| IED ID | IndEnz0002011752 |
| Enzyme Type ID | protease011752 |
| Protein Name |
Prolyl endopeptidase-like EC 3.4.21.- Prolylendopeptidase-like |
| Gene Name | PREPL |
| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Enzyme Sequence | MQQKTKLFLQALKYSIPHLGKCMQKQHLNHYNFADHYYNRIKLKKYHLTKCLQNKPKISELARNIPSRSFSCKDLQPVKQENEKPLPENMDAFEKVRTKLETQPQEEYEIINVEVKHGGFVYYQEGCCLVRSKDEEADNDNYEVLFNLEELKLDQPFIDCIRVAPDEKYVAAKIRTEDSEASTCVIIKLSDQPVMEASFPNVSSFEWVKDEEDEDVLFYTFQRNLRCHDVYRATFGDNKRNERFYTEKDPSYFVFLYLTKDSRFLTINIMNKTTSEVWLIDGLSPWDPPVLIQKRIHGVLYYVEHRDDELYILTNVGEPTEFKLMRTAADTPAIMNWDLFFTMKRNTKVIDLDMFKDHCVLFLKHSNLLYVNVIGLADDSVRSLKLPPWACGFIMDTNSDPKNCPFQLCSPIRPPKYYTYKFAEGKLFEETGHEDPITKTSRVLRLEAKSKDGKLVPMTVFHKTDSEDLQKKPLLVQVYGAYGIDLKMNFRPERRVLVDDGWILAYCHVRGGGELGLQWHADGRLTKKLNGLADLEACIKTLHGQGFSQPSLTTLTAFSAGGVLAGALCNSNPELLRAVTLEAPFLDVLNTMMDTTLPLTLEELEEWGNPSSDEKHKNYIKHYCPYQNIKPQHYPSIHITAYENDERVPLKGIVSYTEKLKEAIAEHAKDTGEGYQSPNIILDIQPGGNHVIEDSHKKITAQIKFLYEELGLDSTSVFEDLKKYLKF |
| Enzyme Length | 727 |
| Uniprot Accession Number | Q5RAK4 |
| Absorption | |
| Active Site | ACT_SITE 559; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6; ACT_SITE 645; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6; ACT_SITE 690; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine peptidase whose precise substrate specificity remains unclear (By similarity). 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 (By similarity). May play a role in the regulation of synaptic vesicle exocytosis (By similarity). {ECO:0000250|UniProtKB:Q4J6C6}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Sequence conflict (5) |
| Keywords | Alternative splicing;Cytoplasm;Cytoskeleton;Golgi apparatus;Hydrolase;Nucleus;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q4J6C6}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8C167}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8C167}. Golgi apparatus {ECO:0000250|UniProtKB:Q8C167}. Nucleus {ECO:0000250|UniProtKB:Q4J6C6}. Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity). Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity). Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By similarity). {ECO:0000250|UniProtKB:Q8C167}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 83,941 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |