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
//