| IED ID | IndEnz0005000570 |
| Enzyme Type ID | lipase000570 |
| Protein Name |
Lipase lipl-4 EC 3.1.1.- EC 3.1.1.3 Lipase-like 4 |
| Gene Name | lipl-4 K04A8.5 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MRESISDLMTVMIPLLIILLLSNYSKSVDLEFYLDTPELIKSWGYSVEIYNTTTKDGFILELHRIPYGREVPTSSDVNNSRPVIFLQHGFLCSSFDWVANSPHQSAGFVFADAGFDVWLGNFRGNTYSRKHVSLNPDKDPKFWDWSWDQISEYDLPAMIGKALEISGQESLYYTGFSLGTLTMFAKLSTDPKFSRKIKKYFALAPIGSIKHAHGVFLFLGRHFGKDYEEYVKKHGSDELFGSSLLFKKIVKYTCGLFDTLEEFCSDITLLFIGTANENWNQTRIPVYLAHTPAGSSSNVMAHLDQMFSYGGVPTFDMGEEKNLKAYGQKLPPQYNFTGIADVPIYLFWSDDDWLSTKQDLEETLFAQLNSQVVQGSFRIENYNHLHFIWGTNAASQVYNVITGIILQDDNT |
| Enzyme Length | 411 |
| Uniprot Accession Number | Q94252 |
| Absorption | |
| Active Site | ACT_SITE 177; /note=Nucleophile; /evidence=ECO:0000255|PIRSR:PIRSR000862-1; ACT_SITE 352; /note=Charge relay system; /evidence=ECO:0000255|PIRSR:PIRSR000862-1; ACT_SITE 384; /note=Charge relay system; /evidence=ECO:0000255|PIRSR:PIRSR000862-1 |
| 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:0000305|PubMed:21906946}; 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:0000305|PubMed:25554789}; |
| DNA Binding | |
| EC Number | 3.1.1.-; 3.1.1.3 |
| Enzyme Function | FUNCTION: Lysosomal lipase that regulates the metabolism of long-chain fatty acids, primarily in response to nutrient availability (PubMed:21906946, PubMed:23392608, PubMed:25554789, PubMed:30713071). The production of these lipid signaling mediators regulates various processes, including lipolysis, autophagy, mitochondrial beta-oxidation, which in turn control lifespan and adaptation to starvation (PubMed:21906946, PubMed:23392608, PubMed:25554789, PubMed:30713071). In response to fasting, promotes the production of omega-6 polyunsaturated fatty acids (PUFAs), which in turn activates autophagy resulting in lifespan extension (PubMed:23392608). Produces oleoylethanolamide (OEA), a ligand for the lysosomal lipid chaperone lbp-8 which translocates into the nucleus where it activates the transcription of genes promoting longevity and activation of mitochondrial beta oxidation (PubMed:25554789, PubMed:30713071). {ECO:0000269|PubMed:21906946, ECO:0000269|PubMed:23392608, ECO:0000269|PubMed:25554789, ECO:0000269|PubMed:30713071}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is acidic. {ECO:0000305|PubMed:25554789}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Glycosylation (4); Signal peptide (1) |
| Keywords | Alternative splicing;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in the intestine by fasting. {ECO:0000269|PubMed:23392608, ECO:0000269|PubMed:23604316}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:25554789}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17592649; 18988854; 21367940; 22286215; 22560298; 23800452; 25487147; 34607947; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,773 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:38575 |
| Cross Reference Brenda |