| IED ID | IndEnz0005000826 |
| Enzyme Type ID | lipase000826 |
| Protein Name |
Patanin-like phospholipase domain-containing protein atgl-1 EC 3.1.1.3 Adipose triglyceride lipase 1 |
| Gene Name | atgl-1 C05D11.7 |
| 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 | MTMINSRPELMNLSFSGCGFLCVYHAGVAAAIKEYAPELLQNKILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEFNLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGGVSDNQPIYDEHTVTVSPFSGESDICPPDWDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALRFLTKCGLAPCIRCLTIQTIDANEPAGRVSSECFSENDDAKKVTHVAVPRMKKRASANALNSFRTRGESECETCGDSDIPLEEVNIQSFFPSIMKKPFEDAVAAERSVFQYMMSFRLVRYATTAMGISKFPFDMALAFVKKVHQYLDMVSPPRWIMLKFRGLADFILGEVEKQKSRYTNFSCLVAVAETDSFGSVLASSTMEKEEHKEIELSEDAKKEMILLRERDRRRKLLKKAGKITPNNSENQFDETSVYDVDSFEHVIDFTKSHEALYEFHYRDENQVMKTFGLFTDSQQRPYSSASQHQHHHTKSLGGTSRLVHVPEEDEDAPLSAVSAPAVIFHGGQEIVELGESDKDSGLSGIDTKRKVPDEPTTRF |
| Enzyme Length | 621 |
| Uniprot Accession Number | Q11186 |
| Absorption | |
| Active Site | ACT_SITE 48; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 167; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| 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:Q96AD5}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (By similarity). Component of a feedback loop involving atfs-1, atgl-1 and hlh-11 (PubMed:33078707). Promotes fat oxidation in response to mitochondrial stress (PubMed:33078707). May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion (PubMed:19052547, PubMed:20176933, PubMed:24120942, PubMed:25202121, PubMed:26083785, PubMed:26098762). Acts coordinately with lid-1 within the lipolytic cascade to distribute stored energy to tissues (PubMed:25202121). Together with lipid droplet protein cgi-58, regulates lipid reserves as well as lipid droplet size and localization during the dauer phase in response to phosphorylation by ampk (PubMed:19052547, PubMed:26083785, PubMed:26098762). May regulate serotonin-mediated lipolysis in metabolic tissues (PubMed:24120942). {ECO:0000250|UniProtKB:Q96AD5, ECO:0000269|PubMed:19052547, ECO:0000269|PubMed:20176933, ECO:0000269|PubMed:24120942, ECO:0000269|PubMed:25202121, ECO:0000269|PubMed:26083785, ECO:0000269|PubMed:26098762, ECO:0000269|PubMed:33078707}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000250|UniProtKB:Q96AD5}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Motif (2); Mutagenesis (1); Region (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cytoplasm;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Ubl conjugation |
| Interact With | |
| Induction | INDUCTION: May be induced by serotonin. {ECO:0000269|PubMed:24120942}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:20176933, ECO:0000269|PubMed:25202121, ECO:0000269|PubMed:26083785, ECO:0000269|PubMed:26098762}. Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:26098762}. Note=Accumulates in the cytoplasm when phosphorylated and within lipid droplets when unphosphorylated during the dauer phase (PubMed:26098762). Localization on lipid droplets enhanced by interaction with cgi-58 (PubMed:26083785). {ECO:0000269|PubMed:26083785, ECO:0000269|PubMed:26098762}. |
| Modified Residue | MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19052547, ECO:0000269|PubMed:25202121, ECO:0000269|PubMed:26098762" |
| Post Translational Modification | PTM: Phosphorylation at Ser-303 by aak-2 results in possible instability and cytoplasmic accumulation during the dauer phase. {ECO:0000269|PubMed:19052547, ECO:0000269|PubMed:26098762}.; PTM: Ubiquitinated (PubMed:25202121, PubMed:26098762). Ubiquitination may decrease upon phosphorylation by kin-1 (PubMed:25202121). {ECO:0000269|PubMed:25202121, ECO:0000269|PubMed:26098762}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 12097347; 15338614; 17164286; 17850180; 19343510; 21085631; 21177967; 22267497; 22347378; 22500807; 22560298; 22921415; 23496871; 23800452; 24884423; 24921650; 25487147; 28545126; 31311719; 6593563; |
| Motif | MOTIF 46..50; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 167..169; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 69,364 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |