| IED ID | IndEnz0002011023 |
| Enzyme Type ID | protease011023 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 4 EC 3.4.19.12 Deubiquitinating enzyme 4 Ubiquitin thioesterase 4 Ubiquitin-specific-processing protease 4 Vacuole biogenesis protein SSV7 |
| Gene Name | DOA4 DOS1 MUT4 NPI2 SSV7 UBP4 SCY_0972 |
| Organism | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
| Enzyme Sequence | MEQNIISTIRDECIRHRSKYLTIAQLTAIAEAKINEFIITGKAKDQDLSSLLDKCIDILSIYKKNSKDIKNIISCKNKGAMISSNSVMIIQLNYVYYKVIHIIVTTNIPHLSEFAKIKLHKSTSDEGNGNNNNNEFQLMNIYNTLLETLLKDENIAKIKSFIKSSIKQTKLNHEQEECNLMRTGSYITSNQLNSLISSSANSTSSQMEILLIDIRSRLEFNKSHIDTKNIICLEPISFKMSYSDHDLEKKSLITSPNSEIKMFQSRNLFKFIILYTDANEYNVKQQSVLLDILVNHSFEKPISDDFTKIFILESGFPGWLKSNYGSQVSSSSPSNNNIKDDSVYINGNTSGLSLQHLPKMSPSIRHSMDDSMKEMLVAPTPLNHLQQQQQQQSDNDHVLKRSSSFKKLFSNYTSPNPKNSNSNLYSISSLSISSSPSPLPLHSPDPVKGNSLPINYPETPHLWKNSETDFMTNQREQLNHNSFAHIAPINTKAITSPSRTATPKLQRFPQTISMNLNMNSNGHSSATSTIQPSCLSLSNNDSLDHTDVTPTSSHNYDLDFAVGLENLGNSCYMNCIIQCILGTHELTQIFLDDSYAKHININSKLGSKGILAKYFARLVHMMYKEQVDGSKKISISPIKFKLACGSVNSLFKTASQQDCQEFCQFLLDGLHEDLNQCGSNPPLKELSQEAEARREKLSLRIASSIEWERFLTTDFSVIVDLFQGQYASRLKCKVCSHTSTTYQPFTVLSIPIPKKNSRNNITIEDCFREFTKCENLEVDEQWLCPHCKKRQPSTKQLTITRLPRNLIVHLKRFDNLLNKNNDFVIYPFLLDLTPFWANDFDGVFPPGVNDDELPIRGQIPPFKYELYGVACHFGTLYGGHYTAYVKKGLKKGWLYFDDTKYKPVKNKADAINSNAYVLFYHRVYGV |
| Enzyme Length | 926 |
| Uniprot Accession Number | A6ZY34 |
| Absorption | |
| Active Site | ACT_SITE 571; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 880; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| Activity Regulation | ACTIVITY REGULATION: RFU1 is an inhibitor of deubiquitination activity. {ECO:0000250}. |
| 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; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Involved in the ammonium-induced down-regulation of the GAP1 permease and the UME3 destruction in response to oxidative stress. Has a role in the RAD9 checkpoint response to TOP1 poisons. Required for promoting coordination of DNA replication and avoids DNA overreplication (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (2); Modified residue (1) |
| Keywords | Cytoplasm;Endosome;Hydrolase;Membrane;Phosphoprotein;Protease;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited to the late endosome by BRO1. {ECO:0000250}. |
| Modified Residue | MOD_RES 443; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P32571 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 105,092 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |