TGL5_YEAST
ID TGL5_YEAST Reviewed; 749 AA.
AC Q12043; D6W2E4; Q7LH13;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Triacylglycerol lipase 5;
DE Short=TAG lipase 5;
DE Short=TG lipase 5;
DE EC=3.1.1.3 {ECO:0000269|PubMed:16135509};
DE AltName: Full=Lipase 5;
GN Name=TGL5; Synonyms=STC2; OrderedLocusNames=YOR081C;
GN ORFNames=YOR29-32, YOR2964C;
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=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 435-749.
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
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, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16135509; DOI=10.1074/jbc.m507261200;
RA Athenstaedt K., Daum G.;
RT "Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces
RT cerevisiae are localized to lipid particles.";
RL J. Biol. Chem. 280:37301-37309(2005).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP ACTIVITY REGULATION.
RX PubMed=27170177; DOI=10.1091/mbc.e15-09-0633;
RA Klein I., Klug L., Schmidt C., Zandl M., Korber M., Daum G.,
RA Athenstaedt K.;
RT "Regulation of the yeast triacylglycerol lipases Tgl4p and Tgl5p by the
RT presence/absence of nonpolar lipids.";
RL Mol. Biol. Cell 27:2014-2024(2016).
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:16135509). Also catalyzes the acylation of
CC lysophosphatidic acid (LPA) (PubMed:20016004).
CC {ECO:0000269|PubMed:16135509, 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:16135509};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000269|PubMed:20016004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:20016004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:42592, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000269|PubMed:20016004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42593;
CC Evidence={ECO:0000305|PubMed:20016004};
CC -!- ACTIVITY REGULATION: Loses its lipolytic activity in cells lacking
CC nonpolar lipids, but retains its side activity as lysophospholipid
CC acyltransferase. {ECO:0000269|PubMed:27170177}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.7 uM for 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC {ECO:0000269|PubMed:20016004};
CC KM=29.3 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20016004};
CC Vmax=28.8 nmol/min/mg enzyme towards 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate {ECO:0000269|PubMed:20016004};
CC Vmax=38.1 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA
CC {ECO:0000269|PubMed:20016004};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:21820081,
CC ECO:0000269|PubMed:24868093, ECO:0000269|PubMed:27170177}.
CC Note=Partially retained in the endoplasmic reticulum in cells lacking
CC triacylglycerols. {ECO:0000269|PubMed:27170177}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X94335; CAA64004.1; -; Genomic_DNA.
DR EMBL; Z74989; CAA99274.1; -; Genomic_DNA.
DR EMBL; Z70678; CAA94566.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10860.1; -; Genomic_DNA.
DR PIR; S61643; S61643.
DR RefSeq; NP_014724.1; NM_001183500.1.
DR AlphaFoldDB; Q12043; -.
DR BioGRID; 34480; 66.
DR DIP; DIP-6280N; -.
DR IntAct; Q12043; 8.
DR MINT; Q12043; -.
DR STRING; 4932.YOR081C; -.
DR SwissLipids; SLP:000000054; -.
DR SwissLipids; SLP:000000673; -.
DR iPTMnet; Q12043; -.
DR MaxQB; Q12043; -.
DR PaxDb; Q12043; -.
DR PRIDE; Q12043; -.
DR EnsemblFungi; YOR081C_mRNA; YOR081C; YOR081C.
DR GeneID; 854248; -.
DR KEGG; sce:YOR081C; -.
DR SGD; S000005607; TGL5.
DR VEuPathDB; FungiDB:YOR081C; -.
DR eggNOG; KOG2214; Eukaryota.
DR GeneTree; ENSGT00940000176365; -.
DR HOGENOM; CLU_009031_4_0_1; -.
DR InParanoid; Q12043; -.
DR OMA; VTEWHDA; -.
DR BioCyc; MetaCyc:G3O-33618-MON; -.
DR BioCyc; YEAST:G3O-33618-MON; -.
DR PRO; PR:Q12043; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12043; protein.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0006642; P:triglyceride mobilization; IDA: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 Glycoprotein; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Sporulation.
FT CHAIN 1..749
FT /note="Triacylglycerol lipase 5"
FT /id="PRO_0000270918"
FT DOMAIN 183..388
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 585..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..59
FT /note="HXXXXD acyltransferase motif"
FT /evidence="ECO:0000305|PubMed:20016004, ECO:0000305|Ref.12"
FT MOTIF 214..218
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 602..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 749 AA; 84716 MW; F3C5DBA97B6BA58B CRC64;
MSNTLPVTEF LLSKYYELSN TPATDSSSLF KWLYHKTLSR KQLLISDLSS QKKHAISYDQ
WNDIASRLDD LTGLSEWKTI DESSLYNYKL LQDLTIRMRH LRTTHDYHRL LYLIRTKWVR
NLGNMNNVNL YRHSHTGTKQ IIHDYLEESQ AVLTALIHQS NMNDHYLLGI LQQTRRNIGR
TALVLSGGST FGLFHIGVLA ALFESDLMPK VISGSSAGAI VASIFCVHTT QEIPSLLTNV
LNMEFNIFND DNSKSPNENL LIKISRFCQN GTWFNNQPLI NTMLSFLGNL TFREAYNKTG
KILNITVSPA SIYEQPKLLN NLTAPNVLIW SAVCASCSLP GVFPSTPLFE KDPHTGKIKE
WGATNLHLSN MKFMDGSVDN DMPISRLSEM FNVDHIIACQ VNIHVFPLLK FSNTCVGGEI
EKEITARFRN QVTKIFKFFS DETIHFLDIL KELEFHPYLM TKLKHLFLQQ YSGNVTILPD
LSMVGQFHEV LKNPSQLFLL HQTTLGARAT WPKISMIQNN CGQEFALDKA ITFLKEKIII
SSSIKNPLQF YQPRFSEQIK SLSIMDADLP GVDLEESSSN SLSIIKSPNK TAAPGRFPLQ
PLPSPSSTFN KRKMDMLSPS PSPSTSPQRS KSSFTQQGTR QKANSLSFAI GASSLRLKKS
PLKVPSRPQF KKRSSYYNQN MSAEMRKNRK KSGTISSYDV QTNSEDFPIP AIENGSFDNT
LFNPSRFPMD AMSAATNDNF MNNSDIFQN
