Detail Information for IndEnz0002018528
IED ID IndEnz0002018528
Enzyme Type ID protease018528
Protein Name Ataxin-3 homolog
EC 3.4.19.12
Machado-Joseph disease-like protein
Gene Name atx-3 CBG18600
Organism Caenorhabditis briggsae
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis briggsae
Enzyme Sequence MSPSDDPISSIFFERQQAALCAQHALNMLLQDSLFTYENLRDLARQMDQMEHDILGNNANAVGRSENMNDSGFFSIQVIEKALETFDLKLINMENPAMAEFKANPLTARAYVLNLREHWFVLRKFGNQWFELNSVKNGPKLLTDTYVKEYLHQFAAENYSIFVVQGILPNSEADDFITLCPVVPKPTDFDKKEPNLVQKFFNSVGRRLGGSQEIPDSQEDRDLAIAMALSMESKESSESSGSDEDQLAKAIEMSLSQDPNIPSTSAAPSELTETPILGPSTSSETPSGRIPSAEQQRRDRAKFLEKLEEEKKSQNVPEE
Enzyme Length 319
Uniprot Accession Number Q60XN1
Absorption
Active Site ACT_SITE 21; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"; ACT_SITE 118; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"; ACT_SITE 133; /evidence="ECO:0000250|UniProtKB:P54252, 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:0000250|UniProtKB:O17850};
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. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. 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. Interacts with key regulators of transcription and represses transcription. Acts as a histone-binding protein that regulates transcription. {ECO:0000250|UniProtKB:O17850, ECO:0000250|UniProtKB:P54252}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (2); Domain (3); Region (2)
Keywords Cytoplasm;Hydrolase;Nucleus;Protease;Reference proteome;Repeat;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O17850}. Nucleus {ECO:0000250|UniProtKB:O17850}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O17850}. Note=Localizes predominantly in the cytoplasm. 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. {ECO:0000250|UniProtKB:O17850}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 35,834
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda