| IED ID | IndEnz0002012187 |
| Enzyme Type ID | protease012187 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 30 EC 3.4.19.12 Deubiquitinating enzyme 30 Ubiquitin thioesterase 30 Ubiquitin-specific-processing protease 30 Ub-specific protease 30 |
| Gene Name | Usp30 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLSSRAQAARTAADKALQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLSLLKALSCQEVTEEEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEMAPRQVTCHTRGSPHPTTNPWKSQHPFHGRLSSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTQNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSQGTPLKRHEHVQFNEFLMMDFYKYRLLGHKPSQHGPKATESPGSALGVQDTQAAPKPGLSQPAAPKTQFFMNGACSPSLLPALPSPMAFPLPVAPDYSSSMYLFRLMAVVVHHGDMHSGHFVTYRRSPPSAKNPLSTSNQWLWISDDTVRKASLQEVLSSSAYLLFYERVLSRVQQQGREYRSEE |
| Enzyme Length | 517 |
| Uniprot Accession Number | D3ZPG5 |
| Absorption | |
| Active Site | ACT_SITE 77; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 452; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the diterpenoid derivative 15-oxospiramilactone (S3). {ECO:0000250|UniProtKB:Q3UN04}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q70CQ3}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy (PubMed:24896179). Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (By similarity). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity). {ECO:0000250|UniProtKB:Q3UN04, ECO:0000250|UniProtKB:Q70CQ3, ECO:0000269|PubMed:24896179}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Cross-link (2); Domain (1); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Hydrolase;Isopeptide bond;Membrane;Mitochondrion;Mitochondrion outer membrane;Protease;Reference proteome;Thiol protease;Transmembrane;Transmembrane helix;Ubl conjugation;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q70CQ3}. |
| Modified Residue | |
| Post Translational Modification | PTM: Ubiquitinated by parkin (PRKN) at Lys-235 and Lys-289, leading to its degradation. {ECO:0000250|UniProtKB:Q70CQ3}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,206 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |