F6PXQ2 · F6PXQ2_MONDO

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 site193Charge relay system
Active site219Charge relay system
Binding site233Ca2+ (UniProtKB | ChEBI)
Binding site238Ca2+ (UniProtKB | ChEBI)
Active site304Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular space
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 Processcholesterol homeostasis
Biological Processcholesterol metabolic process
Biological Processcholesterol transport
Biological Processfatty acid biosynthetic process
Biological Processhigh-density lipoprotein particle remodeling
Biological Processlow-density lipoprotein particle remodeling
Biological Processtriglyceride catabolic process
Biological Processtriglyceride homeostasis
Biological Processvery-low-density lipoprotein particle remodeling

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

Accessions

  • Primary accession
    F6PXQ2

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-21
ChainPRO_500334438422-524Hepatic triacylglycerol lipase

Expression

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias35-50Polar residues
Region35-62Disordered
Domain377-511PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    60,073
  • Last updated
    2013-01-09 v2
  • MD5 Checksum
    B400FB9BB36953A74E6082BAF2CD14D9
MERSLWASLFLLFSFLVQLNAYGRTPDPDEKMEVSSHQTTCPSSHKLCGTKHSTPEAARKSPQKMEIKSLKTETRFLLYSTENGDSCQIHLHHLDTLDRCSFNSSLPLVIIVHGWSVDGILEKWIWQMATALRSQKSNQVNVIVADWMTLAHQHYAVAVRNTRHVGQEIANFLEWLEEAIQFSRSNVHLIGYSLGAHVSGFAGSYINGTNKIGRITGLDAAGPLFEGTSPTERLSPDDADFVDAIHTFTQEHMGLSVGIKQPVAHYDFYPNGGTFQPGCHFLLMYRHIAQRGFHGITETVKCAHERSVHLFIDSILNEHMQSIGYWCSDMNTFNKGLCLDCKKGRCNTLGYHIRKQRQQKSKKLFLVTQAHVPFKVYHYQFKIQFIKQTEEPIEPTFTMTLIGTKKDTHNLPITLVEEIKGNKTYSLLITLDLDIGELTMINFTWKKTAMWANVWDTFHTIIPWATEPQNPQFMIKQIRVKAGETQKKMKFCSQNMDDVQLYRNQEKTFVRCEEGSKPQNQRLR

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5F8G1W6A0A5F8G1W6_MONDOLIPC497

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias35-50Polar residues

Keywords

Sequence databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help