ATX3_CAEBR
ID ATX3_CAEBR Reviewed; 319 AA.
AC Q60XN1; A8XTP1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ataxin-3 homolog;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:O17850};
DE AltName: Full=Machado-Joseph disease-like protein;
GN Name=atx-3 {ECO:0000250|UniProtKB:O17850}; ORFNames=CBG18600;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Acts as chain editing deubiquitinating enzyme that binds and
CC cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for
CC chains containing four or more ubiquitin molecules thereby modulating
CC protein degradation by the ubiquitin-proteasome pathway. Probably by
CC regulating the IGF-1-insulin-like pathway, regulates lifespan.
CC Regulates germline DNA double-strand-break repair and apoptosis in
CC response to DNA damage by recruiting E4 ubiquitin-protein ligase ufd-2
CC to DNA repair foci. Interacts with key regulators of transcription and
CC represses transcription. Acts as a histone-binding protein that
CC regulates transcription. {ECO:0000250|UniProtKB:O17850,
CC ECO:0000250|UniProtKB:P54252}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:O17850};
CC -!- SUBUNIT: Forms a complex composed of deubiquitinating enzyme atx-3,
CC adapter ubxn-5 and cdc-48.1. Forms a complex composed of
CC deubiquitinating enzyme atx-3, E4 ubiquitin-protein ligase ufd-2 and
CC cdc-48.1. Interacts (via RRDR motif) with cdc-48.1 (via N-terminus) and
CC cdc-48.2 (via N-terminus); the interaction with cdc-48.1 is not
CC required for atx-3 enzymatic activity. Interacts (via C-terminus) with
CC ubxn-5. May interact with ned-8. {ECO:0000250|UniProtKB:O17850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O17850}. Nucleus
CC {ECO:0000250|UniProtKB:O17850}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O17850}. Note=Localizes predominantly in the
CC cytoplasm. In the germline, following ionizing radiation-induced DNA
CC damage, localizes to foci within nucleoli where it colocalizes with
CC cdc-48.1 and/or cdc-48.2 and ufd-2, proteasome alpha subunit and
CC ubiquitinated proteins. {ECO:0000250|UniProtKB:O17850}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE601466; CAP36017.3; -; Genomic_DNA.
DR RefSeq; XP_002638391.1; XM_002638345.1.
DR AlphaFoldDB; Q60XN1; -.
DR SMR; Q60XN1; -.
DR STRING; 6238.CBG18600; -.
DR MEROPS; C86.003; -.
DR EnsemblMetazoa; CBG18600.1; CBG18600.1; WBGene00037987.
DR GeneID; 8580388; -.
DR KEGG; cbr:CBG_18600; -.
DR CTD; 8580388; -.
DR WormBase; CBG18600; CBP10927; WBGene00037987; Cbr-atx-3.
DR eggNOG; KOG2935; Eukaryota.
DR HOGENOM; CLU_031228_1_1_1; -.
DR InParanoid; Q60XN1; -.
DR OMA; QQIQRPK; -.
DR OrthoDB; 1482722at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR InterPro; IPR033865; Ataxin-3.
DR InterPro; IPR006155; Josephin.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR14159; PTHR14159; 1.
DR Pfam; PF02099; Josephin; 1.
DR Pfam; PF02809; UIM; 2.
DR SMART; SM01246; Josephin; 1.
DR SMART; SM00726; UIM; 2.
DR PROSITE; PS50957; JOSEPHIN; 1.
DR PROSITE; PS50330; UIM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW Thiol protease; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT CHAIN 1..319
FT /note="Ataxin-3 homolog"
FT /id="PRO_0000232395"
FT DOMAIN 8..179
FT /note="Josephin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT DOMAIN 218..237
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 242..261
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 253..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..300
FT /note="Interaction with cdc-48.1 and cdc-48.2"
FT /evidence="ECO:0000250|UniProtKB:O17850"
FT COMPBIAS 256..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 21
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT ACT_SITE 133
FT /evidence="ECO:0000250|UniProtKB:P54252,
FT ECO:0000255|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 319 AA; 35834 MW; AD08AAAF3065CA0C CRC64;
MSPSDDPISS IFFERQQAAL CAQHALNMLL QDSLFTYENL RDLARQMDQM EHDILGNNAN
AVGRSENMND SGFFSIQVIE KALETFDLKL INMENPAMAE FKANPLTARA YVLNLREHWF
VLRKFGNQWF ELNSVKNGPK LLTDTYVKEY LHQFAAENYS IFVVQGILPN SEADDFITLC
PVVPKPTDFD KKEPNLVQKF FNSVGRRLGG SQEIPDSQED RDLAIAMALS MESKESSESS
GSDEDQLAKA IEMSLSQDPN IPSTSAAPSE LTETPILGPS TSSETPSGRI PSAEQQRRDR
AKFLEKLEEE KKSQNVPEE
