| IED ID | IndEnz0002009221 | 
| Enzyme Type ID | protease009221 | 
| Protein Name | 
                        
                            
                                OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1  OTU domain-containing protein 1 EC 3.4.19.12 Deubiquitinating enzyme OTU1  | 
                    
| Gene Name | OTU1 At1g28120 F13K9.21 | 
| Organism | Arabidopsis thaliana (Mouse-ear cress) | 
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) | 
| Enzyme Sequence | MQNQIDMVKDEAEVAASISAIKGEEWGNCSSVEDQPSFQEEEAAKVPYVGDKEPLSSLAAEYQSGSPILLEKIKILDSQYIGIRRTRGDGNCFFRSFMFSYLEHILESQDRAEVDRIKVNVEKCRKTLQNLGYTDFTFEDFFALFLEQLDDILQGTEESISYDELVNRSRDQSVSDYIVMFFRFVTAGDIRTRADFFEPFITGLSNATVDQFCKSSVEPMGEESDHIHITALSDALGVAIRVVYLDRSSCDSGGVTVNHHDFVPVGITNEKDEEASAPFITLLYRPGHYDILYPKPSCKVSDNVGK | 
| Enzyme Length | 306 | 
| Uniprot Accession Number | Q8LG98 | 
| Absorption | |
| Active Site | ACT_SITE 89; /evidence=ECO:0000250|UniProtKB:Q96DC9; ACT_SITE 92; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q96DC9; ACT_SITE 259; /evidence=ECO:0000250|UniProtKB:Q96FW1; ACT_SITE 288; /evidence=ECO:0000250|UniProtKB:Q96DC9 | 
| Activity Regulation | ACTIVITY REGULATION: Cleavage activities for 'Lys-48'- and 'Lys-63'-linked ubiquitin (UB) tetramers is inhibited by UB aldehyde and N-ethylmaleimide but not by the metalloprotease inhibitors 1,10-phenanthroline and EDTA, and the serine protease inhibitor phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:24659992}. | 
| 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:0000269|PubMed:24659992}; | 
| DNA Binding | |
| EC Number | 3.4.19.12 | 
| Enzyme Function | FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation (PubMed:24659992). Cysteine protease with a preference for Met-1 and 'Lys-48' over 'Lys-63'-linked ubiquitin (UB) tetramers (e.g. Ub2, Ub3 and Ub4) as substrates (PubMed:24659992). {ECO:0000269|PubMed:24659992}. | 
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:24659992}; | 
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Chain (1); Domain (1); Mutagenesis (3); Sequence conflict (1) | 
| Keywords | Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway | 
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | 21798944; 31491807; | 
| Motif | |
| Gene Encoded By | |
| Mass | 34,434 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |