A0A151NEW6 · A0A151NEW6_ALLMI
- ProteinLipoprotein lipase
- GeneLPL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids484 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chylomicron | |
Cellular Component | plasma membrane | |
Cellular Component | very-low-density lipoprotein particle | |
Molecular Function | heparin binding | |
Molecular Function | lipoprotein lipase activity | |
Molecular Function | metal ion binding | |
Biological Process | triglyceride catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLipoprotein lipase
- EC number
- Short namesLPL
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Crocodylia > Alligatoridae > Alligatorinae > Alligator
Accessions
- Primary accessionA0A151NEW6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
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
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MAWGALLVVLCLCLRALA | ||||||
Chain | PRO_5007358853 | 19-484 | Lipoprotein lipase | |||
Sequence: AGPGTTPETRGIFEGIESKFSLRTPAIPDEDICYLVPGQKDSLAHCSFNHTSKTFLVIHGWTVTGMYESWVPKLVDALYKREPDSNVIIVDWLTRAQQHYPISAAYTKLVGKDVASFIDWMEEQFNYPFENVHLLGYSLGAHVAGIAGSLTKKKINRITGLDPAGPTFEYADAPMRLSPDDAEFVDVLHTYTRGSPDRSIGIQQPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFGDVDQLVKCSHERSIHLFIDSLMYEEKPSMAYRCQTKEAFEKGLCLSCRKNRCNNMGYQIHKVRTKRNSKMYLKTRSQAPYKVFHYQVKIHFFGKENVTKTSQPLLISLYGTTDERENIAFILPEISTNKTYSFLVYTEVDIGDLLRLSLQWEKDSFFSWTEWWTSFTFDIHRVRVKAGETQKKMVFCSQDGVAHLQKGGEAVMFVKCLGNPVRRRKAGHKPISEIKTDP |
Post-translational modification
Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.
Keywords
- PTM
Interaction
Subunit
Homodimer. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 338-461 | PLAT | ||||
Sequence: FHYQVKIHFFGKENVTKTSQPLLISLYGTTDERENIAFILPEISTNKTYSFLVYTEVDIGDLLRLSLQWEKDSFFSWTEWWTSFTFDIHRVRVKAGETQKKMVFCSQDGVAHLQKGGEAVMFVK |
Sequence similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length484
- Mass (Da)54,732
- Last updated2016-06-08 v1
- Checksum5D48DEB88AB356B7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AKHW03003207 EMBL· GenBank· DDBJ | KYO35095.1 EMBL· GenBank· DDBJ | Genomic DNA |