| IED ID | IndEnz0002011130 |
| Enzyme Type ID | protease011130 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 4 EC 3.4.19.12 Deubiquitinating enzyme 4 Ubiquitin thioesterase 4 Ubiquitin-specific-processing protease 4 |
| Gene Name | DOA4 UBP4 CAGL0I06765g |
| Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Nakaseomyces Nakaseomyces/Candida clade Candida glabrata (Yeast) (Torulopsis glabrata) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Enzyme Sequence | MPGIEQPVSRKNETLVKLSSLADEFVFNDEVQLNLQDVLQECVDTYQNYQDEVKKIKNMDHTESEKVSELCKSAYIYYKIVHNFITKVIPHLPEFEVATGPKASKLQAELIKIYYSLFSRLESDKKISYIKNIIIKHMDTQENNHSVESHEQVKLSNKKLPVNRDAIEIDKDSILQDIRYINGKRSGSGISCSELLSLMKMKEDSLLLIDVRPKLEYDAHHIKTKNIICIEPISFKESYSDQQIEKTSMIPSPKHEIQLFQRRSEFQYIILYTDLEEKSNFYFQQLKSLLEILLQRSFLRPIDDRKTKVLFLSDSLQNWIKNGGEIDKSQEVSKIRNRSISGSGPLLNSLSERKTIGAFPDINRNSTKQMPISPLPSLPGSERTVATPPNGSSTLGRINSPVTHYPKAPLINDSEFHLNINNNHSPPTHLPSKDNNPLASSMPIGSDHKPFMSPQNSLPLAPKPPTLESKNYNFISDRSNIIDQKQNRSRSLEPQLPPIPSTLIRKNSPEKTLSCNQMMDTSFTVGLENMGNSCYINCIIQCIFATTELIKIFLNGTYAKHINKQSKLGSKGVLSHNFAKLLKDMYEENSSKKIGKKHGAVKTLQFKMACASVNSLFKDASQQDCLEFCQFLLDGLHEDLNQCGANPPLKELSPEAEKMRENLSLRVASSIEWERYLTTDFSIIVDLFQGQYASQLRCKVCNRTSTTYQAFSVLSVPVPSGKSCGLLDCFIEFTKTENLEVDEQWFCPSCKKKQPSTKKLTITRLPRNLIIHLKRFDNMMNKNNIFVRYPQILDLTPFWANDSDGKLPPGITDEIPARGQVPPFNYRLYGAACHFGTLYGGHYTSYVDKGPEKGWIYFDDTVYRPVRFQNEFISPSAYVLFYHRITS |
| Enzyme Length | 887 |
| Uniprot Accession Number | Q6FQF0 |
| Absorption | |
| Active Site | ACT_SITE 534; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10092; ACT_SITE 842; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10092 |
| 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. 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); Compositional bias (3); Domain (2); Region (2) |
| Keywords | Cytoplasm;Endosome;Hydrolase;Membrane;Protease;Reference proteome;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}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 101,165 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |