IED ID | IndEnz0002009232 |
Enzyme Type ID | protease009232 |
Protein Name |
Ubiquitin thioesterase OTU1 EC 3.4.19.12 |
Gene Name | yod1 |
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 | MLRLRCKTREGTQLLQGLTDRSSIRELQERIAGVTGISGPLQRVMVGFPPLSLDLSDEEATLKNMSIKSGDTLIVEEDKSKLRSATPPVSKTDIGNWNAPAQPTIVRRVVPADNSCLFTSIYYVVEGGVYDPACALEMRSLIAEIVASDQSAYCDAVLGKSNEEYCSWIRREDTWGGAIEVSILSKFYQCEICVVDTQTVRIDRFGEDSGYTKRVLLIYDGIHYDPLQRQFPDPDMPPMTVFSTTDDEALVQAMELADDARKKRQFTDVNQFALRCMACQKGLTGQSAARDHAKETGHTNFGEV |
Enzyme Length | 304 |
Uniprot Accession Number | Q0IH43 |
Absorption | |
Active Site | ACT_SITE 113; /evidence=ECO:0000250|UniProtKB:Q96FW1; ACT_SITE 116; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 223; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 298; /evidence=ECO:0000250|UniProtKB:Q96FW1 |
Activity Regulation | |
Binding Site | BINDING 222; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q5VVQ6 |
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:Q5VVQ6}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. {ECO:0000250|UniProtKB:Q5VVQ6}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (4); Binding site (1); Chain (1); Domain (1); Region (5); Zinc finger (1) |
Keywords | Cytoplasm;Hydrolase;Metal-binding;Protease;Thiol protease;Ubl conjugation pathway;Unfolded protein response;Zinc;Zinc-finger |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 33,807 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |