| IED ID | IndEnz0002018534 |
| Enzyme Type ID | protease018534 |
| Protein Name |
Ataxin-3 EC 3.4.19.12 Machado-Joseph disease protein 1 homolog |
| Gene Name | Atxn3 Mjd Sca3 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERLRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIKVQQMHRPKLIGEELAHLKEQSALKADLERVLEAADGPGMFDDDEDDLQRALAMSRQEIDMEDEEADLRRAIQLSMQGSSRGMCEDSPQTSSTDLSSEELRKRREAYFEKQQHQQQEADRPGYLSYPCERPTTSSGGLRSNQAGNAMSEEDVLRATVTVSLETAKDSLKAERKK |
| Enzyme Length | 355 |
| Uniprot Accession Number | O35815 |
| Absorption | |
| Active Site | ACT_SITE 14; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P54252; ACT_SITE 119; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00331; ACT_SITE 134; /evidence=ECO:0000255|PROSITE-ProRule:PRU00331 |
| Activity Regulation | |
| 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:17696782}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (PubMed:17696782). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (By similarity). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (By similarity). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (By similarity). {ECO:0000250|UniProtKB:P54252, ECO:0000250|UniProtKB:Q9CVD2, ECO:0000269|PubMed:17696782}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (3); Cross-link (2); Domain (4); Modified residue (4); Mutagenesis (3); Region (1) |
| Keywords | Hydrolase;Isopeptide bond;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Transcription;Transcription regulation;Ubl conjugation;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54252}. |
| Modified Residue | MOD_RES 268; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9CVD2; MOD_RES 272; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9CVD2; MOD_RES 273; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9CVD2; MOD_RES 321; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9CVD2 |
| Post Translational Modification | PTM: Monoubiquitinated by UBE2W, possibly leading to activate the deubiquitinating enzyme activity (By similarity). {ECO:0000250|UniProtKB:P54252}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17079677; |
| Motif | |
| Gene Encoded By | |
| Mass | 40,446 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |