YP147_YEAST
ID YP147_YEAST Reviewed; 304 AA.
AC Q06522; D6W4E4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Lipid droplet-associated triacylglycerol lipase {ECO:0000305};
DE Short=TAG lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:29491250};
GN OrderedLocusNames=YPR147C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29491250; DOI=10.2323/jgam.2017.08.001;
RA Naresh Kumar M., Thunuguntla V.B.S.C., Chandra Sekhar B., Bondili J.S.;
RT "Saccharomyces cerevisiae lipid droplet associated enzyme Ypr147cp shows
RT both TAG lipase and ester hydrolase activities.";
RL J. Gen. Appl. Microbiol. 64:76-83(2018).
CC -!- FUNCTION: Shows both triacylglycerol (TAG) lipase and ester hydrolase
CC activities. May play a role in TAG homeostasis.
CC {ECO:0000269|PubMed:29491250}.
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:29491250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.07 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:29491250};
CC KM=14.79 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:29491250};
CC Note=kcat is 0.87 sec(-1) with p-nitrophenyl acetat as substrate and
CC 0.44 sec(-1) with p-nitrophenyl butyrate as substrate.
CC {ECO:0000269|PubMed:29491250};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:29491250};
CC Temperature dependence:
CC Optimum temperature is 30X degrees Celsius.
CC {ECO:0000269|PubMed:29491250};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24868093}.
CC Membrane {ECO:0000255}; Peripheral membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Accumulates lipid droplets.
CC {ECO:0000269|PubMed:29491250}.
CC -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. LDAH family.
CC {ECO:0000305}.
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DR EMBL; U40829; AAB68285.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11560.1; -; Genomic_DNA.
DR PIR; S69034; S69034.
DR RefSeq; NP_015473.1; NM_001184244.1.
DR AlphaFoldDB; Q06522; -.
DR SMR; Q06522; -.
DR BioGRID; 36315; 17.
DR IntAct; Q06522; 1.
DR STRING; 4932.YPR147C; -.
DR SwissLipids; SLP:000001910; -.
DR ESTHER; yeast-YPR147C; LIDHydrolase.
DR MaxQB; Q06522; -.
DR PaxDb; Q06522; -.
DR PRIDE; Q06522; -.
DR EnsemblFungi; YPR147C_mRNA; YPR147C; YPR147C.
DR GeneID; 856270; -.
DR KEGG; sce:YPR147C; -.
DR SGD; S000006351; YPR147C.
DR VEuPathDB; FungiDB:YPR147C; -.
DR eggNOG; KOG3975; Eukaryota.
DR GeneTree; ENSGT00390000009688; -.
DR HOGENOM; CLU_018394_1_1_1; -.
DR InParanoid; Q06522; -.
DR OMA; YFVTGNP; -.
DR BioCyc; YEAST:G3O-34279-MON; -.
DR PRO; PR:Q06522; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06522; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
DR GO; GO:0019915; P:lipid storage; 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 InterPro; IPR019363; LDAH.
DR PANTHER; PTHR13390; PTHR13390; 1.
DR Pfam; PF10230; LIDHydrolase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Lipid droplet; Membrane; Reference proteome.
FT CHAIN 1..304
FT /note="Lipid droplet-associated triacylglycerol lipase"
FT /id="PRO_0000257828"
FT TOPO_DOM 1..155
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29491250"
FT INTRAMEM 156..176
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..304
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29491250"
FT MOTIF 107..111
FT /note="GXSXG"
FT /evidence="ECO:0000255"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 304 AA; 34842 MW; B37EE95D46F44F34 CRC64;
MTVKEYTKSK LPCSILNIKP TVTKSGEDAP LLVWIPGNPG LLYYYQEMLH HLHLKHPDWE
ILGISHAGMT LNAHSNTPIF SLQDQVDHQV EVINNFSCKN RKIIIMGHSV GAYIVQKVCL
SNKLVGSVQK VGLVTPTVMD IHTSEMGIKM TAALRYIPPL AHVVSLFSYI FFYWILSEGF
SRFIIDKFMG CGSTGYQAVL STRIFLTHRQ FVRQSLGLAA QEMEEITTNW EFQDRFINYC
EENGISIWFL FSSNDHWVSG KTRSHLSDYY KDKVKQERLK IDVTDKIPHS FVVKHAEYAI
NAFF
