ATX3H_ARATH
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 03-AUG-2022, entry version 127.
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: At1g18710; 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.AT3G54130.1; -.
DR MEROPS; C86.A01; -.
DR iPTMnet; Q9M391; -.
DR PaxDb; Q9M391; -.
DR PRIDE; Q9M391; -.
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; locus:2080330; AT3G54130.
DR eggNOG; KOG2935; Eukaryota.
DR HOGENOM; CLU_031228_0_0_1; -.
DR InParanoid; Q9M391; -.
DR OMA; ICNFDSH; -.
DR OrthoDB; 1482722at2759; -.
DR PhylomeDB; Q9M391; -.
DR PRO; PR:Q9M391; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M391; baseline and differential.
DR Genevisible; Q9M391; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR InterPro; IPR033865; Ataxin-3.
DR InterPro; IPR006155; Josephin.
DR PANTHER; PTHR14159; PTHR14159; 1.
DR Pfam; PF02099; Josephin; 1.
DR SMART; SM01246; Josephin; 1.
DR PROSITE; PS50957; JOSEPHIN; 1.
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
