| IED ID | IndEnz0005000763 |
| Enzyme Type ID | lipase000763 |
| Protein Name |
Triacylglycerol lipase ptl3 EC 3.1.1.3 |
| Gene Name | ptl3 SPAC1A6.05c |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MSKNEIKLQMEYASSYETWLEAAEKLDVIEGKYQWREQKESDEYDYVLVESRLHELRRHRLSKNTRLLLGLLRNSVARDFANMDNSRLYNYAHSGTKKLIDEFIQEVLMCLTYLEETPDLSLDEKITEFSRLKLTTGNTALILSGGGTFGMTHIGVLQSLHEQGLVPKIICGSSAGAIVACAAAVRNKEEQEILLRQFHTGDLSVFTDPNAAPPSVIQSVKQYFTRGCVLDISHLERVMKLLIGDFTFQEAYDRSGYILNVTVSCGSLFEMPSLLNYITAPNVLVWSAVVATCSVPFLFKRATLWERDPLTREVSAFCVTDAPLWMDGSVDNDIPHAKLTELFHVNHFIVSQVNFHIVPFIMDPTSHNWVERCCKKAIDLAAQEVSLTFRLFAELGIFSVLFTKLQSVITQKYSGDITIIPRLNYREVNKVIKNPTPSFLLDAATRGKRGTWTKVPVTRNHCAIEILIAAAYTRLIKRSKSLK |
| Enzyme Length | 483 |
| Uniprot Accession Number | Q9Y827 |
| Absorption | |
| Active Site | ACT_SITE 174; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 327; /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:Q12043}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways. {ECO:0000269|PubMed:22592553}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Motif (2) |
| Keywords | Cytoplasm;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Lipid droplet {ECO:0000250|UniProtKB:Q12043}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 23173672; 23697806; 28945192; 34250083; |
| Motif | MOTIF 145..150; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 172..176; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 54,684 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |