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H3ANV5 · H3ANV5_LATCH

Function

function

Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles. Also exhibits lysophospholipase activity. Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates. In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position.

Caution

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

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = 2,3-di-(9Z)-octadecenoyl-sn-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 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)-sn-glycero-3-phosphocholine + H2O = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+
    This reaction proceeds in the forward direction.
  • 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = 3-(9Z-octadecenoyl)-sn-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + hexadecanoate + H+
    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 = sn-glycerol 3-phosphocholine + a fatty acid + H+
    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.

Type
IDPosition(s)Description
Active site169Nucleophile
Active site195Charge relay system
Binding site209Ca2+ (UniProtKB | ChEBI)
Binding site214Ca2+ (UniProtKB | ChEBI)
Active site280Charge relay system

GO annotations

AspectTerm
Cellular Componenthigh-density lipoprotein particle
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functionapolipoprotein binding
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionlysophospholipase activity
Molecular Functionmetal ion binding
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Biological Processfatty acid biosynthetic process
Biological Processtriglyceride catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      LIPC

Organism names

  • Taxonomic identifier
  • Strain
    • Wild caught
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Coelacanthiformes > Coelacanthidae > Latimeria

Accessions

  • Primary accession
    H3ANV5

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_500358008223-503Hepatic triacylglycerol lipase

Expression

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain353-488PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    503
  • Mass (Da)
    57,547
  • Last updated
    2013-05-01 v2
  • MD5 Checksum
    A46AAB2995365909EA786C93BC2758BB
MRGVRLMFFLLLFCIFISNADTQTSQKKDQKNNYHQAVRIRKDQHISETKFLLYLKDGTSDKTCQILPYQSETIHSCSFNTSFPLVVIIHGWSVDGMLEGWTWELASALKSKLKSVNVIVADWLTLAHQHYPIAAQNTRLVGQETADFLEWLEEFYQFPKDSVHLIGYSLGAHVAGFAGSYINGPRKIGRITGLDPAGPLFEGMSPTDRLSPNDAKFVDAIHTFTQQHMGLSVGIKQPVAHYDFYPNGGNFQPGCHIKYVYNHIAQHGIIGITQTVKCAHERSVYLFIDSLLNEDRQSVAYWCNDITTFDKGVCLSCRKNRCNTLGYNIKKVRSQRSKRMYLKTRSQMPFKVYHYQFKIHFINQIAQKQVEPSLTVSLIGTKEDIENLPISLVESITGNKTYSFLITIDTNIGDLMMIKFKWEGLVAWANIWDTVQTIIPWGKQRTGPELILRKIRVKAGETQEKMTFCSQNEANIHLQPTQEKTFVRCNDSNGKRQRIFKPV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AFYH01095931
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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