| IED ID | IndEnz0005001175 |
| Enzyme Type ID | lipase001175 |
| Protein Name |
Lipase member H EC 3.1.1.- |
| Gene Name | Liph |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MLRLCFFISFMCLVKSDTDETCPSFTRLSFHSAVVGTGLSVRLMLYTQRDQTCAQIINSTALGSLNVTKKTTFIIHGFRPTGSPPVWIEELVQSLISVQEMNVVVVDWNRGATTVIYPHASSKTRQVASILKEFIDQMLVKGASLDNIYMIGVSLGAHIAGFVGESYEGKLGRVTGLDPAGPLFNGRPPEERLDPSDALFVDVIHSDTDALGYKEALGHIDFYPNGGLDQPGCPKTIFGGIKYFKCDHQMSVYLYLASLQNNCSITAYPCDSYRDYRNGKCVSCGAGQIVPCPRVGYYADSWKEYLWDRDPPMTKAFFDTAETKPYCMYHYFVDIVSWNKSVRRGFITIKLRGEDGNITESKIDHEPSAFEKYHQVSLLARFNRDLDKVAEISLLFSTGSVVGPKYKLRVLQMKLRSLAHPDRPHLCRYDLVLMENVETSFQPILCSQQQM |
| Enzyme Length | 451 |
| Uniprot Accession Number | Q8CIV3 |
| Absorption | |
| Active Site | ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 178; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 248; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| 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:0000250|UniProtKB:Q8WWY8};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000250|UniProtKB:Q8WWY8}; |
| 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 (By similarity). Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG) (By similarity). {ECO:0000250|UniProtKB:Q8WWY8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Glycosylation (1); Sequence conflict (4); Signal peptide (1) |
| Keywords | Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8WWY8}. Cell membrane {ECO:0000250|UniProtKB:Q8WWY8}; Peripheral membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11210182; 11217851; 12466851; 12719377; 12904583; 14610273; 16254318; 21267068; 21857648; 22465231; 23677168; 26992132; 9250875; 9499429; 9774969; 9811942; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,675 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:40943; RHEA:40944 |
| Cross Reference Brenda |