A0A3P8SZL5 · A0A3P8SZL5_AMPPE

Function

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine
    This reaction proceeds in the forward direction.
  • 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H+
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H+ + sn-glycero-3-phospho-L-serine
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholine
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    EC:3.1.1.32 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H+ + sn-glycerol 3-phosphocholine
    EC:3.1.1.5 (UniProtKB | ENZYME | Rhea)
  • a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
    EC:3.1.1.3 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site165Nucleophile
Active site191Charge relay system
Binding site205Ca2+ (UniProtKB | ChEBI)
Binding site210Ca2+ (UniProtKB | ChEBI)
Active site276Charge relay system

GO annotations

AspectTerm
Cellular Componenthigh-density lipoprotein particle
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functionheparin binding
Molecular Functionlysophospholipase activity
Molecular Functionmetal ion binding
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Molecular Functiontriglyceride lipase activity
Biological Processlipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hepatic triacylglycerol lipase
  • EC number
  • Alternative names
    • Lipase member C
    • Lysophospholipase
    • Phospholipase A1

Organism names

Accessions

  • Primary accession
    A0A3P8SZL5

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_501826910620-496Hepatic triacylglycerol lipase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain349-482PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    55,770
  • Last updated
    2019-02-13 v1
  • Checksum
    76781F646027793C
MLGVKILCCLLLTCHLSGGKKIKGERASVADIEQRIVLRVKEPYVSSSAFSLFLGGEDTCTLDPLQLHTLTSCGFNSSNPLIIITHGWSVDGMMESWVLRLASALKTNLVSVNVVLTDWLSLAHQHYPMAVQSTRTVGKDISHLLQTLQEQYQYPVKKVHLIGYSLGAHISGFAGSYLEGSEKIGRITGLDPAGPLFEGMSPTDRLSPDDAEFVDAIHTFTHERMGLSVGIKQAVAHFDFYPNGGDFQPGCDLQNIYEHITEYGLLGFEQTVKCAHERSVHLFIDSLLNKDKQSMAYRCSDNNAFVKGVCLDCRKNRCNTLGYDIKKVRTVTSKRLYLKTRSRMPYKLYHYQFRIQFINQVENIDPTLTVALTGTKEESGDVVITFNEKISGNTTFPFLITLDKDLGDLMLVKLHWEGLALWKNVWNRVQTIIPWGGKETKPLLTVGRISVKAGETQERTSFCAMTDDGQQIEVSQDKVFVRCKEDIPKQRRRKHN

Keywords

Genome annotation databases

Similar Proteins

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