| IED ID | IndEnz0005001121 |
| Enzyme Type ID | lipase001121 |
| Protein Name |
Gastric triacylglycerol lipase GL Gastric lipase EC 3.1.1.3 Lingual lipase |
| Gene Name | Lipf |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MWLLLITSVISTFGGAHGLFGKLGPGNPEANMNISQMITYWGYPCQEYEVVTEDGYILGVYRIPHGKNNSENIGKRPVVYLQHGLIASATNWIANLPNNSLAFMLADAGYDVWLGNSRGNTWSRKNVYYSPDSVEFWAFSFDEMAKYDLPATINFIVQKTGQEKIHYVGHSQGTTIGFIAFSTNPTLAKKIKTFYALAPVATVKYTQSPLKKISFIPTFLFKLMFGKKMFLPHTYFDDFLGTEVCSREVLDLLCSNTLFIFCGFDKKNLNVSRFDVYLGHNPAGTSVQDFLHWAQLVRSGKFQAFNWGSPSQNMLHYNQKTPPEYDVSAMTVPVAVWNGGNDILADPQDVAMLLPKLSNLLFHKEILAYNHLDFIWAMDAPQEVYNEMISMMAED |
| Enzyme Length | 395 |
| Uniprot Accession Number | P04634 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P07098; ACT_SITE 342; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 371; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| 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:0000269|PubMed:3839077}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753; Evidence={ECO:0000250|UniProtKB:P07098};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932; Evidence={ECO:0000250|UniProtKB:P07098}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol + H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:76979; Evidence={ECO:0000250|UniProtKB:P07098};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048; Evidence={ECO:0000250|UniProtKB:P07098}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:3839077). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098, ECO:0000269|PubMed:3839077}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:3839077 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12702486; 15809022; 27317984; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,588 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:39931; RHEA:39932; RHEA:40047; RHEA:40048 |
| Cross Reference Brenda |