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Database: UniProt
Entry: I3JCM6_ORENI
LinkDB: I3JCM6_ORENI
Original site: I3JCM6_ORENI 
ID   I3JCM6_ORENI            Unreviewed;       521 AA.
AC   I3JCM6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 69.
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:ENSONIP00000006616.2, 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:ENSONIP00000006616.2}
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; I3JCM6; -.
DR   STRING; 8128.ENSONIP00000040682; -.
DR   Ensembl; ENSONIT00000006621.2; ENSONIP00000006616.2; ENSONIG00000005266.2.
DR   eggNOG; KOG1867; Eukaryota.
DR   GeneTree; ENSGT00940000156623; -.
DR   HOGENOM; CLU_008279_11_1_1; -.
DR   TreeFam; TF323554; -.
DR   Proteomes; UP000005207; Linkage group LG4.
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          4..132
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          170..516
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   521 AA;  59745 MW;  7E12C068828AC8BF CRC64;
     MSPAGCSHVN GYKVDNWKQN LRVIYQCFVW SGTAETRRRK VLHSDAGWAE LAKSCICHMC
     GAHLNRLHSC LYCVFFGCFT KKHIHEHAKN KRHNLAIDLL YGGIYCFVCQ DYIYDKDMEQ
     IAKEEQRKAW KLQGIGEKYT TWEPTKRELE LLRHNPKRRK ITTNCTIGLR GLINLGNTCF
     MNCIVQALTH TPLLRDFFLS DRHKCEMQSN SCLVCEMSQL FQEFYSGHRS PHIPFRLLHL
     VWTHARHLAG YEQQDAHEFL IAALDVLHRH CKGDTINDNG KKANNPNHCN CIIDQIFTGG
     LQSDVTCQVC HGVSTTIDPF WDISLDLPGS STPFWPLSPG GDGSTVNGES HLSGSTTLTD
     CLRRFTRPEH LGSSAKIKCG GCHSYQESTK QLTMKKLPIV ACFHLKRFEH SAKLRRKITT
     YVSFPLELDM TPFMASSKES RMNGQYQQSV DVLNNDNKYS LFAVVNHQGT LESGHYTSFI
     RQHKDQWFKC DDAIITKASI KDVLDSEGYL LFYHKQFLEY E
//
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