| IED ID | IndEnz0002018529 |
| Enzyme Type ID | protease018529 |
| Protein Name |
Ataxin-3 homolog EC 3.4.19.12 Machado-Joseph disease-like protein |
| Gene Name | atx-3 F28F8.6 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MSKDDPINSIFFEHQEAALCAQHALNMLLQDALYKWQDLRDLAIQMDKMEQQILGNANPTPGRSENMNESGYFSIQVLEKALETFSLKLTNIENPAMVDYKNNPLTARAYICNLREHWFVLRKFGNQWFELNSVNRGPKLLSDTYVSMFLHQVSSEGYSIFVVQGVLPRSDADDLISLCPVVPPKVTPKKEQKLEKVMTKFFNTVGKRLGGGSGAPPDSQEEKDLAIAFAMSMETKDGSEVSRSSAEIDEENLRKAIELSQAPGPSEPAEIPLLTRSRSSTPPGASEPFSNAEQQRRDRQKFLERFEKKKEERNDEK |
| Enzyme Length | 317 |
| Uniprot Accession Number | O17850 |
| Absorption | |
| Active Site | ACT_SITE 20; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU00331; ACT_SITE 117; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00331; ACT_SITE 132; /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:17234717, ECO:0000269|PubMed:21317884}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway (PubMed:19545544, PubMed:17234717, PubMed:21317884). Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan (PubMed:21317884). Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin-protein ligase ufd-2 to DNA repair foci (PubMed:27669035). Interacts with key regulators of transcription and represses transcription (By similarity). Acts as a histone-binding protein that regulates transcription (By similarity). {ECO:0000250|UniProtKB:P54252, ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:19545544, ECO:0000269|PubMed:21317884, ECO:0000269|PubMed:27669035}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Domain (3); Mutagenesis (4); Region (2) |
| Keywords | Cytoplasm;Hydrolase;Nucleus;Protease;Reference proteome;Repeat;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway |
| Interact With | P54812 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21526185}. Nucleus {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21526185}. Nucleus, nucleolus {ECO:0000269|PubMed:27669035}. Note=Localizes predominantly in the cytoplasm (PubMed:17234717). In the germline, following ionizing radiation-induced DNA damage, localizes to foci within nucleoli where it colocalizes with cdc-48.1 and/or cdc-48.2 and ufd-2, proteasome alpha subunit and ubiquitinated proteins (PubMed:27669035). {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:27669035}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 12097347; 12445391; 14704431; 15338614; 16194547; 16805848; 17486083; 17850180; 19123269; 21177967; 21367940; 22267497; 22286215; 22560298; 23800452; 24884423; 25487147; 25721663; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 35,864 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |