P36165 · TGL4_YEAST
- ProteinTriacylglycerol lipase 4
- GeneTGL4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids910 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 A2 (PLA2) 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).
Also has steryl ester (SE) hydrolase and phospholipase A2 (PLA2) 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).
Miscellaneous
Present with 195 molecules/cell in log phase SD medium.
Catalytic activity
- a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+This reaction proceeds in the forward direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H+This reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
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).
Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase (PubMed:27170177).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
14.3 μM | 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate | |||||
15.1 μM | (9Z)-octadecenoyl-CoA |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
11.4 nmol/min/mg | towards 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate | ||||
11.98 nmol/min/mg | towards (9Z)-octadecenoyl-CoA |
pH Dependence
Optimum pH is 7-9 for the lysophosphatidic acid acyltransferase (LPAAT) reaction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 315 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 470 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lipid droplet | |
Molecular Function | calcium-independent phospholipase A2 activity | |
Molecular Function | lysophosphatidic acid acyltransferase activity | |
Molecular Function | sterol esterase activity | |
Molecular Function | triglyceride lipase activity | |
Biological Process | cell budding | |
Biological Process | phospholipid metabolic process | |
Biological Process | sporulation resulting in formation of a cellular spore | |
Biological Process | triglyceride catabolic process | |
Biological Process | triglyceride mobilization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameTriacylglycerol lipase 4
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP36165
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
A double deletion of TGL3 and TGL4, the 2 major TGA lipases, leads to fat yeast, rendering growing cells unable to degrade triglycerides.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 675 | Highly stimulates TGA lipolysis. | ||||
Sequence: T → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000203227 | 1-910 | Triacylglycerol lipase 4 | |||
Sequence: MSSKISDLTSTQNKPLLVTQQLIEKYYEQILGTSQNIIPILNPKNKFIRPSKDNSDVERVEEDAGKRLQTGKNKTTNKVNFNLDTGNEDKLDDDQETVTENENNDIEMVETDEGEDERQGSSLASKCKSFLYNVFVGNYERDILIDKVCSQKQHAMSFEEWCSAGARLDDLTGKTEWKQKLESPLYDYKLIKDLTSRMREERLNRNYAQLLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMESDLDDSYLLGILQQTRRNIGRTALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQKSESENLLIKISRFFKNGTWFDNKHLVNTMIEFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEKDPKTGERKPWTGSSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQNLSSIYNFMANEAIHILEIGSEMGIAKNALTKLRSVLSQQYSGDITILPDMCMLFRIKELLSNPTKEFLLREITNGAKATWPKVSIIQNHCGQEFALDKAISYIKGRMIVTSSLKTPFQFADSVIGLIKAPEQTSDESKNPENSTLLTRTPTKGDNHISNVLDDNLLESESTNSLLLLRENASTYGRSPSGFRPRYSITSASLNPRHQRRKSDTISTSRRPAKSFSFSVASPTSRMLRQSSKINGHPPPILQKKTSMGRLMFPMDAKTYDPESHELIPHSASIETPAMVDKKLHFGRKSRYLRHMNKKWVSSSNILYTDSDKEDHPTLRLISNFDSDAMIHSDLAGNFRRHSIDGRPPSQATKSSPFRSRPSSSTQHKSTTSFTQ | ||||||
Modified residue | 55 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 675 | Phosphothreonine; by Cdk1 | ||||
Sequence: T | ||||||
Modified residue | 737 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 749 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 751 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 836 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 890 | Phosphoserine; by Cdk1 | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Thr-675 and Ser-890 by Cdk1/CDC28 stimulates enzyme activity in vivo.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 51-69 | Basic and acidic residues | ||||
Sequence: SKDNSDVERVEEDAGKRLQ | ||||||
Region | 51-120 | Disordered | ||||
Sequence: SKDNSDVERVEEDAGKRLQTGKNKTTNKVNFNLDTGNEDKLDDDQETVTENENNDIEMVETDEGEDERQG | ||||||
Compositional bias | 70-84 | Polar residues | ||||
Sequence: TGKNKTTNKVNFNLD | ||||||
Compositional bias | 89-114 | Acidic residues | ||||
Sequence: DKLDDDQETVTENENNDIEMVETDEG | ||||||
Domain | 282-483 | PNPLA | ||||
Sequence: LVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQKSESENLLIKISRFFKNGTWFDNKHLVNTMIEFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEKDPKTGERKPWTGSSSVKFVDGSVDNDLPISRLS | ||||||
Motif | 286-291 | GXGXXG | ||||
Sequence: GGGTFG | ||||||
Motif | 313-317 | GXSXG | ||||
Sequence: GSSAG | ||||||
Region | 657-683 | Disordered | ||||
Sequence: EQTSDESKNPENSTLLTRTPTKGDNHI | ||||||
Compositional bias | 658-683 | Polar residues | ||||
Sequence: QTSDESKNPENSTLLTRTPTKGDNHI | ||||||
Compositional bias | 713-730 | Polar residues | ||||
Sequence: SPSGFRPRYSITSASLNP | ||||||
Region | 713-777 | Disordered | ||||
Sequence: SPSGFRPRYSITSASLNPRHQRRKSDTISTSRRPAKSFSFSVASPTSRMLRQSSKINGHPPPILQ | ||||||
Compositional bias | 743-766 | Polar residues | ||||
Sequence: SRRPAKSFSFSVASPTSRMLRQSS | ||||||
Region | 874-910 | Disordered | ||||
Sequence: RRHSIDGRPPSQATKSSPFRSRPSSSTQHKSTTSFTQ | ||||||
Compositional bias | 882-910 | Polar residues | ||||
Sequence: PPSQATKSSPFRSRPSSSTQHKSTTSFTQ |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length910
- Mass (Da)102,717
- Last updated1994-06-01 v1
- Checksum1CFC03C4A6E64B9C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 51-69 | Basic and acidic residues | ||||
Sequence: SKDNSDVERVEEDAGKRLQ | ||||||
Compositional bias | 70-84 | Polar residues | ||||
Sequence: TGKNKTTNKVNFNLD | ||||||
Compositional bias | 89-114 | Acidic residues | ||||
Sequence: DKLDDDQETVTENENNDIEMVETDEG | ||||||
Compositional bias | 658-683 | Polar residues | ||||
Sequence: QTSDESKNPENSTLLTRTPTKGDNHI | ||||||
Compositional bias | 713-730 | Polar residues | ||||
Sequence: SPSGFRPRYSITSASLNP | ||||||
Compositional bias | 743-766 | Polar residues | ||||
Sequence: SRRPAKSFSFSVASPTSRMLRQSS | ||||||
Compositional bias | 882-910 | Polar residues | ||||
Sequence: PPSQATKSSPFRSRPSSSTQHKSTTSFTQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z27116 EMBL· GenBank· DDBJ | CAA81640.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28314 EMBL· GenBank· DDBJ | CAA82168.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA09239.1 EMBL· GenBank· DDBJ | Genomic DNA |