ID D3VVN9_HUMAN Unreviewed; 271 AA.
AC D3VVN9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 08-NOV-2023, entry version 53.
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:ADD00767.1};
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:ADD00767.1};
RN [1] {ECO:0000313|EMBL:ADD00767.1}
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; GQ176754; ADD00767.1; -; mRNA.
DR AlphaFoldDB; D3VVN9; -.
DR MEROPS; C86.001; -.
DR PeptideAtlas; D3VVN9; -.
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 Pfam; PF16619; SUIM_assoc; 1.
DR Pfam; PF02809; UIM; 2.
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..125
FT /note="Josephin"
FT /evidence="ECO:0000259|PROSITE:PS50957"
FT REGION 203..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 271
FT /evidence="ECO:0000313|EMBL:ADD00767.1"
SQ SEQUENCE 271 AA; 31128 MW; E605FFAC1F1914C1 CRC64;
MESIFHEKQP SGNMDDSGFF SIQVISNALK VWGLELILFN SPEYQRLRID PINERSFICN
YKEHWFTVRK LGKQWFNLNS LLTGPELISD TYLALFLAQL QQEGYSIFVV KGDLPDCEAD
QLLQMIRVQQ MHRPKLIGEE LAQLKEQRVH KTDLERVLEA NDGSGMLDED EEDLQRALAL
SRQEIDMEDE EADLRRAIQL SMQGSSRNIS QDMTQTSGTN LTSEELRKRR EAYFEKQQQK
QQQQQQQGDL SGQSSHPCER PATSSGALGS D
//
