G9K8I1 · G9K8I1_MUSPF

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.

147450100150200250300350400450
TypeIDPosition(s)Description
Active site159Nucleophile
Active site183Charge relay system
Binding site197Ca2+ (UniProtKB | ChEBI)
Binding site202Ca2+ (UniProtKB | ChEBI)
Active site268Charge 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 Processresponse to glucose
Biological Processtriglyceride catabolic process
Biological Processvery-low-density lipoprotein particle remodeling

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

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

Organism names

Accessions

  • Primary accession
    G9K8I1

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.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_500513311921-474Lipoprotein 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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain341-464PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    474
  • Mass (Da)
    53,115
  • Last updated
    2012-02-22 v1
  • Checksum
    4432A3B31451CAB4
MESKALLLVALGMWFQSLTATRGGVAAADRGRDFIDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGKDVAKFINWMAEEFHYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESDTQTNQAFEISLYGTVAESENIPFTLPEFSANKTYSFLIYTEVDIGELLMLKLKWKNDSYFSWSDWWSSPSFAIEKIRVKAGETQKKVIFCSREKVSHLQKGKASVVFVKCHDKSLNKKS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue474

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JP012608
EMBL· GenBank· DDBJ
AES01206.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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