| IED ID | IndEnz0002006147 |
| Enzyme Type ID | protease006147 |
| Protein Name |
Prolyl endopeptidase-like EC 3.4.21.- Prolylendopeptidase-like |
| Gene Name | Prepl Kiaa0436 |
| 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 | MLQTAKFSLRALKHSIPHLGNCMQKQSYRNVAGPYYSRVRLKKYHLTKCLQNKPRIAGLARNIPSRSFSCKDLLPIKPESEKPISENMDAFEKVRTRLETQPQEEYEVVNAEIKHGGFVYYQEGCCLVRSKDEEADSDNYEVLFNLEELKLDQPFIDCIRVAPDEKYVAAKIRTEDSETSTLVVVKLSDQPVMEASFPNVSSFEWVKDEEDEDVLFYTFQRNLRCHDVYRATFGDNKRNERFYTEKDPSYFVFLYLTKDSRFLTLNIMNKTTSEVWLIDGLSPWDPPVLIQKRIHGMLYYVEHRDDELYILTNVGEPTEFKLMRTAADAPAIMNWDLFFTMKRNTKVVDLDMFKDHCVLFLKHSNLLYVNVIGLADDSVRSLKLPPWACGFIMDTNSDPKNCPFQLCSPIRPPKYYTYKFAEGKLFEETGHEDPITKTSRVLRIEAKSKDGKLVPMTVFHKTDSEDLQRKPLLVHVYGAYGMDLKMNFRPEKRVLVDDGWILAYCHVRGGGELGLQWHADGRLTKKLNGLADLVACIKTLHSQGFSQPSLTTLSAFSAGGVLVGALCNSKPELLRAVTLEAPFLDVLNTMLDTTLPLTLEELEEWGNPSSDEKHKNYIKRYCPCQNIKPQHYPSVHITAYENDERVPLKGIVNYTEKLKEAVAEHTKGAGEGYQPPNIILDIQPGGNHVIEDSHKKITTQMKFLYEELGLDSTDAFEALKKYLKF |
| Enzyme Length | 725 |
| Uniprot Accession Number | Q8C167 |
| Absorption | |
| Active Site | ACT_SITE 557; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21692504; ACT_SITE 643; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6; ACT_SITE 688; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 1-isobutyl-3-oxo-3,5,6,7-tetrahydro-2H-cyclopenta[c]pyridine-4-carbonitrile. {ECO:0000269|PubMed:21692504}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine peptidase whose precise substrate specificity remains unclear (PubMed:21692504). Does not cleave peptides after a arginine or lysine residue (By similarity). Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex (PubMed:23321636). May play a role in the regulation of synaptic vesicle exocytosis (By similarity). {ECO:0000250|UniProtKB:Q4J6C6, ECO:0000269|PubMed:21692504, ECO:0000269|PubMed:23321636}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (1); Mutagenesis (1) |
| Keywords | Alternative splicing;Cytoplasm;Cytoskeleton;Golgi apparatus;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23321636, ECO:0000269|PubMed:23485813}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23321636}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23485813}. Golgi apparatus {ECO:0000269|PubMed:23485813}. Nucleus {ECO:0000250|UniProtKB:Q4J6C6}. Note=Co-localizes with AP-1 in the trans-Golgi network (PubMed:23321636). Co-localizes with MAP2 and ACTB on the cytoskeleton (PubMed:23485813). Co-localizes with STX6 and GOSR2 at the Golgi apparatus (PubMed:23485813). {ECO:0000269|PubMed:23321636, ECO:0000269|PubMed:23485813}. |
| Modified Residue | MOD_RES 137; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 16615898; 18799693; 21267068; |
| Motif | |
| Gene Encoded By | |
| Mass | 83,194 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |