ID I3IWW3_ORENI Unreviewed; 818 AA.
AC I3IWW3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=TNFAIP3 {ECO:0000313|Ensembl:ENSONIP00000001103.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001103.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000001103.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR RefSeq; XP_003438475.1; XM_003438427.4.
DR RefSeq; XP_005474387.1; XM_005474330.3.
DR RefSeq; XP_005474388.1; XM_005474331.3.
DR AlphaFoldDB; I3IWW3; -.
DR STRING; 8128.ENSONIP00000070047; -.
DR MEROPS; C64.003; -.
DR Ensembl; ENSONIT00000001102.2; ENSONIP00000001103.1; ENSONIG00000000871.2.
DR GeneID; 100692128; -.
DR KEGG; onl:100692128; -.
DR CTD; 7128; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158448; -.
DR OrthoDB; 2909231at2759; -.
DR TreeFam; TF323312; -.
DR Proteomes; UP000005207; Linkage group LG13.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd22766; OTU_TNFAIP3; 1.
DR Gene3D; 1.20.5.4770; -; 1.
DR Gene3D; 4.10.240.30; -; 4.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF3; TUMOR NECROSIS FACTOR ALPHA-INDUCED PROTEIN 3; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 5.
DR SMART; SM00259; ZnF_A20; 6.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 4.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 96..265
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 485..520
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 628..663
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 681..716
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 783..818
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 432..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 91082 MW; A643E853F92AD0DE CRC64;
MSQGQNFLPK FLFVSNLLKA VKIRQRVPND VVKPAASGGL MHHLRGMHRY TLEMIAMNHF
PQAFREVVQA AILDRAMQAS LEKEKKLNWC GELKKMVPLR TNGDGNCLLH AASQYMLGVQ
DTDLVLRKAL HGVLKETDTG VFKARFQAEL LQSQEFTQTG LRYTTMNWED EWEKIVKMAS
PVSSSNGLQF DSLEDIHIFI LSNILRRPII VIADQVVRSM KSGTSISPLN VGGIYLPLHW
QPTECYKYPI VLGYDSQHFA PLITIKDSGP EIRAVPLINP RRNGFEELKV HFLMEKEQQQ
KERLLKEYLH LIEIPIRLGH DITQIMKAAR LDEGNLPEDM NLMEDYLQLV NHEYQRWQED
KEQAWAAQPQ RPPPFSVSQL SLIEIRCATP RCTFYVSVDT QPHCHECFEK RQATTGGGAR
IEGVIQTKEG GLQGGVGVIG GSETEVSSRG ARSSSPPCSS SGRGVVLSSP RSAPPTAPSL
SLYSETHAMK CKTPGCLFTL SVEHDGLCER CFNSRQNHGP PGVGTAATGL PGTNGGPVVP
HPAQGSGWNQ WGGCETETER CNMCRKEAFR IFNGLCPPCM QRQQAPDRGE PQQINPRTEA
SSSAWTQARD TERPCLTLTP GHTSAWQGPV ARPCKRSGCQ FFGTPEKLGF CTICYVDYQT
NHHLTPPPAP AQSRHGLETG FQNASRCRGP GCGAVGKVML EGYCDKCYVK EQSARLNQVA
NRTSPPLRER AAKPRSSQQS QTQTQCRRSG CSNVSPGCTD LCPECHTRGQ GREPGRRAQA
PKEKSKQRCR TQGCDHYANQ EKQGYCNECD HFKQIYRG
//
