ID A0A3Q2C6A3_CYPVA Unreviewed; 1044 AA.
AC A0A3Q2C6A3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 4 {ECO:0000256|ARBA:ARBA00040967};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 4 {ECO:0000256|ARBA:ARBA00042237};
DE AltName: Full=Ubiquitin thioesterase 4 {ECO:0000256|ARBA:ARBA00041731};
DE AltName: Full=Ubiquitin-specific-processing protease 4 {ECO:0000256|ARBA:ARBA00042735};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000000144.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000000144.1}
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 -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC {ECO:0000256|ARBA:ARBA00037971}.
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DR RefSeq; XP_015243830.1; XM_015388344.1.
DR AlphaFoldDB; A0A3Q2C6A3; -.
DR STRING; 28743.ENSCVAP00000000144; -.
DR Ensembl; ENSCVAT00000015566.1; ENSCVAP00000000144.1; ENSCVAG00000001021.1.
DR GeneID; 107093343; -.
DR KEGG; cvg:107093343; -.
DR CTD; 7375; -.
DR GeneTree; ENSGT00940000154932; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0060026; P:convergent extension; IEA:Ensembl.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT DOMAIN 70..181
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 363..1016
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 44..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 117358 MW; 1119AA25854FF303 CRC64;
MRESACRVSS SFSTSLRLRL LGGSCLMLVH QPARSRHRST RCMMAEGGGP ESGSAADSDS
EPVAAQMPTP SIENQKQTIG SLLKTTLKKG DDWYLIDSRW FKQWKKYVGF DSWDMYNVGE
RSLYPGPIDN SGLFSDQETQ ALKEHLIDEL DYVLVPTEAW NKLVSWYRCL EGQRPIVRKV
VEHGMFVKHC KVEVYLLELN LCENDNMENV ITRHFSKADT IDTIEKEMRT LFNIPSEKET
RLWNKYMSNT YEQLNKPDST VQDAGLFQGQ VLVIERKNED GTWPRQALQP KSSATPSRNC
STSPKLSSNS SVGASPTVTN GDSSSSPGYA LNNSTSSNNR YGGYNSYSSS YNYRESQSQP
GLCGLSNLGN TCFMNSALQC LSNVSLLTEY FLTDQYEAEI NRENPLGMRG EIAEAYADLV
KQMWMSRNSY VAPRTFKTQV GRFAPQFSGY QQQDSQELLA FLLDGLHEDL NRVKKKPYLA
LRDAEGRPDD IVAKEAWTNH RLRNDSVIVD TFHGLFKSTL VCPECSKVSV TFDPFCYLTL
PLPMKKDRTM EVFLVRSDPQ SRPTQYRVVV PKLGTVTDLC SALSKLCGIP PEKMVVADVY
NHRFHKIYRR DDALNQIMDK DDIFVYEVQE EDSERMNLPV YFRERHSKHV GSSSSTLLFG
QPLLISVPRH NLLADVLYEK ILERIGRYVK QQHNPNGESR ASASATLSSC SQAPECSASS
TINASLGGCG SPQSDGASCS ASSSNGSNHS GTCTEANGLD DGDDEAMDHQ VSPEPENGQS
EEEEESSDLE NGSKGETARL FTFSIVNSYG TVNISPLPCN GNVLKLNPHS TVAIDWDTES
KKLYYDEQEA EAYEKHESML QPQKKKTTVA LKECIELFTT METLGEHDPW YCPTCKKHQQ
ATKKFDLWSL PRILVVHLKR FSYNRCWRDK LDTLVDFPIR DLNMSEFVCD PKASPYVYDL
IAVSNHYGGM GGGHYTAYGK NKMDEKWYYF DDSSVSSASE DQIVTKAAYV LFYQRREEEN
PLKAEPSASL GGAAEAADDH MDTN
//
