| IED ID | IndEnz0005001119 |
| Enzyme Type ID | lipase001119 |
| Protein Name |
Endothelial lipase EC 3.1.1.3 Endothelial-derived lipase EDL Phospholipase A1 EC 3.1.1.32 |
| Gene Name | Lipg |
| 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 | MRDPVFLLGFWSLYCCFPAGSLTTLRPQGSLRDEHHKPTGVPVTITTKPSVTFNIRTSKDPEHEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQTREKEANVVVVDWLPLAHQLYIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTLSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFAYGTISEMVKCEHERAVHLFVDSLVNQDKPSFAFQCTDPNRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFRVYHYQLKVHMFSYKNSGDIQPDLYITLYGSNADSQNLPLEIVEKIELNATNTFLVYTEEYLGDLFKIRLTWEGVSSSWYNLWNEFRSYLSQPSSPSRELHIRRIRVKSGETQRKVAFCVQDPMKNSISPGQELWFYKCQNDCRVKN |
| Enzyme Length | 493 |
| Uniprot Accession Number | Q8VBX1 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 195; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 276; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | |
| 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:0000250|UniProtKB:Q9Y5X9}; 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:Q9Y5X9}; 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:Q9Y5X9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:Q9Y5X9}; 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:Q9Y5X9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:Q9Y5X9}; 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:Q9Y5X9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000250|UniProtKB:Q9Y5X9}; |
| DNA Binding | |
| EC Number | 3.1.1.3; 3.1.1.32 |
| Enzyme Function | FUNCTION: Exerts both phospholipase and triglyceride lipase activities (By similarity). More active as a phospholipase than a triglyceride lipase (By similarity). Hydrolyzes triglycerides, both with short-chain fatty acyl groups (tributyrin) and long-chain fatty acyl groups (triolein) with similar levels of activity toward both types of substrates (By similarity). Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins (By similarity). {ECO:0000250|UniProtKB:Q9Y5X9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Region (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y5X9}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11380807; 12551943; 1935790; 19931348; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,924 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:18689; RHEA:38575; RHEA:38576; RHEA:40475; RHEA:40476; RHEA:41384; RHEA:41385 |
| Cross Reference Brenda |