Q5XTQ4 · LIP1_BOTFB
- ProteinSecreted lipase 1
- Genelip1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids574 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Secreted lipase that allows the use of hydrolyzed lipids as carbon sources (PubMed:20565655, PubMed:7609604).
Has highest activity with methyl umbelliferyl oleate (C18:1), whereas much lower activities are obtained with the respective esters of palmitate (C16:0) and stearate (C18:0) (24% and 12% of the activity obtained with umbelliferyl oleate, respectively) (PubMed:20565655, PubMed:7609604).
Hydrolyzes 1- and 3-positioned ester bonds in preference to 2-positioned ester bonds (PubMed:7609604).
The production rate of monoglycerides is lower than that of diacylglycerides (PubMed:7609604).
Seems not required for the penetration of intact host tissue (PubMed:20565655).
Has highest activity with methyl umbelliferyl oleate (C18:1), whereas much lower activities are obtained with the respective esters of palmitate (C16:0) and stearate (C18:0) (24% and 12% of the activity obtained with umbelliferyl oleate, respectively) (PubMed:20565655, PubMed:7609604).
Hydrolyzes 1- and 3-positioned ester bonds in preference to 2-positioned ester bonds (PubMed:7609604).
The production rate of monoglycerides is lower than that of diacylglycerides (PubMed:7609604).
Seems not required for the penetration of intact host tissue (PubMed:20565655).
Catalytic activity
- a carboxylic ester + H2O = an alcohol + a carboxylate + H+
pH Dependence
Optimum pH is 6.
Temperature Dependence
Optimum temperature is 38 degrees Celsius.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 244 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 376 | Charge relay system | ||||
Sequence: E | ||||||
Active site | 489 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | carboxylesterase activity | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSecreted lipase 1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Sclerotiniaceae > Botrytis
Accessions
- Primary accessionQ5XTQ4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MKLSLVPIFALLSTAFA | ||||||
Chain | PRO_5005143767 | 18-574 | Secreted lipase 1 | |||
Sequence: LPVENAERDVPIEERAAAPTVTIASPAATIIGGAGATVETFAGVPFAKPPVGALRLKPPQPITSALGTIKATAQAASCPQFFFSTTINDAIPTSALGLLLNTPVFQQVLNAGEDCLYLNIQRPVGTTASSKLPVLFWIFGGGFELGGTAMYDGSSWVAESIAEGKPIIFVQVAYRVGGFGFLPGAEILADGSANLGLLDQRLGLQWVADNIAAFGGDPSKVTIWGESAGAISVFDQMALYGGDNTYKGKSLFRGAIMNSGSIVPADPVDCPKGQIIYDNVVASAGCSAAANTLTCLRGVPYSTLLNATNSVPGLLSYSSIALSYLPRPDGTALTKSPDLLLASGNWAKVPFIIGDQEDEGTIFALFQSNISTTAQLTTYFSDFFFHNAPTSVLTGLLNTYPNDLISGSPFRTLLLNNWYPQFKRLAAILGDLTFTLTRRVFLKTALKVAPTVPSWSYLSSYDYGTPVLGTFHGSDILQVFNGIKPNYAASASKAYYLSFVNTLDPNNGTSSAYANWPQYSNGAQLLNLYASFGGFISDNFRSTSYDYIVANLPSFYI | ||||||
Disulfide bond | 95↔132 | |||||
Sequence: CPQFFFSTTINDAIPTSALGLLLNTPVFQQVLNAGEDC | ||||||
Disulfide bond | 303↔312 | |||||
Sequence: CSAAANTLTC | ||||||
Glycosylation | 323 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 386 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 524 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Induction
Expression is repressed by glucose or other simple sugars such as sucrose, fructose, galactose and mannose.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length574
- Mass (Da)60,894
- Last updated2004-11-23 v1
- ChecksumA03AEAA2F79AFFB3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY738714 EMBL· GenBank· DDBJ | AAU87359.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP009813 EMBL· GenBank· DDBJ | ATZ53935.1 EMBL· GenBank· DDBJ | Genomic DNA |