| IED ID | IndEnz0002010027 |
| Enzyme Type ID | protease010027 |
| 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 YDR069C D4270 YD8554.02C YD9609.23C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (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 ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MEQNIISTIRDECIRHRSKYLTIAQLTAIAEAKINEFIITGKAKDQDLSSLLDKCIDILSIYKKNSKDIKNIISCKNKGAMISSNSVMIIQLNYVYYKVIHIIVTTNIPHLSEFAKIKLHKSTSDEGNGNNNNNEFQLMNIYNTLLETLLKDENIAKIKSFIKSSIKQTKLNHEQEECNLMRTGSYITSNQLNSLISSSANSASSQMEILLIDIRSRLEFNKSHIDTKNIICLEPISFKMSYSDHDLEKKSLITSPNSEIKMFQSRNLFKFIILYTDANEYNVKQQSVLLDILVNHSFEKPISDDFTKIFILESGFPGWLKSNYGRQVSSSFPSNNNIKDDSVYINGNTSGLSLQHLPKMSPSIRHSMDDSMKEMLVAPTPLNHLQQQQQQQSDNDHVLKRSSSFKKLFSNYTSPNPKNSNSNLYSISSLSISSSPSPLPLHSPDPVKGNSLPINYPETPHLWKNSETDFMTNQREQLNHNSFAHIAPINTKAITSPSRTATPKLQRFPQTISMNLNMNSNGHSSATSTIQPSCLSLSNNDSLDHTDVTPTSSHNYDLDFAVGLENLGNSCYMNCIIQCILGTHELTQIFLDDSYAKHININSKLGSKGILAKYFARLVHMMYKEQVDGSKKISISPIKFKLACGSVNSLFKTASQQDCQEFCQFLLDGLHEDLNQCGSNPPLKELSQEAEARREKLSLRIASSIEWERFLTTDFSVIVDLFQGQYASRLKCKVCSHTSTTYQPFTVLSIPIPKKNSRNNITIEDCFREFTKCENLEVDEQWLCPHCEKRQPSTKQLTITRLPRNLIVHLKRFDNLLNKNNDFVIYPFLLDLTPFWANDFDGVFPPGVNDDELPIRGQIPPFKYELYGVACHFGTLYGGHYTAYVKKGLKKGWLYFDDTKYKPVKNKADAINSNAYVLFYHRVYGV |
| Enzyme Length | 926 |
| Uniprot Accession Number | P32571 |
| Absorption | |
| Active Site | ACT_SITE 571; /note="Nucleophile"; 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:0000269|PubMed:19410548}. |
| 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. {ECO:0000269|PubMed:10194416, ECO:0000269|PubMed:10207058, ECO:0000269|PubMed:10436014, ECO:0000269|PubMed:11029042, ECO:0000269|PubMed:11294906, ECO:0000269|PubMed:11325936, ECO:0000269|PubMed:11416128, ECO:0000269|PubMed:14523026, ECO:0000269|PubMed:14990574, ECO:0000269|PubMed:15326198, ECO:0000269|PubMed:16641373, ECO:0000269|PubMed:17145966, ECO:0000269|PubMed:17376168, ECO:0000269|PubMed:17446860, ECO:0000269|PubMed:8247125, ECO:0000269|PubMed:8657109, ECO:0000269|PubMed:9119204, ECO:0000269|PubMed:9312043, ECO:0000269|PubMed:9447974}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (2); Modified residue (1); Mutagenesis (4); Sequence conflict (9) |
| Keywords | Cytoplasm;Endosome;Hydrolase;Membrane;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | P48582; Q08003 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Late endosome membrane; Peripheral membrane protein. Note=Recruited to the late endosome by BRO1. |
| Modified Residue | MOD_RES 443; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10570463; 11076031; 11193926; 11283351; 11805826; 11830665; 11995965; 12461556; 12871900; 14690591; 15119940; 15166140; 15188770; 15451116; 15571806; 15905137; 16157669; 16420678; 16429126; 16505373; 16552446; 16554755; 16864574; 16897085; 16922378; 18199684; 18489705; 18537571; 18634833; 18794364; 18806212; 18951365; 19143620; 19143630; 19150335; 19286982; 19410534; 19447341; 19489724; 19536198; 19596888; 19628586; 20028738; 20058707; 20074044; 21332354; 21447998; 21543789; 21665945; 21810245; 22072716; 22350874; 22533807; 22723847; 23208446; 23444383; 23514624; 23545414; 23697803; 23747013; 23974285; 24148098; 24158909; 24563465; 24821015; 25002535; 25072887; 25333764; 25396681; 25462441; 26262643; 26344761; 26427873; 26503604; 26503781; 26585826; 27693354; 32184262; 34342352; 6343083; 6343084; 7871889; 8824423; 9852113; |
| Motif | |
| Gene Encoded By | |
| Mass | 105,192 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |