D4P6H2 · D4P6H2_PIG

  • Protein
    Triacylglycerol lipase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + 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 + H+ + hexadecanoate
    This reaction proceeds in the forward direction.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site169Nucleophile
Active site193Charge relay system
Binding site204Ca2+ (UniProtKB | ChEBI)
Binding site207Ca2+ (UniProtKB | ChEBI)
Binding site209Ca2+ (UniProtKB | ChEBI)
Binding site212Ca2+ (UniProtKB | ChEBI)
Active site280Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionall-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity
Molecular Functionmetal ion binding
Molecular Functiontriglyceride lipase activity
Biological Processlipid catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

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

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    D4P6H2

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-16
ChainPRO_500512650817-465Triacylglycerol lipase
Disulfide bond20↔26
Disulfide bond107↔118
Disulfide bond254↔278
Disulfide bond302↔313
Disulfide bond316↔321
Disulfide bond449↔465

Keywords

Interaction

Subunit

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

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain355-465PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    465
  • Mass (Da)
    51,680
  • Last updated
    2010-05-18 v1
  • Checksum
    24E703643C4986FA
MLLIWTLSLLLGAVLGSEVCFPRLGCFSDDAPWAGIVQRPLKILPWDPKDVNTRFLLYTNENQDNYQELVADPSTITDSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQVVGHLDFFPNGGKEMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSNEFDSDVEVGDLQKVKFIWYNNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLTPC

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GU576971
EMBL· GenBank· DDBJ
ADD71520.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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