| IED ID | IndEnz0005000375 |
| Enzyme Type ID | lipase000375 |
| Protein Name |
Gastric triacylglycerol lipase GL Gastric lipase EC 3.1.1.3 |
| Gene Name | LIPF |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK |
| Enzyme Length | 398 |
| Uniprot Accession Number | P07098 |
| Absorption | |
| Active Site | ACT_SITE 172; /note=Nucleophile; /evidence=ECO:0000269|PubMed:10358049; ACT_SITE 343; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10358049; ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10358049 |
| 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:10358049, ECO:0000269|PubMed:2243091}; 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:0000269|PubMed:2243091};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932; Evidence={ECO:0000305|PubMed:2243091}; 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:0000269|PubMed:2243091};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048; Evidence={ECO:0000305|PubMed:2243091}; |
| 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:2243091, PubMed:10358049). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (PubMed:2243091). {ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (12); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (4); Helix (23); Natural variant (3); Sequence conflict (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | Q6FHY5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:2753032 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1HLG; |
| Mapped Pubmed ID | 11940604; 12941646; 16385451; 18681781; 18996102; 19913121; 20043075; 20602615; 20628086; 20885390; 20965171; 21163940; 21945702; 25059952; 27498782; 28694218; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,238 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:39931; RHEA:39932; RHEA:40047; RHEA:40048 |
| Cross Reference Brenda |