| IED ID | IndEnz0002012736 |
| Enzyme Type ID | protease012736 |
| Protein Name |
Thimet oligopeptidase EC 3.4.24.15 |
| Gene Name | Thop1 |
| 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 | MKPPAACAGDVVDAASPASTVNHLRWDLSAQQIRALTTQLIEQTKCVYDRVGAQNFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPCKDIRAASTEADKKLSEFDVEMSMRQDVYQRVVWLQEKTPKNSLKPEAARYLERLIKLGRRNGLHLPQDTQEKIKNIKKRLSLLCIDFNKNLNEDTTFLPFTREELGGLPEDFLSSLEKAEDGKLKVTLKYPHYFPLLKKCHVPETRRLLEEAFNCRCKEENCAILKELVSLRAQKSSLLGFHTHADYVLEMNMAKTSQTVATFLDELAQKLKPLGEQERAVILELKEAECAKRGLPFDGRIHAWDMRYYMNQVEETRYRVDQNLLKEYFPMQVVTRGLLAIYQELLGLTFTLEEGAAAWHEDVRLYSVRDAASGEEIGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQLAVAAMVANFTKPTPDAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEKEPLMRMSQHYRTGSEAPQDLLEKLIKSRQANAGLFNLRQIVLAKVDQVLHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLSPKVGMDYRTSILRPGGSEDASAMLKQFLGRDPKQDAFLLSKGLQVEGSEAPAC |
| Enzyme Length | 687 |
| Uniprot Accession Number | Q8C1A5 |
| Absorption | |
| Active Site | ACT_SITE 474; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.; EC=3.4.24.15; |
| DNA Binding | |
| EC Number | 3.4.24.15 |
| Enzyme Function | FUNCTION: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Modified residue (5); Sequence conflict (5) |
| Keywords | Acetylation;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 16; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52888; MOD_RES 172; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 257; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P52888; MOD_RES 278; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:18034455; MOD_RES 538; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P52888 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10984455; 12466851; 12520002; 14610273; 15287887; 15741177; 17620116; 18571100; 18799693; 20456597; 21267068; 21677750; 24216478; 31431000; 32079362; |
| Motif | |
| Gene Encoded By | |
| Mass | 78,026 |
| Kinetics | |
| Metal Binding | METAL 473; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 477; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 480; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.15; |