| IED ID | IndEnz0005000334 |
| Enzyme Type ID | lipase000334 |
| Protein Name |
Lipase lipl-1 EC 3.1.1.- Lipase-like 1 |
| Gene Name | lipl-1 F54F3.3 |
| 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 | MRSWSTVMLAVLATAATVFGHDADPEMKMTTPQIIMRWGYPAMIYDVTTEDGYILELHRIPYGKTNVTWPNGKKPVVFMQHGLECSSSNWVVNLPTESAAFLFADAGYDVWLGNFRGNTYSMKHKNLKPSHSAFWDWSWDEMQQYDLPAMIEKALEVTGQDSLYYIGHSQGTLTMFSRLSEDKVGWGNKIKKFFALAPVGSVKHIKGALKFFADYFSLEFDGWFDVFGSGEFLPNNWIMKLVSESVCAGLKVEAGVCDDVMFLIAGPESNQLNATRVPIYVAHTPAGTSTQNIVHWIQMVRHGGTPKYDYGEKGNKKHYGQANVPAYDFTTVNRPVYLYWGDSDWLADPTDVTDFLLTHLNPSTVVQNNKLIDYNHLDFIWGLRAPKDIYEPIIDIVRNDVLNGS |
| Enzyme Length | 405 |
| Uniprot Accession Number | Q93789 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Nucleophile; /evidence=ECO:0000255|PIRSR:PIRSR000862-1; ACT_SITE 344; /note=Charge relay system; /evidence=ECO:0000255|PIRSR:PIRSR000862-1; ACT_SITE 376; /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 that, together with lipl-3, plays a role in the response to nutrient deprivation by controlling lipid metabolism (PubMed:23604316). Specifically, involved in the breakdown of lipids during lipophagy, a process during which lipids contained in lipid droplets that have been delivered to lysosomes by autophagy are degraded (PubMed:23604316). {ECO:0000269|PubMed:23604316}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is acidic. {ECO:0000305|PubMed:23604316}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (2); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in the intestine by fasting (PubMed:23604316). Down-regulated in response to a high-glucose diet (PubMed:29113111). {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:29113111}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604316}. Lysosome lumen {ECO:0000269|PubMed:23604316}. Note=Secreted into the intestinal lumen. {ECO:0000269|PubMed:23604316}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 15338614; 17486083; 17850180; 22267497; 22560298; 23800452; 24884423; 25487147; 27506200; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,790 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |