| IED ID | IndEnz0005000897 |
| Enzyme Type ID | lipase000897 |
| Protein Name |
Triacylglycerol lipase 4 EC 3.1.1.3 Lipase 4 |
| Gene Name | TGL4 STC1 YKR089C YKR409 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSSKISDLTSTQNKPLLVTQQLIEKYYEQILGTSQNIIPILNPKNKFIRPSKDNSDVERVEEDAGKRLQTGKNKTTNKVNFNLDTGNEDKLDDDQETVTENENNDIEMVETDEGEDERQGSSLASKCKSFLYNVFVGNYERDILIDKVCSQKQHAMSFEEWCSAGARLDDLTGKTEWKQKLESPLYDYKLIKDLTSRMREERLNRNYAQLLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMESDLDDSYLLGILQQTRRNIGRTALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQKSESENLLIKISRFFKNGTWFDNKHLVNTMIEFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEKDPKTGERKPWTGSSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQNLSSIYNFMANEAIHILEIGSEMGIAKNALTKLRSVLSQQYSGDITILPDMCMLFRIKELLSNPTKEFLLREITNGAKATWPKVSIIQNHCGQEFALDKAISYIKGRMIVTSSLKTPFQFADSVIGLIKAPEQTSDESKNPENSTLLTRTPTKGDNHISNVLDDNLLESESTNSLLLLRENASTYGRSPSGFRPRYSITSASLNPRHQRRKSDTISTSRRPAKSFSFSVASPTSRMLRQSSKINGHPPPILQKKTSMGRLMFPMDAKTYDPESHELIPHSASIETPAMVDKKLHFGRKSRYLRHMNKKWVSSSNILYTDSDKEDHPTLRLISNFDSDAMIHSDLAGNFRRHSIDGRPPSQATKSSPFRSRPSSSTQHKSTTSFTQ |
| Enzyme Length | 910 |
| Uniprot Accession Number | P36165 |
| Absorption | |
| Active Site | ACT_SITE 315; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 470; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: Phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/CDC28) (PubMed:19150427). Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase (PubMed:27170177). {ECO:0000269|PubMed:19150427, ECO:0000269|PubMed:27170177}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:16135509};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:16135509}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:20332534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:16267052, ECO:0000305|PubMed:20332534}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:20332534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000305|PubMed:20332534}; CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, ChEBI:CHEBI:46898; Evidence={ECO:0000269|PubMed:20332534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; Evidence={ECO:0000305|PubMed:20332534}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:20332534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000305|PubMed:20332534}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: 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:16135509, PubMed:16267052). Also has steryl ester (SE) hydrolase and phospholipase A(2) (PLA(2)) activities, and catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20332534). Contributes to early bud formation in late G1 phase of the cell cycle upon phosphorylation and activation by cyclin-dependent kinase 1 (Cdk1/CDC28) (PubMed:19150427). {ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:19150427, ECO:0000269|PubMed:20332534}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9 for the lysophosphatidic acid acyltransferase (LPAAT) reaction. {ECO:0000269|PubMed:20332534}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (7); Domain (1); Modified residue (7); Motif (2); Mutagenesis (1); Region (4) |
| Keywords | Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Phosphoprotein;Reference proteome;Sporulation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:19150427, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093, ECO:0000269|PubMed:27170177}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols. {ECO:0000269|PubMed:27170177}. |
| Modified Residue | MOD_RES 55; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 675; /note="Phosphothreonine; by Cdk1"; /evidence="ECO:0000269|PubMed:19150427"; MOD_RES 737; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956"; MOD_RES 749; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 751; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:19779198"; MOD_RES 836; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 890; /note="Phosphoserine; by Cdk1"; /evidence="ECO:0000269|PubMed:19150427" |
| Post Translational Modification | PTM: Phosphorylation at Thr-675 and Ser-890 by Cdk1/CDC28 stimulates enzyme activity in vivo. {ECO:0000269|PubMed:19150427}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10375630; 11283351; 14574415; 16606443; 16916618; 16919863; 17559233; 18258205; 18269180; 18367008; 18467557; 19037676; 19436716; 19696439; 19754450; 20056167; 20231294; 20379744; 20452973; 20465793; 20727985; 22312416; 22345606; 22578140; 22592553; 22989772; 23042128; 23139841; 23275493; 23631861; 24390141; 24418527; 24520995; 24597968; 24678285; 25016085; 25475986; 25500271; 25713391; 25894691; 26061644; 26162625; 26636650; 26907989; 27797916; 27932491; |
| Motif | MOTIF 286..291; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 313..317; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 102,717 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.3 uM for 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:20332534}; KM=15.1 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20332534}; Vmax=11.4 nmol/min/mg enzyme towards 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:20332534}; Vmax=11.98 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20332534}; |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:12045; RHEA:38575; RHEA:38576; RHEA:41223; RHEA:41224; RHEA:33875; RHEA:33876; RHEA:37131; RHEA:37132 |
| Cross Reference Brenda |