ID   ATX3H_ARATH             Reviewed;         280 AA.
AC   Q9M391; Q53XG9;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Ataxin-3 homolog;
DE            EC=3.4.19.12;
DE   AltName: Full=MJD1a-like;
DE   AltName: Full=Machado-Joseph disease-like protein;
GN   OrderedLocusNames=At3g54130; ORFNames=F24B22.90;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: Interacts with key regulators of transcription and represses
CC       transcription. Acts as a histone-binding protein that regulates
CC       transcription. Acts as a deubiquitinating enzyme (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- INTERACTION:
CC       Q9M391; A0A178W4W9: AXX17_At1g19640; NbExp=3; IntAct=EBI-25520805, EBI-25520823;
CC       Q9M391; Q42569: CYP90A1; NbExp=3; IntAct=EBI-25520805, EBI-17071660;
CC       Q9M391; Q39085: DIM; NbExp=3; IntAct=EBI-25520805, EBI-16906963;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; AL132957; CAB70987.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79191.1; -; Genomic_DNA.
DR   EMBL; BT010762; AAR23732.1; -; mRNA.
DR   EMBL; BT010992; AAR24770.1; -; mRNA.
DR   PIR; T47572; T47572.
DR   RefSeq; NP_190981.1; NM_115273.4.
DR   AlphaFoldDB; Q9M391; -.
DR   SMR; Q9M391; -.
DR   BioGRID; 9897; 5.
DR   IntAct; Q9M391; 3.
DR   STRING; 3702.Q9M391; -.
DR   MEROPS; C86.A01; -.
DR   iPTMnet; Q9M391; -.
DR   PaxDb; 3702-AT3G54130-1; -.
DR   ProteomicsDB; 241098; -.
DR   EnsemblPlants; AT3G54130.1; AT3G54130.1; AT3G54130.
DR   GeneID; 824580; -.
DR   Gramene; AT3G54130.1; AT3G54130.1; AT3G54130.
DR   KEGG; ath:AT3G54130; -.
DR   Araport; AT3G54130; -.
DR   TAIR; AT3G54130; -.
DR   eggNOG; KOG2935; Eukaryota.
DR   HOGENOM; CLU_031228_0_0_1; -.
DR   InParanoid; Q9M391; -.
DR   OMA; EMTEMDM; -.
DR   OrthoDB; 337428at2759; -.
DR   PhylomeDB; Q9M391; -.
DR   PRO; PR:Q9M391; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M391; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.40; -; 1.
DR   Gene3D; 6.10.140.100; -; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   InterPro; IPR033865; Ataxin-3.
DR   InterPro; IPR006155; Josephin.
DR   PANTHER; PTHR14159; ATAXIN-3-RELATED; 1.
DR   PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1.
DR   Pfam; PF02099; Josephin; 1.
DR   PRINTS; PR01233; JOSEPHIN.
DR   SMART; SM01246; Josephin; 1.
DR   PROSITE; PS50957; JOSEPHIN; 1.
DR   Genevisible; Q9M391; AT.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
KW   Transcription; Transcription regulation; Ubl conjugation pathway.
FT   CHAIN           1..280
FT                   /note="Ataxin-3 homolog"
FT                   /id="PRO_0000053836"
FT   DOMAIN          7..187
FT                   /note="Josephin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   DOMAIN          243..262
FT                   /note="UIM"
FT                   /evidence="ECO:0000305"
FT   REGION          183..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        20
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
SQ   SEQUENCE   280 AA;  30692 MW;  F4A1C9A3F9A25A78 CRC64;
     MERTSNGGML YHEVQESNLC AVHCVNTVLQ GPFFSEFDLA AVAADLDGKE RQVMLEGAAV
     GGFAPGDFLA EESHNVSLGG DFSIQVLQKA LEVWDLQVIP LNCPDAEPAQ IDPELESAFI
     CHLHDHWFCI RKVNGEWYNF DSLLAAPQHL SKFYLSAFLD SLKGAGWSIF IVKGNFPQEC
     PMSSSSEASN SFGQWLSPED AERIRKNTSS GSSARNKRSN DNVNQQRRNQ ALSREEVQAF
     SEMEDDDLKA AIAASLLDAS AAEANLGAVG TSEKETEKQK
//