UniProtKB - P40308 (TGL3_YEAST)
Protein
Triacylglycerol lipase 3
Gene
TGL3
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:10515935, PubMed:12682047, PubMed:16267052). Also catalyzes the acylation of lysophosphatidic acid (LPA). Important for efficient sporulation, but rather through its acyltransferase than lipase activity (PubMed:20016004).4 Publications
Miscellaneous
Present with 3210 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- EC:3.1.1.31 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphoethanolamine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphoethanolamine + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
- a 1-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
Loses its lipolytic activity in cells lacking nonpolar lipids.1 Publication
Kineticsi
- KM=19 µM for 1-acyl-sn-glycero-3-phosphoethanolamine1 Publication
- KM=18 µM for (9Z)-octadecenoyl-CoA1 Publication
- Vmax=46.26 nmol/min/mg enzyme towards 1-acyl-sn-glycero-3-phosphoethanolamine1 Publication
- Vmax=44.25 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 237 | NucleophilePROSITE-ProRule annotation | 1 | |
Active sitei | 403 | Proton acceptorBy similarity | 1 |
GO - Molecular functioni
- lysophosphatidylethanolamine acyltransferase activity Source: SGD
- triglyceride lipase activity Source: SGD
GO - Biological processi
- cell budding Source: SGD
- cellular lipid metabolic process Source: SGD
- triglyceride catabolic process Source: SGD
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid degradation, Lipid metabolism |
Enzyme and pathway databases
BioCyci | MetaCyc:G3O-32977-MONOMER YEAST:G3O-32977-MONOMER |
Chemistry databases
SwissLipidsi | SLP:000000052 SLP:000000671 SLP:000000678 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:TGL3 Ordered Locus Names:YMR313C ORF Names:YM9924.05C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000004930, TGL3 |
VEuPathDBi | FungiDB:YMR313C |
Subcellular locationi
Other locations
- Lipid droplet 5 Publications
Note: Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols.1 Publication
Other locations
- lipid droplet Source: SGD
Keywords - Cellular componenti
Lipid dropletPathology & Biotechi
Disruption phenotypei
A double deletion of TGL3 and TGL4, the 2 major TGA lipases, leads to fat yeast, rendering growing cells unable to degrade triglycerides.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 237 | S → A: Abolishes TAG lipolytic activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000203356 | 1 – 642 | Triacylglycerol lipase 3Add BLAST | 642 |
Proteomic databases
MaxQBi | P40308 |
PaxDbi | P40308 |
PRIDEi | P40308 |
PTM databases
iPTMneti | P40308 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 35493, 86 interactors |
DIPi | DIP-5641N |
IntActi | P40308, 3 interactors |
MINTi | P40308 |
STRINGi | 4932.YMR313C |
Miscellaneous databases
RNActi | P40308, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 204 – 392 | PNPLAPROSITE-ProRule annotationAdd BLAST | 189 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 235 – 239 | GXSXGPROSITE-ProRule annotation | 5 | |
Motifi | 298 – 303 | HXXXXD acyltransferase motif2 Publications | 6 |
Phylogenomic databases
eggNOGi | KOG2214, Eukaryota |
GeneTreei | ENSGT00940000176365 |
HOGENOMi | CLU_009031_5_0_1 |
InParanoidi | P40308 |
OMAi | GYGNIDQ |
Family and domain databases
InterProi | View protein in InterPro IPR016035, Acyl_Trfase/lysoPLipase IPR002641, PNPLA_dom IPR021771, Triacylglycerol_lipase_N |
Pfami | View protein in Pfam PF11815, DUF3336, 1 hit PF01734, Patatin, 1 hit |
SUPFAMi | SSF52151, SSF52151, 1 hit |
PROSITEi | View protein in PROSITE PS51635, PNPLA, 1 hit |
i Sequence
Sequence statusi: Complete.
