A0A3Q2XLN1 · A0A3Q2XLN1_HIPCM

Function

function

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Caution

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

Catalytic activity

Features

Showing features for active site, binding site.

152050100150200250300350400450500
TypeIDPosition(s)Description
Active site183Nucleophile
Active site207Charge relay system
Binding site226Ca2+ (UniProtKB | ChEBI)
Active site295Charge relay system

GO annotations

AspectTerm
Cellular Componentchylomicron
Cellular Componentplasma membrane
Cellular Componentvery-low-density lipoprotein particle
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionmetal ion binding
Biological Processtriglyceride catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipoprotein lipase
  • EC number
  • Short names
    LPL

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Syngnathiaria > Syngnathiformes > Syngnathoidei > Syngnathidae > Hippocampus

Accessions

  • Primary accession
    A0A3Q2XLN1

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein
Secreted
Note: Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles.

Keywords

PTM/Processing

Post-translational modification

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.

Keywords

Interaction

Subunit

Homodimer. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain368-491PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    520
  • Mass (Da)
    58,872
  • Last updated
    2019-04-10 v1
  • Checksum
    4F8F78A72FD64ABC
KLLKLLFFNEHNYEKLPNLVFCAPMTSHISVSACVTTVNGSVTPTSLPVTTTEWLTDYTDIVSKFSLRSADTPDDDMCYIVAGRPDTIQECKFNAQTQTFVIIHGWTVTGMFESWVPKLVSALYERVPNANVIVVDWLTRANQHYSTSAAYTKLAGRDVAKFVTWIQKELQLPWDKIHLLGYSLGAHVAGIAGYLTDHKISRITGLDPAGPTFEHAEDQNTLSRDDAQFVDVLHTNTRGSPGRSIGIQKPVGHIDIYPNGGAFQPGCDIQNTLKGIALEGLKGLQNMDQLVKCSHERSIHLFIDSLLNTQQQSMAYRCNSRESFNKGLCLSCRKNRCNKIGYNINKVRTARSAMMYLKTREKMPYKVFHYQVKMHMFSDRRLTFNEQPIKVSLYGTHGEKEDISFVLPVMNHNSTVSFLITTDVDIGDLMIVKLRWEKDSIFSWPDWRGSNKFYIRKLRIKSGETQSKVSFRAKEAEFSDLVRGGEAAVFVKSKEDNLSRKERLMHKIKTQGSLFGQTDA

Genome annotation databases

Similar Proteins

Disclaimer

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