ID A0A1S3P4K8_SALSA Unreviewed; 1007 AA.
AC A0A1S3P4K8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=LOC106583188 {ECO:0000313|RefSeq:XP_014022568.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014022568.1};
RN [1] {ECO:0000313|RefSeq:XP_014022568.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014022568.1};
RG RefSeq;
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_014022568.1; XM_014167093.1.
DR AlphaFoldDB; A0A1S3P4K8; -.
DR STRING; 8030.ENSSSAP00000107067; -.
DR PaxDb; 8030-ENSSSAP00000107067; -.
DR GeneID; 106583188; -.
DR KEGG; sasa:106583188; -.
DR OMA; ALKWHHD; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000087266; Chromosome ssa22.
DR Bgee; ENSSSAG00000073426; Expressed in sexually immature organism and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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:0000313|RefSeq:XP_014022568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 28..139
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 321..978
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 112248 MW; 6E71176199CA9C45 CRC64;
MMAEGGGPES GSAADPDPES VATQIPTPST ESQKQSIGTL LKTTLRKSDE WFLIDSRWFK
QWKKYVGFDS WDMYNVGEHS LYPGPVDNSG LFSDHETQIL KEHLIDELDY VLVPTEAWNK
FVSWYGCLEG QRPIVRKVVE HGMFVKHCKV EVYLLELNLC ENDNMDNVVT RHFSKADTID
TIEKEMRSLF EIPTGKETRL WNKYMSNTYE QLNKPDSTVQ DAGLFQGQVL VIECKNEDGT
WPRQASHPKS STATSRNFTT SPKLSSNSSA TISSTVTNGD SSSNSGYTLN NSTSSGNRLG
GYNSYSSSYN YRESPSQPGL CGLSNLGNTC FMNSALQCLS NACPLTEYFL NDQYEAEINR
ENPLGMRGEI AEAYADLVKQ MWLSRSSYVA PRTFKTQVGR FAPQFSGYQQ QDSQELLAFL
MDGLHEDLNR VKKKPYLALQ DAGGRPDEIV AKEAWTNHRL RNDSVIVDIF HGLFKSTLVC
PECAKISVTF DPFCYLTLPL PMKKDRTMEV FLVRIDPQSR PTQYRVVVPK LGSVTDLCSA
LSRLSGIPAE NMVVADVYNH RFHKIYRRDD GLNQIMEKDD IFVYEVAEED RERMNLPVYF
RERHSKHTGG STGTMLFGQP LLITVPRQNL AADMLYEKVL ERIGRYVNRA QSSTGEGRAN
ASASSASCSL AAECAATSSN HNTAGSGSPL SEGPSCSSSN GSNHSGTSNR SNGNGVCEGE
EEAMDHQVSP EPENGQSGEE EEASDLENGP KTKQCSSTPP KLFSFSMVNS YGTANISPLP
CDGNFLKLNT HSTVAIDWDS DTKKLCYDDQ EAEAYEKHES MLQAQKKKAT VALRECMELF
TTMETLGEHD PWYCPTCKKH QQATKKFDLW SLPRILVVHL KRFSYNRCWR DKLDTVVDFP
VRDLNMSEFV CDPKAGPYVY DLIAVSNHYG GMGGGHYTAY GKNKADGKWH YFDDSSVSAA
SEDQIVTKAA YVLFYQRRDV GDVPAKPSPS ASLGGATAEA ADHMDTN
//
