| IED ID | IndEnz0005000924 |
| Enzyme Type ID | lipase000924 |
| Protein Name |
Sterol esterase TGL1 EC 3.1.1.13 Triglyceride lipase-cholesterol esterase 1 |
| Gene Name | TGL1 YKL140W YKL5 |
| 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 | MYFPFLGRLSITDYIIVVLVYIESIISSVLKLIPQPMINLFEWLINFSTSSDDNTIEEKLRSAPTIHEMCAIFDISVEDHLVRTEDNYILTLHRIPPISKNRFNNKVVYLHHGLLMCSDVWCCNIERHKNLPFVLHDLGYDVWMGNNRGNKYSTAHLNKPPKSNKFWDFSIDEFAFFDIPNSIEFILDITKVDKVICIGFSQGSAQMFAAFSLSEKLNRKVSHFIAIAPAMTPKGLHNRIVDTLAKSSPGFMYLFFGRKIVLPSAVIWQRTLHPTLFNLCIDIANKILFNWKSFNILPRQKIASYAKLYSTTSVKSIVHWFQILRSQKFQMFEESDNMLNSLTRPYQIANFPTRTNIKIPILLIYGGIDSLVDIDVMKKNLPFNSVFDVKVDNYEHLDLIWGKDADTLVIAKVLRFIEFFNPGNVSVKTNQLLPSASLVEELPSTTWKTTHPTHGLSYRTHSADRSPLSVQADEADEVHNADNSRFLRRVFSTSAIDEDNENEHQDDTEDQIHKEQQRRLSAYLESSKDLRQLDANSSTTALDALNKE |
| Enzyme Length | 548 |
| Uniprot Accession Number | P34163 |
| Absorption | |
| Active Site | ACT_SITE 201; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P80035; ACT_SITE 369; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P80035; ACT_SITE 396; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P80035 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+); Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13; Evidence={ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:15922657, ECO:0000269|PubMed:28866104}; |
| DNA Binding | |
| EC Number | 3.1.1.13 |
| Enzyme Function | FUNCTION: Mediates the hydrolysis of steryl esters (SE) (PubMed:10515935, PubMed:14640980, PubMed:15713625). Preferentially hydrolyzes ergosteryl and zymosteryl esters (PubMed:19111628). Required for mobilization of SEs from lipid particles/droplets, thereby playing a central role in lipid metabolism and sterol homeostasis. Sterol intermediates stored in SE and set free by SE hydrolases are recycled to the sterol biosynthetic pathway and converted to the final product, ergosterol, in the endoplasmic reticulum. Has also weak lipase activity toward triglycerides at neutral pH, however, the physiological relevance of this activity is unclear (PubMed:15922657, PubMed:19111628, PubMed:28866104). {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:14640980, ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:15922657, ECO:0000269|PubMed:19111628, ECO:0000269|PubMed:28866104}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:15922657}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (6); Motif (1); Region (3); Topological domain (2); Transmembrane (1) |
| Keywords | Acetylation;Hydrolase;Isopeptide bond;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:15922657, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:23613772, ECO:0000269|PubMed:24868093, ECO:0000269|PubMed:28866104}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols and consequently lipid droplets. {ECO:0000269|PubMed:28866104}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; partial; /evidence=ECO:0000305|PubMed:23613772; MOD_RES 462; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 466; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 521; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17287358; MOD_RES 538; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 539; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:19779198 |
| Post Translational Modification | PTM: Not N-glycosylated. {ECO:0000269|PubMed:15713625}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10998572; 11805837; 15218532; 16246075; 16835446; 16916618; 16919863; 17434796; 18258205; 18269180; 18467557; 19536198; 19696439; 20056167; 20231294; 20489023; 21621788; 21693588; 22101561; 22345606; 23139841; 23275493; 24597968; 25720564; 25894691; 26224664; 26636650; 27050453; 27591256; 28772; |
| Motif | MOTIF 199..203; /note=GXSXG; /evidence=ECO:0000305|Ref.16 |
| Gene Encoded By | |
| Mass | 62,979 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:10100 |
| Cross Reference Brenda | 3.1.1.13; |