Detail Information for IndEnz0005000576
IED ID IndEnz0005000576
Enzyme Type ID lipase000576
Protein Name Lipoprotein lipase
LPL
EC 3.1.1.34
Phospholipase A1
EC 3.1.1.32
Gene Name LPL
Organism Ovis aries (Sheep)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Caprinae Ovis Ovis aries (Sheep)
Enzyme Sequence MESKVLLLLALSVWLQSLTVSRGGLVAADRITRGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG
Enzyme Length 478
Uniprot Accession Number Q29524
Absorption
Active Site ACT_SITE 162; /note=Nucleophile; ACT_SITE 186; /note=Charge relay system; ACT_SITE 271; /note=Charge relay system
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}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34; Evidence={ECO:0000250|UniProtKB:P11151}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:P06858}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P06858};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P06858}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000250|UniProtKB:P06858};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000250|UniProtKB:P06858}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P06858};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P06858}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P06858};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000250|UniProtKB:P06858};
DNA Binding
EC Number 3.1.1.34; 3.1.1.32
Enzyme Function FUNCTION: Key enzyme in triglyceride metabolism (By similarity). 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 (By similarity). 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 (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity). {ECO:0000250|UniProtKB:P06858}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Metal binding (4); Modified residue (3); Region (5); Signal peptide (1)
Keywords Calcium;Cell membrane;Chylomicron;Disulfide bond;Extracellular matrix;Glycoprotein;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Metal-binding;Nitration;Reference proteome;Secreted;Signal;VLDL
Interact With
Induction
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:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. 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. {ECO:0000250|UniProtKB:P11151}.
Modified Residue MOD_RES 124; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:Q06000; MOD_RES 194; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:Q06000; MOD_RES 346; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:Q06000
Post Translational Modification PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 53,588
Kinetics
Metal Binding METAL 197; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P06858; METAL 200; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P06858; METAL 202; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P06858; METAL 205; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P06858
Rhea ID RHEA:12044; RHEA:18689; RHEA:38575; RHEA:38576; RHEA:38699; RHEA:38700; RHEA:40475; RHEA:40476; RHEA:41384; RHEA:41385
Cross Reference Brenda