A0A3L7IKX6 · A0A3L7IKX6_CRIGR
- ProteinLipoprotein lipase
- GeneLpl
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids474 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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
- 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-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+This reaction proceeds in the forward direction.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 159 | Nucleophile | |||
Active site | 183 | Charge relay system | |||
Binding site | 197 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 202 | Ca2+ (UniProtKB | ChEBI) | |||
Active site | 268 | Charge relay system | |||
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoprotein lipase
- EC number
- Short namesLPL
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionA0A3L7IKX6
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 | 1-20 | ||||
Chain | PRO_5042655006 | 21-474 | Lipoprotein lipase | ||
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.
Homodimer. Interacts with GPIHBP1 with 1:1 stoichiometry. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interaction with heparan sulfate proteoglycans is required to protect LPL against loss of activity. Associates with lipoprotein particles in blood plasma. Interacts with LMF1 and SEL1L; interaction with SEL1L is required to prevent aggregation of newly synthesized LPL in the endoplasmic reticulum (ER), and for normal export of LPL from the ER to the extracellular space. Interacts with SORL1; SORL1 acts as a sorting receptor, promoting LPL localization to endosomes and later to lysosomes, leading to degradation of newly synthesized LPL.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 341-464 | PLAT | |||
Sequence similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length474
- Mass (Da)52,945
- Last updated2019-02-13 v1
- Checksum80410C198E04054D