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 20-JAN-2016, entry version 131. 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; OC Saccharomycetes; 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 RT chromosome XI of Saccharomyces cerevisiae reveals five tightly linked RT 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., RA Bossier P., 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., RA Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., RA Zimmermann J., Haasemann M., 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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 RT of 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., RA Dephoure N., 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 RT and/or 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 RT for 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 RP 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 RT 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-466; SER-538 RP AND THR-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT insights into evolution."; RL Science 325:1682-1686(2009). RN [14] RP IDENTIFICATION BY 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 CC lipid metabolism. May have weak lipase activity toward CC triglycerides upon some conditions, however, the relevance of such CC activity is unclear in vivo. {ECO:0000269|PubMed:10515935, CC ECO:0000269|PubMed:14640980, ECO:0000269|PubMed:15713625, CC ECO:0000269|PubMed:15922657}. CC -!- CATALYTIC ACTIVITY: A steryl ester + H(2)O = a sterol + a fatty CC acid. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane CC protein. Lipid droplet. CC -!- PTM: Not N-glycosylated. CC -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. CC {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 ProteinModelPortal; P34163; -. DR SMR; P34163; 66-417. DR BioGrid; 33996; 37. DR DIP; DIP-6306N; -. DR IntAct; P34163; 11. DR MINT; MINT-4493007; -. DR ESTHER; yeast-tgl1; Acidic_Lipase. DR iPTMnet; P34163; -. DR MaxQB; P34163; -. DR EnsemblFungi; YKL140W; YKL140W; YKL140W. DR GeneID; 853717; -. DR KEGG; sce:YKL140W; -. DR EuPathDB; FungiDB:YKL140W; -. DR SGD; S000001623; TGL1. DR GeneTree; ENSGT00550000074328; -. DR HOGENOM; HOG000173756; -. DR InParanoid; P34163; -. DR KO; K01052; -. DR OMA; ICIGFSQ; -. DR OrthoDB; EOG790G8X; -. DR BioCyc; MetaCyc:YKL140W-MONOMER; -. DR BioCyc; YEAST:YKL140W-MONOMER; -. DR BRENDA; 3.1.1.13; 984. DR NextBio; 974734; -. DR PRO; PR:P34163; -. DR Proteomes; UP000002311; Chromosome XI. DR GO; GO:0016021; C:integral component of membrane; IDA:SGD. DR GO; GO:0005811; C:lipid particle; IDA:SGD. DR GO; GO:0016298; F:lipase activity; ISS: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 SUPFAM; SSF53474; SSF53474; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Lipid degradation; Lipid droplet; KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1 548 Sterol esterase TGL1. FT /FTId=PRO_0000090379. FT TOPO_DOM 1 13 Lumenal. {ECO:0000255}. FT TRANSMEM 14 34 Helical; Signal-anchor for type III FT membrane protein. {ECO:0000255}. FT TOPO_DOM 35 548 Cytoplasmic. {ECO:0000255}. FT ACT_SITE 201 201 Nucleophile. {ECO:0000250}. FT ACT_SITE 369 369 Charge relay system. {ECO:0000250}. FT ACT_SITE 396 396 Charge relay system. {ECO:0000250}. FT MOD_RES 462 462 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 466 466 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 521 521 Phosphoserine. FT {ECO:0000244|PubMed:17287358}. FT MOD_RES 538 538 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 539 539 Phosphothreonine. FT {ECO:0000244|PubMed:19779198}. 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 //