Q12043 · TGL5_YEAST
- ProteinTriacylglycerol lipase 5
- GeneTGL5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids749 (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).
Also catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20016004).
Also catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20016004).
Miscellaneous
Present with 358 molecules/cell in log phase SD medium.
Catalytic activity
- a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
- (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.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
Activity regulation
Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
18.7 μM | 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate | |||||
29.3 μM | (9Z)-octadecenoyl-CoA |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
28.8 nmol/min/mg | towards 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate | ||||
38.1 nmol/min/mg | towards (9Z)-octadecenoyl-CoA |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 216 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 375 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lipid droplet | |
Molecular Function | lysophosphatidic acid acyltransferase activity | |
Molecular Function | triglyceride lipase activity | |
Biological Process | lipid catabolic process | |
Biological Process | sporulation resulting in formation of a cellular spore | |
Biological Process | triglyceride mobilization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameTriacylglycerol lipase 5
- EC number
- Short namesTAG lipase 5; TG lipase 5
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ12043
- 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
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000270918 | 1-749 | Triacylglycerol lipase 5 | |||
Sequence: MSNTLPVTEFLLSKYYELSNTPATDSSSLFKWLYHKTLSRKQLLISDLSSQKKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNSKSPNENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDPHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITARFRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMVGQFHEVLKNPSQLFLLHQTTLGARATWPKISMIQNNCGQEFALDKAITFLKEKIIISSSIKNPLQFYQPRFSEQIKSLSIMDADLPGVDLEESSSNSLSIIKSPNKTAAPGRFPLQPLPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKANSLSFAIGASSLRLKKSPLKVPSRPQFKKRSSYYNQNMSAEMRKNRKKSGTISSYDVQTNSEDFPIPAIENGSFDNTLFNPSRFPMDAMSAATNDNFMNNSDIFQN | ||||||
Glycosylation | 270 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 289 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 304 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 321 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 474 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 589 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 645 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 680 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 714 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 742 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for motif, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 54-59 | HXXXXD acyltransferase motif | ||||
Sequence: HAISYD | ||||||
Domain | 183-388 | PNPLA | ||||
Sequence: LVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNSKSPNENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDPHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLS | ||||||
Motif | 214-218 | GXSXG | ||||
Sequence: GSSAG | ||||||
Region | 585-643 | Disordered | ||||
Sequence: IKSPNKTAAPGRFPLQPLPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKA | ||||||
Compositional bias | 602-643 | Polar residues | ||||
Sequence: LPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKA |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length749
- Mass (Da)84,716
- Last updated1996-11-01 v1
- ChecksumF3C5DBA97B6BA58B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 602-643 | Polar residues | ||||
Sequence: LPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X94335 EMBL· GenBank· DDBJ | CAA64004.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74989 EMBL· GenBank· DDBJ | CAA99274.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z70678 EMBL· GenBank· DDBJ | CAA94566.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006948 EMBL· GenBank· DDBJ | DAA10860.1 EMBL· GenBank· DDBJ | Genomic DNA |