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Database: UniProt
Entry: I3KUD4_ORENI
LinkDB: I3KUD4_ORENI
Original site: I3KUD4_ORENI 
ID   I3KUD4_ORENI            Unreviewed;       518 AA.
AC   I3KUD4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:ENSONIP00000024730.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Ensembl:ENSONIP00000024730.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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         ECO:0000256|RuleBase:RU366025};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038490}.
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DR   AlphaFoldDB; I3KUD4; -.
DR   STRING; 8128.ENSONIP00000067561; -.
DR   Ensembl; ENSONIT00000024751.2; ENSONIP00000024730.2; ENSONIG00000019644.2.
DR   eggNOG; KOG1867; Eukaryota.
DR   GeneTree; ENSGT00940000156623; -.
DR   HOGENOM; CLU_008279_11_0_1; -.
DR   TreeFam; TF323554; -.
DR   Proteomes; UP000005207; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02660; Peptidase_C19D; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          16..133
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          171..513
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   518 AA;  59547 MW;  4423F8D610E8BB6F CRC64;
     QLARTQHSVD NEPCPAGCPH VNGFKVDNWK QNLRVIYQCF VWSGSAETRK RKAKSCICHM
     CGAHLNRLHS CLYCVFFACF AKKHIHEHAK SKRHNLAIDL LYGGIYCFMC QDYIYDKEME
     QIAKEEQRKA WKMQGIGEKY STWEPTKREL ELLRHNPKRR RITSNCTIGL RGLINLGNTC
     FMNCIVQALT HTPLLRDFFL SDRHKCEMQS NSCLVCEMSQ LFQEFYSGHR SPHIPFRLLH
     LVWTHARHLA GYEQQDAHEF LIAALDVLHR HCKDDNGKKA NNPNHCNCII DQIFTGGLQS
     DVTCQACHGV STTIDPFWDI SLDLPGSSTP FWPLSPGGDG SALNGESHTT GATTLTDCLR
     RFTRPEHLGS SAKIKCSGCH SYQESTKQLT MKKLPIVACF HLKRFEHSAK LRRKITTYVS
     FPLELDMTPF MASSKESRMN GQYQQTVDPF NNDNKYSLFA VVNHQGTLES GHYTTFIRQH
     KDQWFKCDDA IITKASIKDV LDSEGYLLFY HKQFLEYE
//
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