full=Sterol esterase TGL1; DE EC=3.1.1.13; 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; 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. 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, SUBCELLULAR LOCATION, LACK OF GLYCOSYLATION, AND MEMBRANE RP TOPOLOGY. 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 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 [14] 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). CC -!- FUNCTION: Mediates the hydrolysis of steryl esters. Required for CC mobilization of steryl ester, thereby playing a central role in lipid CC metabolism. May have weak lipase activity toward triglycerides upon CC some conditions, however, the relevance of such activity is unclear in CC vivo. {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:14640980, CC ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:15922657}. 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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. CC Lipid droplet. CC -!- PTM: Not N-glycosylated. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 BioGrid; 33996; 70. 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 EuPathDB; FungiDB:YKL140W; -. DR SGD; S000001623; TGL1. DR HOGENOM; HOG000173756; -. DR InParanoid; P34163; -. DR KO; K01052; -. DR OMA; GANDWMC; -. DR BioCyc; MetaCyc:YKL140W-MONOMER; -. DR BioCyc; YEAST:YKL140W-MONOMER; -. 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 Hydrolase; Isopeptide bond; Lipid degradation; Lipid droplet; KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; KW Signal-anchor; 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:0000255" FT TRANSMEM 14..34 FT /note="Helical; Signal-anchor for type III membrane FT protein" FT /evidence="ECO:0000255" FT TOPO_DOM 35..548 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 107..402 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 201 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 369 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 396 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT MOD_RES 462 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 466 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 521 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17287358" FT MOD_RES 538 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 539 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:19779198" FT CROSSLNK 246 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000244|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 //