LPL
entrez
4023
canonical
uniprot
P06858
canonical
ensembl
ENSG00000175445
resolver
ensp
ENSP00000497642
resolver
ensp
ENSP00000635987
resolver
enst
ENST00000650287
resolver
enst
ENST00000965928
resolver
genesymbol
LPL
resolver
genesymbol_syn
LIPD
resolver
hgnc
HGNC:6677
resolver
uniprot
B2R5T9
resolver
uniprot
Q16282
resolver
uniprot
Q16283
resolver
uniprot
Q96FC4
resolver
uniprot_entry
LIPL_HUMAN
resolver
uniprot_sec
B2R5T9
resolver
uniprot_sec
Q16282
resolver
uniprot_sec
Q16283
resolver
uniprot_sec
Q96FC4
resolver
activity_regulation
ACTIVITY REGULATION: The apolipoprotein APOC2 acts as a coactivator of LPL activity (PubMed:12032167). Ca(2+) binding promotes protein stability and formation of the active homodimer (PubMed:16179346). Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4 (PubMed:27929370, PubMed:29899144). Inhibited by NaCl (PubMed:12032167). {ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144}.
uniprot
proteins
amino_acid_sequence
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
uniprot
proteins
disease_involvement
DISEASE: Hyperlipoproteinemia 1 (HLPP1) [MIM:238600]: An autosomal recessive metabolic disorder characterized by defective breakdown of dietary fats, impaired clearance of chylomicrons from plasma causing the plasma to have a milky appearance, and severe hypertriglyceridemia. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis. {ECO:0000269|PubMed:10660334, ECO:0000269|PubMed:10787434, ECO:0000269|PubMed:11068186, ECO:0000269|PubMed:11099402, ECO:0000269|PubMed:11134145, ECO:0000269|PubMed:11441134, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12204001, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:1400331, ECO:0000269|PubMed:1479292, ECO:0000269|PubMed:14984478, ECO:0000269|PubMed:15185149, ECO:0000269|PubMed:1521525, ECO:0000269|PubMed:15256764, ECO:0000269|PubMed:15877202, ECO:0000269|PubMed:1598907, ECO:0000269|PubMed:1619366, ECO:0000269|PubMed:1639392, ECO:0000269|PubMed:1674945, ECO:0000269|PubMed:1702428, ECO:0000269|PubMed:1730727, ECO:0000269|PubMed:1752947, ECO:0000269|PubMed:1907278, ECO:0000269|PubMed:1969408, ECO:0000269|PubMed:1975597, ECO:0000269|PubMed:2010533, ECO:0000269|PubMed:2038366, ECO:0000269|PubMed:2110364, ECO:0000269|PubMed:2121025, ECO:0000269|PubMed:24291057, ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189, ECO:0000269|PubMed:7806969, ECO:0000269|PubMed:7906986, ECO:0000269|PubMed:7912254, ECO:0000269|PubMed:7999071, ECO:0000269|PubMed:8077845, ECO:0000269|PubMed:8096693, ECO:0000269|PubMed:8135797, ECO:0000269|PubMed:8288243, ECO:0000269|PubMed:8301230, ECO:0000269|PubMed:8325986, ECO:0000269|PubMed:8486765, ECO:0000269|PubMed:8728326, ECO:0000269|PubMed:8778602, ECO:0000269|PubMed:8858123, ECO:0000269|PubMed:8956048, ECO:0000269|PubMed:8956052, ECO:0000269|PubMed:8973094, ECO:0000269|PubMed:9279761, ECO:0000269|PubMed:9298816, ECO:0000269|PubMed:9401010, ECO:0000269|PubMed:9498099, ECO:0000269|PubMed:9714430, ECO:0000269|PubMed:9719626}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hyperlipidemia, familial combined, 3 (FCHL3) [MIM:144250]: A disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease. FCHL3 inheritance is autosomal dominant. {ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:7647785, ECO:0000269|PubMed:8728326, ECO:0000269|PubMed:8872057, ECO:0000269|PubMed:9662394, ECO:0000269|PubMed:9719626}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
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:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). 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). {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:27811232, ECO:0000269|PubMed:7592706, ECO:0000269|PubMed:8675619}.
