Q2VG90 · LIP1_MALFU
- ProteinSecreted triacylglycerol lipase LIP1
- GeneLIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids488 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Secreted lipase that releases free fatty acids from monoacylglycerol and triacylglycerol but has no phospholipase or lysophospholipase activities (PubMed:16436442).
Has minor esterase activity (PubMed:16436442).
Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth (Probable). Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable). Hydrolyzes lipids, such as Tween 20, 40 and 80, with Tween 80 being the best substrate (PubMed:16436442).
Has minor esterase activity (PubMed:16436442).
Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth (Probable). Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable). Hydrolyzes lipids, such as Tween 20, 40 and 80, with Tween 80 being the best substrate (PubMed:16436442).
Catalytic activity
- a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
- a monoacylglycerol + H2O = glycerol + a fatty acid + H+
- a diacylglycerol + H2O = a monoacylglycerol + a fatty acid + H+
Activity regulation
Inhibited by different metal ions including Fe2+, Fe3+, Cu2+, and Zn2+ (PubMed:16436442).
The monovalent ions Na+ and K+ exhibit less dramatic inhibition (PubMed:16436442).
The monovalent ions Na+ and K+ exhibit less dramatic inhibition (PubMed:16436442).
pH Dependence
Optimum pH is 5.8.
Temperature Dependence
Optimum temperature is 40 degrees Celsius.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 201 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 348 | |||||
Sequence: D | ||||||
Active site | 382 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | triacylglycerol lipase activity | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSecreted triacylglycerol lipase LIP1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Malasseziomycetes > Malasseziales > Malasseziaceae > Malassezia
Accessions
- Primary accessionQ2VG90
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MPSMLSLFYLAQSLFLLLLFPLYGHA | ||||||
Chain | PRO_0000459492 | 27-488 | Secreted triacylglycerol lipase LIP1 | |||
Sequence: SVLKRGNNDPFYQPPAHWKSKQPGDILRWRKIEPKFIGGDFNVAEAYQLLYRTSQNTPNEPQHTVTTILVPHNAKKDILVVGSVAQDANGQQCTPSAGYTYNSESNFVFWLDETFFLQYLQEGYIMTIPDKEGPKNAFAAGRMEGYMTLDSIRATLNFSKLKLSSNTRIAGYGYSGGAITLGWASSLKPSYAPELNIIGWSFGGTPSNLLGTINHIDGTIFSGLILAGVTGVTDVYPEIHEYIQTVLNSAGREGLEFCRNHCLQEIILRYPLKSIYSYEFQTRGKDVFNNATVQQMFTDLTMGIRPHETPDVPVFMYHAQHDEIVPYDDAHKTAKAWCRNGAQVKFTTYSHYEMGHFTTEITGSVPAFHFIRDLFNGKEVSQGCDFKTEDTLFFNPSVLGGNANEIIDAILGIFGQRIGPEGRILAAKKTVVKGSKSGSSLKSHSHSQTHKHRKDVSTISNA | ||||||
Disulfide bond | 119↔288 | |||||
Sequence: CTPSAGYTYNSESNFVFWLDETFFLQYLQEGYIMTIPDKEGPKNAFAAGRMEGYMTLDSIRATLNFSKLKLSSNTRIAGYGYSGGAITLGWASSLKPSYAPELNIIGWSFGGTPSNLLGTINHIDGTIFSGLILAGVTGVTDVYPEIHEYIQTVLNSAGREGLEFCRNHC | ||||||
Glycosylation | 183 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 316 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Induction
Not expressed in laboratory conditions.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 461-488 | Disordered | ||||
Sequence: SKSGSSLKSHSHSQTHKHRKDVSTISNA |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length488
- Mass (Da)54,357
- Last updated2006-01-10 v1
- Checksum2D611BD8B4C97142