P34163 · TGL1_YEAST
- ProteinSterol esterase TGL1
- GeneTGL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids548 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
Miscellaneous
Present with 1470 molecules/cell in log phase SD medium.
Catalytic activity
- a sterol ester + H2O = a fatty acid + a sterol + H+
pH Dependence
Optimum pH is 7.4.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 201 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 369 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 396 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lipid droplet | |
Cellular Component | membrane | |
Molecular Function | sterol esterase activity | |
Biological Process | cellular lipid metabolic process | |
Biological Process | lipid catabolic process | |
Biological Process | sterol metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSterol esterase TGL1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP34163
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Note: Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols and consequently lipid droplets.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-13 | Lumenal | ||||
Sequence: MYFPFLGRLSITD | ||||||
Transmembrane | 14-34 | Helical | ||||
Sequence: YIIVVLVYIESIISSVLKLIP | ||||||
Topological domain | 35-548 | Cytoplasmic | ||||
Sequence: QPMINLFEWLINFSTSSDDNTIEEKLRSAPTIHEMCAIFDISVEDHLVRTEDNYILTLHRIPPISKNRFNNKVVYLHHGLLMCSDVWCCNIERHKNLPFVLHDLGYDVWMGNNRGNKYSTAHLNKPPKSNKFWDFSIDEFAFFDIPNSIEFILDITKVDKVICIGFSQGSAQMFAAFSLSEKLNRKVSHFIAIAPAMTPKGLHNRIVDTLAKSSPGFMYLFFGRKIVLPSAVIWQRTLHPTLFNLCIDIANKILFNWKSFNILPRQKIASYAKLYSTTSVKSIVHWFQILRSQKFQMFEESDNMLNSLTRPYQIANFPTRTNIKIPILLIYGGIDSLVDIDVMKKNLPFNSVFDVKVDNYEHLDLIWGKDADTLVIAKVLRFIEFFNPGNVSVKTNQLLPSASLVEELPSTTWKTTHPTHGLSYRTHSADRSPLSVQADEADEVHNADNSRFLRRVFSTSAIDEDNENEHQDDTEDQIHKEQQRRLSAYLESSKDLRQLDANSSTTALDALNKE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine; partial | ||||
Sequence: M | ||||||
Chain | PRO_0000090379 | 1-548 | Sterol esterase TGL1 | |||
Sequence: MYFPFLGRLSITDYIIVVLVYIESIISSVLKLIPQPMINLFEWLINFSTSSDDNTIEEKLRSAPTIHEMCAIFDISVEDHLVRTEDNYILTLHRIPPISKNRFNNKVVYLHHGLLMCSDVWCCNIERHKNLPFVLHDLGYDVWMGNNRGNKYSTAHLNKPPKSNKFWDFSIDEFAFFDIPNSIEFILDITKVDKVICIGFSQGSAQMFAAFSLSEKLNRKVSHFIAIAPAMTPKGLHNRIVDTLAKSSPGFMYLFFGRKIVLPSAVIWQRTLHPTLFNLCIDIANKILFNWKSFNILPRQKIASYAKLYSTTSVKSIVHWFQILRSQKFQMFEESDNMLNSLTRPYQIANFPTRTNIKIPILLIYGGIDSLVDIDVMKKNLPFNSVFDVKVDNYEHLDLIWGKDADTLVIAKVLRFIEFFNPGNVSVKTNQLLPSASLVEELPSTTWKTTHPTHGLSYRTHSADRSPLSVQADEADEVHNADNSRFLRRVFSTSAIDEDNENEHQDDTEDQIHKEQQRRLSAYLESSKDLRQLDANSSTTALDALNKE | ||||||
Cross-link | 246 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 462 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 466 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 521 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 538 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 539 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Not N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, motif, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 107-402 | AB hydrolase-1 | ||||
Sequence: VVYLHHGLLMCSDVWCCNIERHKNLPFVLHDLGYDVWMGNNRGNKYSTAHLNKPPKSNKFWDFSIDEFAFFDIPNSIEFILDITKVDKVICIGFSQGSAQMFAAFSLSEKLNRKVSHFIAIAPAMTPKGLHNRIVDTLAKSSPGFMYLFFGRKIVLPSAVIWQRTLHPTLFNLCIDIANKILFNWKSFNILPRQKIASYAKLYSTTSVKSIVHWFQILRSQKFQMFEESDNMLNSLTRPYQIANFPTRTNIKIPILLIYGGIDSLVDIDVMKKNLPFNSVFDVKVDNYEHLDLIWG | ||||||
Motif | 199-203 | GXSXG | ||||
Sequence: GFSQG | ||||||
Compositional bias | 449-467 | Polar residues | ||||
Sequence: TTHPTHGLSYRTHSADRSP | ||||||
Region | 449-477 | Disordered | ||||
Sequence: TTHPTHGLSYRTHSADRSPLSVQADEADE | ||||||
Region | 496-516 | Disordered | ||||
Sequence: IDEDNENEHQDDTEDQIHKEQ | ||||||
Region | 528-548 | Disordered | ||||
Sequence: KDLRQLDANSSTTALDALNKE | ||||||
Compositional bias | 530-548 | Polar residues | ||||
Sequence: LRQLDANSSTTALDALNKE |
Sequence similarities
Belongs to the AB hydrolase superfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length548
- Mass (Da)62,979
- Last updated1994-02-01 v1
- Checksum32D1F230701CB083
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 449-467 | Polar residues | ||||
Sequence: TTHPTHGLSYRTHSADRSP | ||||||
Compositional bias | 530-548 | Polar residues | ||||
Sequence: LRQLDANSSTTALDALNKE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z25464 EMBL· GenBank· DDBJ | CAA80958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28140 EMBL· GenBank· DDBJ | CAA81981.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA09022.1 EMBL· GenBank· DDBJ | Genomic DNA |