A0A8D0GW52 · A0A8D0GW52_SPHPU

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.

145150100150200250300350400450
Type
IDPosition(s)Description
Active site138Nucleophile
Active site162Charge relay system
Binding site176Ca2+ (UniProtKB | ChEBI)
Binding site181Ca2+ (UniProtKB | ChEBI)
Active site247Charge 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

    • Name
      LPL

Organism names

Accessions

  • Primary accession
    A0A8D0GW52

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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain320-443PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    451
  • Mass (Da)
    51,340
  • Last updated
    2022-01-19 v1
  • Checksum
    F02738A6196D645C
PCLAWASPEKRDFGGIESKFALRTVKEPDEDTCYLVPGQEDTVAKCNFNHTSKTFVVIHGWTVTGMYESWIPKLVYALYKREPESNVIVVDWLRRAQQHYPVSAAYAQQVGEDIATFVDWMEEQFNYQLDNLHLLGYSLGAHAAGIAGSLTKTKINRITGLDPAGPNFEYAEANTRLSPDDAGFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGETIRLLAERGFGDVDQLVKCSHERSIHLFIDSLLYEESPSLAYRCSTKETFEKGLCLSCRKNRCNSLGYNINKVRTKRSTKMYLKTRSQMPYKVFHYQVKIHFFGKLNVTKTNQPFLLSLYGTLDESENIAFILPEISTNKTASFLIYTEVNIGDLLMLKLQWENDSIFSWSNWWINPEFRIQRVRVKAGETQKKLVFCSRDGISHLKKGKEAVVFVRCTDKFMNV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8D0GXM9A0A8D0GXM9_SPHPULPL457

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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