A0A8D0GXM9 · A0A8D0GXM9_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.

145750100150200250300350400450
Type
IDPosition(s)Description
Active site144Nucleophile
Active site168Charge relay system
Binding site182Ca2+ (UniProtKB | ChEBI)
Binding site187Ca2+ (UniProtKB | ChEBI)
Active site253Charge relay system

GO annotations

AspectTerm
Cellular Componentcatalytic complex
Cellular Componentchylomicron
Cellular Componentplasma membrane
Cellular Componentvery-low-density lipoprotein particle
Molecular Functionapolipoprotein binding
Molecular Functioncalcium ion binding
Molecular Functionheparan sulfate proteoglycan binding
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionlipoprotein particle binding
Molecular Functionphospholipase A1 activity
Molecular Functionprotein homodimerization activity
Molecular Functionsignaling receptor binding
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 production
Biological Processpositive regulation of cholesterol storage
Biological Processpositive regulation of fat cell differentiation
Biological Processpositive regulation of sequestering of triglyceride
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
    A0A8D0GXM9

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
Domain326-449PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    457
  • Mass (Da)
    51,929
  • Last updated
    2022-01-19 v1
  • Checksum
    18777FCA86E949ED
MQESISLCLRGGEPQAQDFGGIESKFALRTVKEPDEDTCYLVPGQEDTVAKCNFNHTSKTFVVIHGWTVTGMYESWIPKLVYALYKREPESNVIVVDWLRRAQQHYPVSAAYAQQVGEDIATFVDWMEEQFNYQLDNLHLLGYSLGAHAAGIAGSLTKTKINRITGLDPAGPNFEYAEANTRLSPDDAGFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGETIRLLAERGFGDVDQLVKCSHERSIHLFIDSLLYEESPSLAYRCSTKETFEKGLCLSCRKNRCNSLGYNINKVRTKRSTKMYLKTRSQMPYKVFHYQVKIHFFGKLNVTKTNQPFLLSLYGTLDESENIAFILPEISTNKTASFLIYTEVNIGDLLMLKLQWENDSIFSWSNWWINPEFRIQRVRVKAGETQKKLVFCSRDGISHLKKGKEAVVFVRCTDKFMNV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8D0GW52A0A8D0GW52_SPHPULPL451

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp