Detail Information for IndEnz0002013681
IED ID IndEnz0002013681
Enzyme Type ID protease013681
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 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 MLSSRAQAARTAADKALQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLNLLKALSCQEVTEDEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEMAPRQVTCHTRGSPHPTTNHWKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEARGTLTGEKVEHQRSTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDFYKYRLLGHKPSQHGPKATENPGSAPEVQDAQAAPKPGLSQPGAPKTQIFLNGACSPSLLPALPSPVAFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPSAKNPLSTSNQWLWISDDTVRKASLQEVLSSSAYLLFYERVLSRVQQQGREYRSEE
Enzyme Length 517
Uniprot Accession Number Q3UN04
Absorption
Active Site ACT_SITE 77; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000269|PubMed:24513856"; ACT_SITE 452; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000269|PubMed:24513856"
Activity Regulation ACTIVITY REGULATION: Inhibited by the diterpenoid derivative 15-oxospiramilactone (S3). {ECO:0000269|PubMed:24513856}.
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. 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 (PubMed:24513856). {ECO:0000250|UniProtKB:Q70CQ3, ECO:0000269|PubMed:24513856}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Cross-link (2); Domain (1); Erroneous initiation (1); Mutagenesis (4); Region (2); 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:0000269|PubMed:24513856}.
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 10725249; 12466851; 12520002; 21267068; 32142684; 34648346;
Motif
Gene Encoded By
Mass 58,221
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda