| IED ID | IndEnz0005000394 |
| Enzyme Type ID | lipase000394 |
| Protein Name |
Lipase member H EC 3.1.1.- Lacrimal lipase |
| Gene Name | LIPH |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MLRFYLFISLLCLVRSDTDETCPSFTKLSFHSAVVGTELNVRLLLYTRKNYTCAQIINSTTFGNLNVTKKTTFVVHGFRPTGSPPVWLQDLVKALLMVEDMNLVVVDWNRGATTVIYTQASNKTRKVAIILKEFIDQMLARGASLDDIYMIGVSLGAHISGFVGKMYNGQLGRITGLDPAGPLFNGKPPQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGVDQPGCPKTIFEAGMQYFKCDHQMSVYLYLSSLRKNCTITAYPCDSYRDYRNGKCINCGLPQGKPCPLLGYYADNWKDYLSEKDPPMTKAFFDTAEKEPYCMYHYFVDIITWNKSIRRGSITIKLKDEAGNTTESKINHEPVTFEKYHQVSLLARFNQDLDKVAEISLVFSTGAVIGPKYKLRILRMKLRSLAHPERPQLCRYDLVLTENVETPFQPIVCQKLQM |
| Enzyme Length | 452 |
| Uniprot Accession Number | Q9BDJ4 |
| Absorption | |
| Active Site | ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 178; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 249; /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); Chain (1); Disulfide bond (4); Glycosylation (4); Signal peptide (1) |
| Keywords | 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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,164 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:40943; RHEA:40944 |
| Cross Reference Brenda |