Q5XTQ4 · LIP1_BOTFB

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).

Catalytic activity

pH Dependence

Optimum pH is 6.

Temperature Dependence

Optimum temperature is 38 degrees Celsius.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site244Acyl-ester intermediate
Active site376Charge relay system
Active site489Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncarboxylesterase activity
Biological Processlipid catabolic process

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Secreted lipase 1
  • Alternative names
    • Carboxylesterase LIP1
      (EC:3.1.1.1
      ) . EC:3.1.1.1 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      lip1
    • ORF names
      BCIN_09g06880

Organism names

Accessions

  • Primary accession
    Q5XTQ4
  • Secondary accessions
    • A0A384JTM0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Impairs all extracellular esterase activity (PubMed:20565655).
Does not affect host cuticle penetration (PubMed:20565655).

Miscellaneous

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_500514376718-574Secreted lipase 1
Disulfide bond95↔132
Disulfide bond303↔312
Glycosylation323N-linked (GlcNAc...) asparagine
Glycosylation386N-linked (GlcNAc...) asparagine
Glycosylation524N-linked (GlcNAc...) asparagine

Keywords

Expression

Induction

Expression is repressed by glucose or other simple sugars such as sucrose, fructose, galactose and mannose.

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    574
  • Mass (Da)
    60,894
  • Last updated
    2004-11-23 v1
  • Checksum
    A03AEAA2F79AFFB3
MKLSLVPIFALLSTAFALPVENAERDVPIEERAAAPTVTIASPAATIIGGAGATVETFAGVPFAKPPVGALRLKPPQPITSALGTIKATAQAASCPQFFFSTTINDAIPTSALGLLLNTPVFQQVLNAGEDCLYLNIQRPVGTTASSKLPVLFWIFGGGFELGGTAMYDGSSWVAESIAEGKPIIFVQVAYRVGGFGFLPGAEILADGSANLGLLDQRLGLQWVADNIAAFGGDPSKVTIWGESAGAISVFDQMALYGGDNTYKGKSLFRGAIMNSGSIVPADPVDCPKGQIIYDNVVASAGCSAAANTLTCLRGVPYSTLLNATNSVPGLLSYSSIALSYLPRPDGTALTKSPDLLLASGNWAKVPFIIGDQEDEGTIFALFQSNISTTAQLTTYFSDFFFHNAPTSVLTGLLNTYPNDLISGSPFRTLLLNNWYPQFKRLAAILGDLTFTLTRRVFLKTALKVAPTVPSWSYLSSYDYGTPVLGTFHGSDILQVFNGIKPNYAASASKAYYLSFVNTLDPNNGTSSAYANWPQYSNGAQLLNLYASFGGFISDNFRSTSYDYIVANLPSFYI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY738714
EMBL· GenBank· DDBJ
AAU87359.1
EMBL· GenBank· DDBJ
Genomic DNA
CP009813
EMBL· GenBank· DDBJ
ATZ53935.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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