Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

LPL (P06858) - Overview - Molecular Target Synopsis

Protein


LPL, Lipoprotein lipase
Enzyme Classification 3.1.1.34
UniProt P06858

Also Known as LIPL_HUMAN, LPL, LIPD

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 (PubMed:8675619, PubMed:11342582, PubMed:27578112). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232). Homodimer (PubMed:16179346, PubMed:26725083, PubMed:11893776) (Probable). Interacts with GPIHBP1 with 1:1 stoichiometry (PubMed:17997385, PubMed:27929370, PubMed:26725083, PubMed:27811232, PubMed:29899144, PubMed:30559189). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interaction with heparan sulfate proteoglycans is required to protect LPL against loss of activity (PubMed:11342582). Associates with lipoprotein particles in blood plasma (PubMed:11342582, PubMed:11893776). 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 (PubMed:25066055).

6OB0
COMPOUND 2 BOUND STRUCTURE OF WT LIPOPROTEIN LIPASE IN COMPLEX WITH GPIHBP1 MUTANT N78D N82D PRODUCED IN HEK293-F CELLS
RCSB/PDB
Inspect Structure
See all 3D Structures for LPL

Isoforms / Transcripts (Protein Coding)


Sub-cellular localization


UniProt: LPL is active in the following subcellular-locations: cell membrane, extracellular matrix, extracellular space, secreted.
GO terms: LPL is active in the following subcellular-locations: anchored component of membrane, cell surface, chylomicron, extracellular region, extracellular space, plasma membrane, very-low-density lipoprotein particle.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project LPL has gain in 0 cell-lines, loss in 11 cell-lines and no signal in 994 cell-lines. (see details)

Gene Expression


In NCI60, the highest expressing cell lines are: UACC_62, HL_60, RPMI_8226

In Array Express (RNA-seq of 675 commonly used human cancer cell lines), the highest expressing cell lines are: MFM-223, HeLa, NCI-H889

In Array Express (RNA-seq of long poly adenylated RNA and long non poly adenylated RNA from ENCODE cell lines), the highest expressing cell lines are: SK-N-SH, NHLF, HSMM

(see details)

3D Structures


For LPL there are:
4 structures (12 chains) solved
4 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


LPL has been screened with 66 compounds (96 bioactivities), 1 compounds have bioactivities that show binding affinity of <= 500nM (1 bioactivities). (see details)