P34163 · TGL1_YEAST

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).

Miscellaneous

Present with 1470 molecules/cell in log phase SD medium.

Catalytic activity

pH Dependence

Optimum pH is 7.4.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site201Nucleophile
Active site369Charge relay system
Active site396Charge relay system

GO annotations

AspectTerm
Cellular Componentlipid droplet
Cellular Componentmembrane
Molecular Functionsterol esterase activity
Biological Processcellular lipid metabolic process
Biological Processlipid catabolic process
Biological Processsterol metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Sterol esterase TGL1
  • EC number
  • Alternative names
    • Triglyceride lipase-cholesterol esterase 1

Gene names

    • Name
      TGL1
    • ORF names
      YKL5
    • Ordered locus names
      YKL140W

Organism names

Accessions

  • Primary accession
    P34163
  • Secondary accessions
    • D6VX56

Proteomes

Organism-specific databases

Subcellular Location

Lipid droplet
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.

TypeIDPosition(s)Description
Topological domain1-13Lumenal
Transmembrane14-34Helical
Topological domain35-548Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for modified residue, chain, cross-link.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine; partial
ChainPRO_00000903791-548Sterol esterase TGL1
Cross-link246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue462Phosphoserine
Modified residue466Phosphoserine
Modified residue521Phosphoserine
Modified residue538Phosphoserine
Modified residue539Phosphothreonine

Post-translational modification

Not N-glycosylated.

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, motif, compositional bias, region.

TypeIDPosition(s)Description
Domain107-402AB hydrolase-1
Motif199-203GXSXG
Compositional bias449-467Polar residues
Region449-477Disordered
Region496-516Disordered
Region528-548Disordered
Compositional bias530-548Polar residues

Sequence similarities

Belongs to the AB hydrolase superfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    548
  • Mass (Da)
    62,979
  • Last updated
    1994-02-01 v1
  • Checksum
    32D1F230701CB083
MYFPFLGRLSITDYIIVVLVYIESIISSVLKLIPQPMINLFEWLINFSTSSDDNTIEEKLRSAPTIHEMCAIFDISVEDHLVRTEDNYILTLHRIPPISKNRFNNKVVYLHHGLLMCSDVWCCNIERHKNLPFVLHDLGYDVWMGNNRGNKYSTAHLNKPPKSNKFWDFSIDEFAFFDIPNSIEFILDITKVDKVICIGFSQGSAQMFAAFSLSEKLNRKVSHFIAIAPAMTPKGLHNRIVDTLAKSSPGFMYLFFGRKIVLPSAVIWQRTLHPTLFNLCIDIANKILFNWKSFNILPRQKIASYAKLYSTTSVKSIVHWFQILRSQKFQMFEESDNMLNSLTRPYQIANFPTRTNIKIPILLIYGGIDSLVDIDVMKKNLPFNSVFDVKVDNYEHLDLIWGKDADTLVIAKVLRFIEFFNPGNVSVKTNQLLPSASLVEELPSTTWKTTHPTHGLSYRTHSADRSPLSVQADEADEVHNADNSRFLRRVFSTSAIDEDNENEHQDDTEDQIHKEQQRRLSAYLESSKDLRQLDANSSTTALDALNKE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias449-467Polar residues
Compositional bias530-548Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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