A0A974CB89 · A0A974CB89_XENLA

Function

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)-octadecenoylglycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol + butanoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
    This reaction proceeds in the forward direction.
    EC:3.1.1.3 (UniProtKB | ENZYME | Rhea)
  • all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + hexadecanoate + H+
    This reaction proceeds in the forward direction.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site171Nucleophile
Active site194Charge relay system
Binding site208Ca2+ (UniProtKB | ChEBI)
Binding site210Ca2+ (UniProtKB | ChEBI)
Binding site213Ca2+ (UniProtKB | ChEBI)
Active site281Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionmetal ion binding
Molecular Functiontriacylglycerol lipase activity
Biological Processlipid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Triacylglycerol lipase
  • EC number
  • Alternative names
    • Pancreatic lipase

Gene names

    • ORF names
      XELAEV_18036656mg

Organism names

  • Taxonomic identifier
  • Strain
    • J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    A0A974CB89

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-17
ChainPRO_503816837518-474Triacylglycerol lipase
Disulfide bond451↔467

Keywords

Interaction

Subunit

Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain355-470PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    474
  • Mass (Da)
    52,744
  • Last updated
    2023-02-22 v1
  • Checksum
    BD81E3B90826C691
MVGRWRLIFFLLGCVQGEQVCYKRLGCFTDEAPWGGTAERPLRRLPMSPEKINTRFFLLTKDNPEKFQEISTFNLSSVSTSNFKPNRKTRFIIHGFLSSAEGSWLMDMCKTLLKVEDVNCFCVDWKAGSRTLYSQAANNIRVVGAEVAYFIDFLSSKYNYSSSKIHIIGHSLGSHTAGEVGKRVPGIGRITGLDPAGPLFRNTPPEVRLDPTDADFVDTIHTDTFPLIPKIGFGMSQSVGHLDFFPNGGEKMPGCHTSIITKLLHINEIWEGSDDLMACNHLRSYKYYTESILTPDAFIGYPSNTYQAFTEGSGFPCSSTSCHLMGHHVDSNGWDTLRGQSLFLNTGDVKPYARWRYKVTVNTSSSVWFLGSINVALHGVKGNTMEHRIASGLIKPGQTYTAFIDVEVDVGPLTTVSFSWNKSLVNIIPSTFRADTISVQYGKDGQTHQFCGTNWVMAKVLQILTPCDSQLSTK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM004479
EMBL· GenBank· DDBJ
OCT69732.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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