uniprot
proteins
mass_dalton
53162
uniprot
proteins
mutagenesis
MUTAGEN 159; /note="S->G: Loss of enzyme activity with triolein and tributyrin."; /evidence="ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:30559189"; MUTAGEN 159; /note="S->T: Loss of enzyme activity with triolein and tributyrin."; /evidence="ECO:0000269|PubMed:1371284"; MUTAGEN 183; /note="D->G,N: Loss of enzyme activity with triolein and tributyrin."; /evidence="ECO:0000269|PubMed:1371284"; MUTAGEN 199; /note="S->G: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:1371284"; MUTAGEN 201; /note="D->E: No effect on enzyme activity."; /evidence="ECO:0000269|PubMed:30559189"; MUTAGEN 202; /note="D->E: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:30559189"; MUTAGEN 244..264; /note="NIGEAIRVIAERGLGDVDQLV->HFLELYRHIAQHGFNAITQTI: Reduced triglyceride hydrolase activity and increased phospholipase activity."; /evidence="ECO:0000269|PubMed:7592706"; MUTAGEN 245..263; /note="IGEAIRVIAERGLGDVDQL->GIAEIRVIEARGGLDVDLQ: Loss of both triglyceride hydrolase and phospholipase activity."; /evidence="ECO:0000269|PubMed:7592706"; MUTAGEN 245..248; /note="IGEA->GIAE: Loss of triglyceride hydrolase activity while phospholipase activity remains intact."; /evidence="ECO:0000269|PubMed:7592706"; MUTAGEN 262..263; /note="QL->LQ: Loss of triglyceride hydrolase activity while phospholipase activity remains intact."; /evidence="ECO:0000269|PubMed:7592706"; MUTAGEN 268; /note="H->G: Loss of enzyme activity with triolein and tributyrin."; /evidence="ECO:0000269|PubMed:1371284"; MUTAGEN 268; /note="H->Q: Loss of enzyme activity with triolein and tributyrin."; /evidence="ECO:0000269|PubMed:1371284"; MUTAGEN 417; /note="W->A: Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with 420-A-A-421."; /evidence="ECO:0000269|PubMed:24726386"; MUTAGEN 420..421; /note="WW->AA: Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with A-417."; /evidence="ECO:0000269|PubMed:24726386"; MUTAGEN 430; /note="K->N: Impaired heparin-binding; when associated with N-432 and N-437."; /evidence="ECO:0000269|PubMed:11342582"; MUTAGEN 432; /note="R->N: Impaired heparin-binding; when associated with N-430 and N-437."; /evidence="ECO:0000269|PubMed:11342582"; MUTAGEN 434; /note="K->N: Impaired heparin-binding; when associated with N-430 and N-432."; /evidence="ECO:0000269|PubMed:11342582
uniprot
proteins
post_translational_modification
PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10660334
uniprot
proteins
pubmed
10787434
uniprot
proteins
pubmed
11068186
uniprot
proteins
pubmed
11099402
uniprot
proteins
pubmed
11134145
uniprot
proteins
pubmed
11342582
uniprot
proteins
pubmed
11441134
uniprot
proteins
pubmed
11893776
uniprot
proteins
pubmed
12032167
uniprot
proteins
pubmed
12204001
uniprot
proteins
pubmed
12641539
uniprot
proteins
pubmed
12966036
uniprot
proteins
pubmed
1371284
uniprot
proteins
pubmed
1400331
uniprot
proteins
pubmed
1406652
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1479292
uniprot
proteins
pubmed
14984478
uniprot
proteins
pubmed
15185149
uniprot
proteins
pubmed
1521525
uniprot
proteins
pubmed
15256764
uniprot
proteins
pubmed
1537564
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15877202
uniprot
proteins
pubmed
1598907
uniprot
proteins
pubmed
16179346
uniprot
proteins
pubmed
1619366
uniprot
proteins
pubmed
1639392
uniprot
proteins
pubmed
1674945
uniprot
proteins
pubmed
1702428
uniprot
proteins
pubmed
1730727
uniprot
proteins
pubmed
1752947
uniprot
proteins
pubmed
17997385
uniprot
proteins
pubmed
18780401
uniprot
proteins
pubmed
1907278
uniprot
proteins
pubmed
1969408
uniprot
proteins
pubmed
1975597
uniprot
proteins
pubmed
2010533
uniprot
proteins
pubmed
2038366
uniprot
proteins
pubmed
2110364
uniprot
proteins
pubmed
2121025
uniprot
proteins
pubmed
21385844
uniprot
proteins
pubmed
2243796
uniprot
proteins
pubmed
2340307
uniprot
proteins
pubmed
24291057
uniprot
proteins
pubmed
24726386
uniprot
proteins
pubmed
25066055
uniprot
proteins
pubmed
26725083
uniprot
proteins
pubmed
2701938
uniprot
proteins
pubmed
27578112
uniprot
proteins
pubmed
27811232
uniprot
proteins
pubmed
27929370
uniprot
proteins
pubmed
29899144
uniprot
proteins
pubmed
30559189
uniprot
proteins
pubmed
3823907
uniprot
proteins
pubmed
7592706
uniprot
proteins
pubmed
7647785
uniprot
proteins
pubmed
7806969
uniprot
proteins
pubmed
7906986
uniprot
proteins
pubmed
7912254
uniprot
proteins
pubmed
7999071
uniprot
proteins
pubmed
8077845
uniprot
proteins
pubmed
8096693
uniprot
proteins
pubmed
8135797
uniprot
proteins
pubmed
8288243
uniprot
proteins
pubmed
8301230
uniprot
proteins
pubmed
8308035
uniprot
proteins
pubmed
8325986
uniprot
proteins
pubmed
8486765
uniprot
proteins
pubmed
8675619
uniprot
proteins
pubmed
8728326
uniprot
proteins
pubmed
8778602
uniprot
proteins
pubmed
8858123
uniprot
proteins
pubmed
8872057
uniprot
proteins
pubmed
8956048
uniprot
proteins
pubmed
8956052
uniprot
proteins
pubmed
8973094
uniprot
proteins
pubmed
9279761
uniprot
proteins
pubmed
9298816
uniprot
proteins
pubmed
9401010
uniprot
proteins
pubmed
9498099
uniprot
proteins
pubmed
9662394
uniprot
proteins
pubmed
9714430
uniprot
proteins
pubmed
9719626
uniprot
proteins
sequence_length
475
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000269|PubMed:11342582, ECO:0000269|PubMed:11893776, ECO:0000269|PubMed:12641539, ECO:0000269|PubMed:1371284, ECO:0000269|PubMed:2340307, ECO:0000269|PubMed:24291057, ECO:0000269|PubMed:27578112, ECO:0000269|PubMed:30559189}. 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