ATX3_CHICK
ID ATX3_CHICK Reviewed; 363 AA.
AC Q9W689;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ataxin-3;
DE EC=3.4.19.12;
DE AltName: Full=Machado-Joseph disease protein 1 homolog;
GN Name=ATXN3; Synonyms=MDJ1, MJD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=SPAFAS;
RX PubMed=10023088; DOI=10.1016/s0167-4781(99)00004-4;
RA Linhartova I., Repitz M., Draber P., Nemec M., Wiche G., Propst F.;
RT "Conserved domains and lack of evidence for polyglutamine length
RT polymorphism in the chicken homolog of the Machado-Joseph disease gene
RT product ataxin-3.";
RL Biochim. Biophys. Acta 1444:299-305(1999).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=12486728; DOI=10.1002/prot.10280;
RA Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.;
RT "Structural modeling of ataxin-3 reveals distant homology to adaptins.";
RL Proteins 50:355-370(2003).
CC -!- FUNCTION: Deubiquitinating enzyme involved in protein homeostasis
CC maintenance, transcription, cytoskeleton regulation, myogenesis and
CC degradation of misfolded chaperone substrates (By similarity). Binds
CC long polyubiquitin chains and trims them, while it has weak or no
CC activity against chains of 4 or less ubiquitins (By similarity).
CC Involved in degradation of misfolded chaperone substrates via its
CC interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP,
CC and restricts the length of ubiquitin chain attached to STUB1/CHIP
CC substrates and preventing further chain extension (By similarity).
CC Interacts with key regulators of transcription and represses
CC transcription: acts as a histone-binding protein that regulates
CC transcription (By similarity). Regulates autophagy via the
CC deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of
CC BECN1 (By similarity). {ECO:0000250|UniProtKB:P54252,
CC ECO:0000250|UniProtKB:Q9CVD2}.
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:P54252};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54252}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10023088).
CC {ECO:0000269|PubMed:10023088}.
CC -!- DOMAIN: The UIM domains bind ubiquitin and interact with various E3
CC ubiquitin-protein ligase, such as STUB1/CHIP (By similarity). They are
CC essential to limit the length of ubiquitin chains (By similarity).
CC {ECO:0000250|UniProtKB:Q9CVD2}.
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DR EMBL; AF085247; AAD21923.1; -; mRNA.
DR RefSeq; NP_989688.1; NM_204357.1.
DR AlphaFoldDB; Q9W689; -.
DR SMR; Q9W689; -.
DR STRING; 9031.ENSGALP00000017488; -.
DR MEROPS; C86.001; -.
DR PaxDb; Q9W689; -.
DR PRIDE; Q9W689; -.
DR Ensembl; ENSGALT00000017509; ENSGALP00000017488; ENSGALG00000010766.
DR GeneID; 378424; -.
DR KEGG; gga:378424; -.
DR CTD; 4287; -.
DR VEuPathDB; HostDB:geneid_378424; -.
DR eggNOG; KOG2935; Eukaryota.
DR GeneTree; ENSGT00390000001830; -.
DR HOGENOM; CLU_031228_1_0_1; -.
DR InParanoid; Q9W689; -.
DR OrthoDB; 1482722at2759; -.
DR PhylomeDB; Q9W689; -.
DR TreeFam; TF314228; -.
DR Reactome; R-GGA-5689877; Josephin domain DUBs.
DR PRO; PR:Q9W689; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000010766; Expressed in testis and 13 other tissues.
DR ExpressionAtlas; Q9W689; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
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; 3.
DR SMART; SM01246; Josephin; 1.
DR SMART; SM00726; UIM; 3.
DR PROSITE; PS50957; JOSEPHIN; 1.
DR PROSITE; PS50330; UIM; 3.
PE 2: Evidence at transcript level;
KW Hydrolase; Nucleus; Protease; Reference proteome; Repeat; Thiol protease;
KW Transcription; Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..363
FT /note="Ataxin-3"
FT /id="PRO_0000053834"
FT DOMAIN 1..180
FT /note="Josephin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT DOMAIN 227..246
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 247..266
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 337..356
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 192..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT ACT_SITE 134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 363 AA; 41608 MW; 15C81537096DE8C4 CRC64;
MESIFHERQE GSLCAQHCLN NLLQGEYFSP VELSSIAQQL DEEERMRMAE GGVSSEEYRT
FLQQPSVNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ RLGIDPINEK SFICNYKEHW
FTVRKLGKQW FNLNSLLMGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM
IRVQQVQRPK LIGEETAQSR DQRLPRSDVD QAIEVSHPFD GTGMLDEDEE NFQRALALSR
QEIDMEDEEA DLRRAIQLSM QGSRQSEFSN SLPQNASQPP HTSQTDSLSS EDLRRRRQAY
FEKQQQQLQQ QDLTLNLHDK PTINSSTLEA DPGGDMSEED MLQAAMNMSL ESARNHLSTE
EKK
