Lpl
entrez
16956
canonical
uniprot
P11152
canonical
ensembl
ENSMUSG00000015568
resolver
ensp
ENSMUSP00000015712
resolver
ensp
ENSMUSP00000132259
resolver
enst
ENSMUST00000015712
resolver
enst
ENSMUST00000168401
resolver
genesymbol
Lpl
resolver
uniprot
Q05956
resolver
uniprot
Q542L4
resolver
uniprot
Q9D3M9
resolver
uniprot
Q9DCM8
resolver
uniprot_entry
LIPL_MOUSE
resolver
uniprot_sec
Q05956
resolver
uniprot_sec
Q542L4
resolver
uniprot_sec
Q9D3M9
resolver
uniprot_sec
Q9DCM8
resolver
activity_regulation
ACTIVITY REGULATION: The apolipoprotein APOC2 acts as a coactivator of LPL activity (By similarity). Ca(2+) binding promotes protein stability and formation of the active homodimer. Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4 (By similarity). {ECO:0000250|UniProtKB:P06858, ECO:0000250|UniProtKB:P11151}.
uniprot
proteins
amino_acid_sequence
MESKALLLVVLGVWLQSLTAFRGGVAAADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG
uniprot
proteins
ec_number
3.1.1.32
uniprot
proteins
ec_number
3.1.1.34
uniprot
proteins
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 (PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232). {ECO:0000250|UniProtKB:P06858, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232, ECO:0000269|PubMed:8675619}.
uniprot
proteins
mass_dalton
53109
uniprot
proteins
post_translational_modification
PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.; PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
1339460
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17403372
uniprot
proteins
pubmed
1748295
uniprot
proteins
pubmed
1765386
uniprot
proteins
pubmed
20620994
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24726386
uniprot
proteins
pubmed
25066055
uniprot
proteins
pubmed
2723548
uniprot
proteins
pubmed
27811232
uniprot
proteins
pubmed
3597382
uniprot
proteins
pubmed
8675619
uniprot
proteins
sequence_length
474
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Peripheral membrane protein {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Extracellular side {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}. Secreted {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:25066055}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:27811232}. 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 (PubMed:27811232). 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 (By similarity). {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}.
uniprot
proteins