ID A0A2K5HPE3_COLAP Unreviewed; 295 AA.
AC A0A2K5HPE3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000006218.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000006218.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A2K5HPE3; -.
DR Ensembl; ENSCANT00000023510.1; ENSCANP00000006218.1; ENSCANG00000020292.1.
DR Proteomes; UP000233080; Unplaced.
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; 1.10.287.10; S15/NS1, RNA-binding; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00331}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..175
FT /note="Josephin"
FT /evidence="ECO:0000259|PROSITE:PS50957"
FT REGION 252..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 9
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1,
FT ECO:0000256|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 295 AA; 34049 MW; CEA9AB2358FD872F CRC64;
PRRQEGSLCA QHCLNNLLQG EYFSPVELSS IAHQLDEEER MRMAEGGVTS EDYRTFLQQP
SGNMDDSGFF SIQVISNALK VWGLELILFN SPEYQRLRID PINERSFICN YKEHWFTVRK
LGKQWFNLNS LLTGPELISD TYLALFLAQL QQEGYSIFVV KGDLPDCEAD QLLQMIRVQQ
MHRPKLIGEE LAQLKEQRVH KTDLERVLEA NDGSGMLDED EDLQRALALS RQEIDMEDEE
ADLRRAIQLS MQGSSRNISQ DIPQTSGTNL TSEELRKRRE AYFENHNSEV DEGKF
//
