Detail Information for IndEnz0002009229
IED ID IndEnz0002009229
Enzyme Type ID protease009229
Protein Name Ubiquitin thioesterase OTU1
EC 3.4.19.12
Gene Name Yod1
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 MFGGAKGGHFGVPPAGYSGAVPQSEAGTKAGPAGGRPADTMWRVRCKAKGGTHLLQGLSSRTRLRELQGQIAAITGIAPGSQRILVGYPPECLDLSDRDITLGDLPIQSGDMLIVEEDQTRPKASPAFSKYGAPSYVREALPVLTRTAVPADNSCLFTSVYYVVEGGVLNPACAPEMRRLIAQIVASDPVLYSEAILGKTNEDYCDWIRRDDTWGGAIEISILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRKRQFTDVNRFTLRCMICQKGLTGQAEARDHARETGHTNFGEV
Enzyme Length 343
Uniprot Accession Number Q8CB27
Absorption
Active Site ACT_SITE 152; /evidence=ECO:0000250|UniProtKB:Q96FW1; ACT_SITE 155; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 262; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 337; /evidence=ECO:0000250|UniProtKB:Q96FW1
Activity Regulation
Binding Site BINDING 261; /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. May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome membranes decorated with K48-linked ubiquitin chains and remove these chains allowing autophagosome formation. {ECO:0000250|UniProtKB:Q5VVQ6}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (4); Beta strand (4); Binding site (1); Chain (1); Domain (1); Erroneous termination (1); Frameshift (1); Helix (1); Region (5); Turn (2); Zinc finger (1)
Keywords 3D-structure;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Unfolded protein response;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}. Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. {ECO:0000250|UniProtKB:Q5VVQ6}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 2KZR;
Mapped Pubmed ID 11217851; 12466851; 21267068; 23243279; 24194600; 28416659; 29330040; 30952814; 31916733;
Motif
Gene Encoded By
Mass 37,485
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda