| IED ID | IndEnz0005000853 |
| Enzyme Type ID | lipase000853 |
| Protein Name |
Lipase lipl-5 EC 3.1.1.- Lipase-like 5 |
| Gene Name | lipl-5 ZK6.7 |
| 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 | MWRFAVFLAAFFVQDVVGSHGDPELHMTTPQIIERWGYPAMIYTVATDDGYILEMHRIPFGKTNVTWPNGKRPVVFMQHGLLCASSDWVVNLPDQSAGFLFADAGFDVWLGNMRGNTYSMKHKDLKPSHSAFWDWSWDEMATYDLNAMINHVLEVTGQDSVYYMGHSQGTLTMFSHLSKDDGSFAKKIKKFFALAPIGSVKHIKGFLSFFANYFSLEFDGWFDIFGAGEFLPNNWAMKLAAKDICGGLKVEADLCDNVLFLIAGPESDQWNQTRVPVYATHDPAGTSTQNIVHWMQMVHHGGVPAYDWGTKTNKKKYGQANPPEYDFTAIKGTKIYLYWSDADWLADTPDVPDYLLTRLNPAIVAQNNHLPDYNHLDFTWGLRAPDDIYRPAIKLCTDDYLGK |
| Enzyme Length | 403 |
| Uniprot Accession Number | O61866 |
| Absorption | |
| Active Site | ACT_SITE 167; /note=Nucleophile; /evidence=ECO:0000255|PIRSR:PIRSR000862-1; ACT_SITE 343; /note=Charge relay system; /evidence=ECO:0000255|PIRSR:PIRSR000862-1; ACT_SITE 375; /note=Charge relay system; /evidence=ECO:0000255|PIRSR:PIRSR000862-1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Lipase involved in lipid homeostasis (PubMed:31676440). Regulates mitochondrial lipid composition, in particular cardiolipins and coenzyme Q-9 levels, in response to nutrient availability (PubMed:31676440). Does not affect global triglyceride levels in response to nutrient availability (PubMed:31676440). However, in coelomocytes, specifically promotes triglyceride catabolism and lifespan extension in response to nutrient deprivation (PubMed:31340142). {ECO:0000269|PubMed:31340142, ECO:0000269|PubMed:31676440}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (1); Glycosylation (2); Signal peptide (1) |
| Keywords | Alternative splicing;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated by fasting. {ECO:0000269|PubMed:31340142}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:31340142}. Secreted {ECO:0000269|PubMed:31340142}. Note=Localizes to lysosomes in coelomocytes. {ECO:0000269|PubMed:31340142}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 12176330; 12529635; 12529643; 21980510; 22267497; 22286215; 22560298; 23800452; 24884423; 25487147; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,704 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |