| IED ID | IndEnz0005000316 |
| Enzyme Type ID | lipase000316 |
| Protein Name |
Acyl-protein thioesterase 1 APT-1 EC 3.1.2.- Lysophospholipase 1 Lysophospholipase I LPL-I LysoPLA I Palmitoyl-protein hydrolase EC 3.1.2.22 |
| Gene Name | Lypla1 Apt1 Pla1a |
| 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 | MCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSPHIKYICPHAPVMPVTLNMNMAMPSWFDIVGLSPDSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSANRDISVLQCHGDCDPLVPLMFGSLTVERLKALINPANVTFKIYEGMMHSSCQQEMMDVKHFIDKLLPPID |
| Enzyme Length | 230 |
| Uniprot Accession Number | P97823 |
| Absorption | |
| Active Site | ACT_SITE 119; /note=Charge relay system; /evidence=ECO:0000269|PubMed:9139730; ACT_SITE 174; /note=Charge relay system; /evidence=ECO:0000269|PubMed:9268342; ACT_SITE 208; /note=Charge relay system; /evidence=ECO:0000269|PubMed:9268342 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniProtKB:O75608}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:O75608};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:O75608}; CATALYTIC ACTIVITY: Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57875, ChEBI:CHEBI:78421; Evidence={ECO:0000250|UniProtKB:O75608};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41721; Evidence={ECO:0000250|UniProtKB:O75608}; |
| DNA Binding | |
| EC Number | 3.1.2.-; 3.1.2.22 |
| Enzyme Function | FUNCTION: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS)(PubMed:9139730). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity). {ECO:0000250|UniProtKB:O75608, ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:9139730}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (1); Mutagenesis (3); Sequence conflict (1) |
| Keywords | Acetylation;Alternative splicing;Cell membrane;Cytoplasm;Direct protein sequencing;Endoplasmic reticulum;Fatty acid metabolism;Hydrolase;Lipid metabolism;Membrane;Nucleus;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75608}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}. |
| Modified Residue | MOD_RES 224; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23576753 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10064901; 11217851; 12466851; 14651853; 14681479; 22399288; 23396970; 24194600; 25271157; 27307232; 29084768; 29733200; 32233916; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,688 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19233; RHEA:40435; RHEA:40436; RHEA:41720; RHEA:41721 |
| Cross Reference Brenda |