| IED ID | IndEnz0005000007 |
| Enzyme Type ID | lipase000007 |
| Protein Name |
Hepatic triacylglycerol lipase HL Hepatic lipase EC 3.1.1.3 Lipase member C Lysophospholipase EC 3.1.1.5 Phospholipase A1 EC 3.1.1.32 |
| Gene Name | Lipc |
| Organism | Rattus norvegicus (Rat) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MGNHLQISVSLVLCIFIQSSACGQGVGTEPFGRNLGATEERKPLQKPEIRFLLFKDESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLLETWIWKIVGALKSRQSQPVNVGLVDWISLAYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMGGKRKIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTINCAHERSVHLFIDSLQHSNLQNTGFQCSNMDSFSQGLCLNCKKGRCNSLGYDIRRIGHVKSKTLFLITRAQSPFKVYHYQFKIQFINQMEKPMEPTFTMTLLGTKEEIKKIPITLGEGITSNKTYSLLITLNKDIGELIMLKFKWENSAVWANVWNTVQTIMLWDTEPHYAGLIVKTIWVKAGETQQRMTFCPDNVDDLQLHPTQEKVFVKCDLKSKD |
| Enzyme Length | 494 |
| Uniprot Accession Number | P07867 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 195; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 280; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | ACTIVITY REGULATION: Phospholipase A1 and lysophospholipase activities are inhibited by annexin II. {ECO:0000269|PubMed:1531641}. |
| 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=3.1.1.3; Evidence={ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1770315, ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:7074125}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:1531641}; 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:0000269|PubMed:1531641, ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:6747460, ECO:0000269|PubMed:7074125}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:1865764};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512; Evidence={ECO:0000305|PubMed:1865764}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; Evidence={ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:7074125};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; Evidence={ECO:0000305|PubMed:1531641}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000269|PubMed:1531641};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000305|PubMed:1531641}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:1531641};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:1531641}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938; Evidence={ECO:0000269|PubMed:1531641};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652; Evidence={ECO:0000305|PubMed:1531641}; 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:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P11150}; 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:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000250|UniProtKB:P11150}; 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:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P11150}; 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:0000269|PubMed:7074125};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000269|PubMed:7074125}; |
| DNA Binding | |
| EC Number | 3.1.1.3; 3.1.1.5; 3.1.1.32 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (PubMed:7074125, PubMed:6747460, PubMed:1770315, PubMed:1865764, PubMed:1531641). Also exhibits lysophospholipase activity (PubMed:1531641). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (PubMed:1865764). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity). {ECO:0000250|UniProtKB:P11150, ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1770315, ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:6747460, ECO:0000269|PubMed:7074125}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:7074125}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Glycosylation (2); Region (1); Sequence conflict (7); Signal peptide (1) |
| Keywords | Glycoprotein;HDL;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11150}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000250|UniProtKB:P11150 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10600655; 10681410; 10734075; 10823662; 10844597; 11004003; 11427199; 11544558; 12234100; 12841343; 12935429; 1391269; 14531811; 14701798; 15102889; 15271879; 15744060; 16546477; 17709442; 18675312; 1868959; 18691644; 18758746; 19165521; 1918876; 19212806; 1940628; 2046484; 2086700; 2113037; 2223857; 3420106; 384999; 6480830; 6696938; 6791934; 7047662; 7078435; 7666262; 7830494; 7897313; 8071607; 8157689; 8192680; 8322779; 8510508; 8636395; 9020876; 9048565; 9106496; 9186885; 9480878; 9540793; 9685400; 9721028; 9728079; 9822677; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,623 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:7074125}; KM=0.16 mM for 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine {ECO:0000269|PubMed:7074125}; Vmax=144 umol/min/mg enzyme with 1-oleoyl-sn-glycerol as substrate {ECO:0000269|PubMed:1865764}; Vmax=163 umol/min/mg enzyme with 1,2-dioleoyl-sn-glycerol as substrate {ECO:0000269|PubMed:1865764}; Vmax=145 umol/min/mg enzyme with 1,3-dioleoyl-sn-glycerol as substrate {ECO:0000269|PubMed:1865764}; Vmax=67 umol/min/mg enzyme with phosphatidic acid as substrate {ECO:0000269|PubMed:1865764}; Vmax=50 umol/min/mg enzyme with phosphatidylethanolamine as substrate {ECO:0000269|PubMed:1865764}; Vmax=4 umol/min/mg enzyme with phosphatidylcholine as substrate {ECO:0000269|PubMed:1865764}; |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:15177; RHEA:18689; RHEA:38511; RHEA:38512; RHEA:38391; RHEA:38392; RHEA:40499; RHEA:40500; RHEA:40435; RHEA:40436; RHEA:38651; RHEA:38652; RHEA:38575; RHEA:38576; RHEA:38699; RHEA:38700; RHEA:40475; RHEA:40476; RHEA:41384; RHEA:41385 |
| Cross Reference Brenda |