IED ID | IndEnz0005000036 |
Enzyme Type ID | lipase000036 |
Protein Name |
GPI inositol-deacylase EC 3.1.-.- Post-GPI attachment to proteins factor 1 |
Gene Name | Pgap1 |
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 | MFLHSVNLWNLAFYVFMVFLATLGLWDVFFGFEENKCSMSYMFEYPEYQKIELPKKLTKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQVRSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKAILKLYKGQEFAPTSVAIIGHSMGGLVARALLTLKNFKQDLINLLVTQATPHVAPVMPLDRFITEFYMNVNNYWILNARHINLTTLSVAGGFRDYQVRSGLTFLPKLSHYTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTIRAFFDLIDADTKQITQKPKKKLSVLNHHFIRHPAKQFEENPSIISDLTGTSMWVPVKVSRWSYVAYNESDKIYFAFPLANHRKIYTHAYCQSTMLDTNSWIFGCINSTSMCRQGVDLSWKAELLPTIKSLTLRLQDYPSLSHIVVYVPSVHGSKFVVDCEFFKKEARSMQLPVTHLFSFGLSSRKVTLNTNGLYYNIELLNFGQIYQAFKVNVVSKCTGSKEEITSIYKLHIPWSYEDSLTIAQVPSSTDISLKLHVAQPENDSHVALLKMYTSSDCQYEVTIKTSFPQILGQVVRFHGGALPAYVVSSILLAYGGQLYSLLSTGYCLEYSTILDKEAKPYKVDPFVIMIKFLLGYKWFKELWDAVLLPELDAIVLTSQSMCFPLVSLILFLFGTCTAYWSGLLSSTSVQLLSSLWLALKRPAELPKDIKVMSPDLPVLTVVFLIVSWTTCGALAILLSYLYYVFKVVHLQASLTTFKNNQPVNPKHSRRSEKKSNHHKDSAVQSLRLCANDAEDSLRMHSTVINLLTWVVLLSMPSLIYWLKNLRYYFKLSPDPCKPLAFLLIPAIAILGNTHTVSVKSSKLLKTVSQFPLPLAVGVIAFGSSHLYRVPCFVIIPLVFHALCNFM |
Enzyme Length | 922 |
Uniprot Accession Number | Q3UUQ7 |
Absorption | |
Active Site | ACT_SITE 174; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.1.-.- |
Enzyme Function | FUNCTION: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (3); Region (1); Sequence conflict (2); Topological domain (9); Transmembrane (8) |
Keywords | Alternative splicing;Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10529425; 11217851; 12466851; 14610273; 14681479; 15235602; 16107646; 17329413; 17711852; 19593386; 20562862; 21267068; 23213481; 26273529; 28706241; 4019727; 5289032; |
Motif | |
Gene Encoded By | |
Mass | 104,578 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |