| IED ID | IndEnz0005000387 |
| Enzyme Type ID | lipase000387 |
| Protein Name |
Lipase member I LIPI EC 3.1.1.- Cancer/testis antigen 17 CT17 LPD lipase Membrane-associated phosphatidic acid-selective phospholipase A1-beta mPA-PLA1 beta |
| Gene Name | LIPI LPDL PRED5 |
| 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 | MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLLNQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQSLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT |
| Enzyme Length | 460 |
| Uniprot Accession Number | Q6XZB0 |
| Absorption | |
| Active Site | ACT_SITE 159; /note=Nucleophile; ACT_SITE 183; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 253; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by sodium vanadate. {ECO:0000269|PubMed:12963729}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839, ChEBI:CHEBI:77593; Evidence={ECO:0000269|PubMed:12963729};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000305|PubMed:12963729}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG). {ECO:0000269|PubMed:12963729}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (9); Chain (1); Disulfide bond (4); Glycosylation (2); Mutagenesis (1); Natural variant (4); Sequence conflict (1); Signal peptide (1) |
| Keywords | Alternative splicing;Cell membrane;Disease variant;Disulfide bond;Glycoprotein;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:12963729}. Secreted {ECO:0000269|PubMed:12963729}. Note=May associate with lipid draft. {ECO:0000269|PubMed:12963729}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:12963729}. Secreted {ECO:0000269|PubMed:12963729}. Note=May associate with lipid draft. {ECO:0000269|PubMed:12963729}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12063250; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,922 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:40943; RHEA:40944 |
| Cross Reference Brenda | 3.1.1.111;3.1.1.32; |