ID I3KS31_ORENI Unreviewed; 997 AA.
AC I3KS31;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=usp4 {ECO:0000313|Ensembl:ENSONIP00000023927.1};
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:ENSONIP00000023927.1, 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:ENSONIP00000023927.1}
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 ECO:0000256|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC {ECO:0000256|ARBA:ARBA00037971}.
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DR RefSeq; XP_003441495.1; XM_003441447.4.
DR AlphaFoldDB; I3KS31; -.
DR STRING; 8128.ENSONIP00000044089; -.
DR MEROPS; C19.010; -.
DR Ensembl; ENSONIT00000023948.2; ENSONIP00000023927.1; ENSONIG00000019003.2.
DR GeneID; 100694486; -.
DR KEGG; onl:100694486; -.
DR CTD; 7375; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000154932; -.
DR HOGENOM; CLU_001060_7_1_1; -.
DR OrthoDB; 5474185at2759; -.
DR TreeFam; TF106276; -.
DR Proteomes; UP000005207; Linkage group LG5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
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}.
FT DOMAIN 28..139
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 316..969
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 112034 MW; 5510F5DCB08D4625 CRC64;
MMAEGGGPES GNAADSDSEP VAAQIPTPST ESQKQTIGSL LKTSLKKGDE WYLIDSRWFK
QWKKYVGFDS WDMYNVGERS LYPGPIDNSG LFSDQETQAL KEHLIDELDY VLVPTEAWNK
LVSWYGCLEG QRPIVRKVVE HGMFVKHCKV EVYLLELNLC ENDNMDNVVT RHFSKADTID
TIEKEMRTLF NIPSEEETRL WNKYMSNTYE QLNKPDSTVQ DAGLFQGQVL VIERKNEDGT
WPRQASHPKS STTPSRNFTT SPKLSSNSSP AVTNGDSNCS PGYTLNNSTS SSNRYGGYNS
YSSYNYRESQ SQPGLCGLSN LGNTCFMNSA LQCLSNASPL TEYFLTDQYE AEINRENPLG
MRGEIAEAYA DLVKQMWLSR SSYVAPRTFK TQVGRFAPQF SGYQQQDSQE LLAFLLDGLH
EDLNRVKKKP YLALRDAEGR PDEIVAKEAW TNHRLRNDSI IVDIFHGLFK STLVCPECSK
VSVTFDPFCY LTLPLPLKKD RTMEVFLVRS DPQSRPTQYR VVVPKLGTIT DLCSALSKLC
GIPPENMVVA DVYNHRFHKL YRRDDGLNQI MEKDDIFVYE VQEENSERMN LPVYFRERHS
KHAGSSTSTM LFGQPLLITV PRHNLIADVL YDKILERIGR YVKHSQSPST ESRASASATL
SSCSQAPECS TSSSLIASLG GCGSPLSDGA SCSASSSNGS NHSGTCNETN GLYDGEEEAM
DHQVSPEPEN GQSEEEEEAS DLQNGSKGDT TKLFTFSIVN SYGTANISPL PCDGNVLKLN
PHSTVAIDWD TESKKLYYDE PEAEAYEKHE SMLQPQRKKT TVALRECIEL FTTMETLGEH
DPWYCPTCKK HQQATKKFDL WSLPRILVVH LKRFSYNRCW RDKLDTVVDF PIRDLNMSEF
VCDPKAGPYI YDLIAVSNHY GGMGGGHYTA YGKNKVDGKW YYFDDSSVSS ATEDQIVTKA
AYVLFYQRRD EESPSKPQPS ASLGGAPEPA DDHMDTN
//
