A0A4Z2B7R0 · A0A4Z2B7R0_9TELE

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site179Nucleophile
Active site203Charge relay system
Binding site222Ca2+ (UniProtKB | ChEBI)
Active site291Charge relay system

GO annotations

AspectTerm
Cellular Componentchylomicron
Cellular Componentplasma membrane
Cellular Componentvery-low-density lipoprotein particle
Molecular Functionapolipoprotein binding
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionmetal ion binding
Biological Processfatty acid biosynthetic process
Biological Processtriglyceride catabolic process
Biological Processvery-low-density lipoprotein particle remodeling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • ORF names
      fugu_006070

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • TB-2018
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Tetraodontiformes > Tetradontoidea > Tetraodontidae > Takifugu

Accessions

  • Primary accession
    A0A4Z2B7R0

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

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-23
ChainPRO_502151068724-535Lipoprotein lipase

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.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain364-487PLAT
Region489-514Disordered
Compositional bias493-510Polar residues

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    535
  • Mass (Da)
    60,153
  • Last updated
    2019-09-18 v1
  • Checksum
    445A4F6A2F52E01B
MGIKNIFFFTLWIILGKCCATFASEPDTDTDAEFVTTSLPGTPLPTTADWINNFTDIVSKFSLRTAEIPDDDMCYIVPGRPETISECHFNPDTQTFVVIHGWTVTGMFESWVPKLVSALYEREPSANVIVVDWLTRANQHYPMSAAFTKLVGRDVAKFVSWIQNELNLPWERIHLLGYSLGAHVAGIAGDLTDHKISRITGLDPAGPTFEHADNQNTLSPDDAKFVDVLHTNTRGSPNRSIGIQRPVGHVDIYPNGGTFQPGCDIQNTLLGIAAEGIKGLHNMDQLVKCSHERSIHLFIDSLINTEQQSVAYRCNSKEAFNKGLCLSCRKNRCNKLGYNVNHVRTTRGAKLYLKTREMMPYKVFHYQVKVHFFSETQQSFTEQPMKISLYGTHGEKEDIPFVLPELNSNTTVSFLLTTDVDLGDLMIVKLRWEKDAIISWSDWWGSSRVHIRKLRIKSGESQSKVIFGAKDGEYVHLVRGGEDGVFSQVEGGPNEPQGETDAQTQDPRQPFQERSLRRHVHAAAAYRARHLSVKT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias493-510Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SWLE01000019
EMBL· GenBank· DDBJ
TNM87849.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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