P40308-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKETAQEYKV SAVIPTLLKN WILRVVYATL DHIPPFVWEI LHVITDIYFF
60 70 80 90 100
WVQKLINYVR PHSRVIYYNA IKKLDECDTY QMWCQQASVV DEITGANLWR
110 120 130 140 150
RNFFSRRYDF NSVIEQYSIL ENMLREEKYD VVKEKFSTTG PCMLRNFAGI
160 170 180 190 200
GDKKLFTKSL MGTKLLIEQY LTRILEGLDI LNNQTLTPTS FFQRCKLSLG
210 220 230 240 250
TTALILQGGS LFGLFHLGVI RGLLLQDLMP NIISGSSMGA CVASLFGCLS
260 270 280 290 300
NEQLKQLLTD DNLLNIIKND VDLLKSCGYG NLEQHLNLGT LIQNLIHHGY
310 320 330 340 350
SQDVYLFIRF VMKYIVKEKT FEEVYQITGK VFNIVIHPTD KSCPNLLNYV
360 370 380 390 400
TTPNVLIKSA IECSLGSGVI SEDTSLLCKN LENEIEPFLN INKNKQVKFL
410 420 430 440 450
TPENANNPSI TESPYTRLTE LFNVNNFIVS LARPYLAPLV VNDLKHEIKT
460 470 480 490 500
SKYYYYKHYP NMPPINANTV RKTQRSSSQS PIKAGTVEDL EPEPLMSPVP
510 520 530 540 550
PSSAVNDSAE YIIPELGIPQ LNFTEMEPLA FKFKYHLERK LKNIATMEFR
560 570 580 590 600
HRMEVLDNLG LLCSLIKRLI IDEKTPRSAT EIAVVPRMKS LSLTRIIEGQ
610 620 630 640
LNNIPYWIKS GERSTWPALA LIKTRCAVEF KLDDIIRARR SR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 96 | A → P in AAA53543 (PubMed:7918444).Curated | 1 | |
Sequence conflicti | 100 | R → P in AAA53543 (PubMed:7918444).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z54141 Genomic DNA Translation: CAA90831.1 L34347 Genomic DNA Translation: AAA53543.1 BK006946 Genomic DNA Translation: DAA10214.1 |
PIRi | S59306 |
RefSeqi | NP_014044.1, NM_001182824.1 |
Genome annotation databases
EnsemblFungii | YMR313C_mRNA; YMR313C; YMR313C |
GeneIDi | 855361 |
KEGGi | sce:YMR313C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z54141 Genomic DNA Translation: CAA90831.1 L34347 Genomic DNA Translation: AAA53543.1 BK006946 Genomic DNA Translation: DAA10214.1 |
PIRi | S59306 |
RefSeqi | NP_014044.1, NM_001182824.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 35493, 86 interactors |
DIPi | DIP-5641N |
IntActi | P40308, 3 interactors |
MINTi | P40308 |
STRINGi | 4932.YMR313C |
Chemistry databases
SwissLipidsi | SLP:000000052 SLP:000000671 SLP:000000678 |
PTM databases
iPTMneti | P40308 |
Proteomic databases
MaxQBi | P40308 |
PaxDbi | P40308 |
PRIDEi | P40308 |
Genome annotation databases
EnsemblFungii | YMR313C_mRNA; YMR313C; YMR313C |
GeneIDi | 855361 |
KEGGi | sce:YMR313C |
Organism-specific databases
SGDi | S000004930, TGL3 |
VEuPathDBi | FungiDB:YMR313C |
Phylogenomic databases
eggNOGi | KOG2214, Eukaryota |
GeneTreei | ENSGT00940000176365 |
HOGENOMi | CLU_009031_5_0_1 |
InParanoidi | P40308 |
OMAi | GYGNIDQ |
Enzyme and pathway databases
BioCyci | MetaCyc:G3O-32977-MONOMER YEAST:G3O-32977-MONOMER |
Miscellaneous databases
PROi | PR:P40308 |
RNActi | P40308, protein |
Family and domain databases
InterProi | View protein in InterPro IPR016035, Acyl_Trfase/lysoPLipase IPR002641, PNPLA_dom IPR021771, Triacylglycerol_lipase_N |
Pfami | View protein in Pfam PF11815, DUF3336, 1 hit PF01734, Patatin, 1 hit |
SUPFAMi | SSF52151, SSF52151, 1 hit |
PROSITEi | View protein in PROSITE PS51635, PNPLA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TGL3_YEAST | |
Accessioni | P40308Primary (citable) accession number: P40308 Secondary accession number(s): D6W0E0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | October 1, 1996 | |
Last modified: | February 10, 2021 | |
This is version 155 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names