ID   D3VVR5_HUMAN            Unreviewed;       278 AA.
AC   D3VVR5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
GN   Name=ATXN3 {ECO:0000313|EMBL:ADD00793.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ADD00793.1};
RN   [1] {ECO:0000313|EMBL:ADD00793.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19714377; DOI=10.1007/s10048-009-0216-y;
RA   Bettencourt C., Santos C., Montiel R., Costa M.D., Cruz-Morales P.,
RA   Santos L.R., Simoes N., Kay T., Vasconcelos J., Maciel P., Lima M.;
RT   "Increased transcript diversity: novel splicing variants of Machado-Joseph
RT   Disease gene (ATXN3).";
RL   Neurogenetics 0:0-0(2009).
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:0000256|ARBA:ARBA00000707};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00331}.
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DR   EMBL; GQ176799; ADD00793.1; -; mRNA.
DR   AlphaFoldDB; D3VVR5; -.
DR   MEROPS; C86.001; -.
DR   PeptideAtlas; D3VVR5; -.
DR   ChiTaRS; ATXN3; human.
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   InterPro; IPR033865; Ataxin-3.
DR   InterPro; IPR006155; Josephin.
DR   InterPro; IPR003903; UIM_dom.
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   SMART; SM00726; UIM; 2.
DR   PROSITE; PS50957; JOSEPHIN; 1.
DR   PROSITE; PS50330; UIM; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..74
FT                   /note="Josephin"
FT                   /evidence="ECO:0000259|PROSITE:PS50957"
FT   REGION          152..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         278
FT                   /evidence="ECO:0000313|EMBL:ADD00793.1"
SQ   SEQUENCE   278 AA;  32520 MW;  5814F10B49EED964 CRC64;
     MESIFHEKQP SGNMDDSGLF SIQWFNLNSL LTGPELISDT YLALFLAQLQ QEGYSIFVVK
     GDLPDCEADQ LLQMIRVQQM HRPKLIGEEL AQLKEQRVHK TDLERMLEAN DGSGMLDEDE
     EDLQRALALS RQEIDMEDEE ADLRRAIQLS MQGSSRNISQ DMTQTSGTNL TSEELRKRRE
     AYFEKQQQKQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQQQRDLSGQ SPHPCERPAT SSGALGSD
//