| IED ID | IndEnz0002010921 |
| Enzyme Type ID | protease010921 |
| Protein Name |
Prolyl endopeptidase-like EC 3.4.21.- Prolylendopeptidase-like |
| Gene Name | prepl |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MMRNLAQQVGLFVCRISSGTSAWNSVISASYFSAGITRYSRSTVYRGYKAWQNLLDSEKRRWQRACAKYQGLVTSLEKRLCDMHQSYSTGDEKGMIIYEDYIYFQDNGCICRYKPNTGEDSLEVLLISEDLGLGDYEIQKIRVSPKQKFMAVTLKGYEREESTCVVVKLDNGPQVTHCIENVFSCEWATDRMLLHTSQVNVQCRQVFATDFSDANGAAQLVYTENDPRFFVDLYCTRDKRFITINSNSKSTSEVRLIDNRCPFEPPVLVQKRIAGVIYYIEHSNGCLYMLRRHGEAAEYKILKAAVSSGMKHWEPVYEVQERTKLVDMEMLKDHCLLFLKNHNQLSLEVIGLPSGAVLQSIKLPAWACALELDHQAEYGAGTVGFSLSSPVHPPVHFEYSLRKKQLSVDTNHSSDGIHQFHTLRLEAKSKDGTSVPLTLLYKDSEKQMRQRPLLIHVYGAYGMDLNMSFKVEKRMLVEEGWLLAYCHVRGGGELGCNWHSEGVLDKKLNGLEDLGSCISHLHGLGYSQPHYSAVEAASAGGVLAGALCNSAPRLFRAVVLEAPFLDVLNTMMNVSLPLTIEEQEEWGNPLSDEKYHRYIKSYCPYQNITPQNYPCVRITAYENDQRVPIQGLLGYITRLRKAARDYCHESGTSESRIPHIYLDVHPGGSHCDSLSWEESLRKVATQLAFLHMELKLDIPRRCKGSTQ |
| Enzyme Length | 707 |
| Uniprot Accession Number | Q32N48 |
| Absorption | |
| Active Site | ACT_SITE 538; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6; ACT_SITE 624; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q4J6C6; ACT_SITE 670; /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); Chain (1) |
| Keywords | Cytoplasm;Hydrolase;Protease;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q4J6C6}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,168 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |