A0A3L7IKX6 · A0A3L7IKX6_CRIGR

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

  • 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.
  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    EC:3.1.1.32 (UniProtKB | ENZYME | Rhea)
  • a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
    EC:3.1.1.34 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site159Nucleophile
Active site183Charge relay system
Binding site197Ca2+ (UniProtKB | ChEBI)
Binding site202Ca2+ (UniProtKB | ChEBI)
Active site268Charge relay system

GO annotations

AspectTerm
Cellular Componentcatalytic complex
Cellular Componentcell surface
Cellular Componentchylomicron
Cellular Componentplasma membrane
Cellular Componentvery-low-density lipoprotein particle
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functionapolipoprotein binding
Molecular Functioncalcium ion binding
Molecular Functionheparan sulfate proteoglycan binding
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionlipoprotein particle binding
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Molecular Functionprotein homodimerization activity
Molecular Functionsignaling receptor binding
Biological Processcellular response to fatty acid
Biological Processcellular response to nutrient
Biological Processcholesterol homeostasis
Biological Processchylomicron remodeling
Biological Processfatty acid biosynthetic process
Biological Processlow-density lipoprotein particle mediated signaling
Biological Processpositive regulation of adipose tissue development
Biological Processpositive regulation of chemokine (C-X-C motif) ligand 2 production
Biological Processpositive regulation of cholesterol storage
Biological Processpositive regulation of fat cell differentiation
Biological Processpositive regulation of inflammatory response
Biological Processpositive regulation of interleukin-1 beta production
Biological Processpositive regulation of interleukin-6 production
Biological Processpositive regulation of macrophage derived foam cell differentiation
Biological Processpositive regulation of sequestering of triglyceride
Biological Processpositive regulation of tumor necrosis factor production
Biological Processresponse to bacterium
Biological Processtriglyceride catabolic process
Biological Processtriglyceride homeostasis
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
    A0A3L7IKX6

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
Signal1-20
ChainPRO_504265500621-474Lipoprotein 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.
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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain341-464PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    474
  • Mass (Da)
    52,945
  • Last updated
    2019-02-13 v1
  • Checksum
    80410C198E04054D
MESKALLLVALGVWLQSLTASQGGVAAADGGRDFTDIESKFALRTPDDTAEDNCHLIPGIAESVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESDKQLNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWKSDSYFSWSDWWSSPGFVIEKIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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