ID A0A1S3KX33_SALSA Unreviewed; 887 AA.
AC A0A1S3KX33;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=LOC106562719 {ECO:0000313|RefSeq:XP_013983198.1};
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_013983198.1};
RN [1] {ECO:0000313|RefSeq:XP_013983198.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013983198.1};
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_013983198.1; XM_014127723.1.
DR AlphaFoldDB; A0A1S3KX33; -.
DR GeneID; 106562719; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
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; 2.
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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR PROSITE; PS51283; DUSP; 2.
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 ECO:0000313|RefSeq:XP_013983198.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 93..660
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 662..755
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 764..866
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 206..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 98913 MW; C0550214A13FC007 CRC64;
MLAVEKPFQI TAPYMHRIWC YVCEREVFLE QRPAVVPAMS ATHTPHHCKA KEHQDAVHQP
VSHHHPLKAV PIAVAEEEWS ESEEDALKPR GLTGMKNIGN SCYMNAALQA LSNCPPLTQF
FLDCSGLVRT DKKPALCKSY QKLISELWHK KRPSYVVPTS LSQGIKLVNP MFRGYAQQVG
ASSQQDTQEF LRCLMDQLHE ELKEPLAECG GEGDDRRDGG DRSPSEDEFL SCDSGASSDR
GEGGGLGEPE LLIQDECGVG PRVGGGGTGT GGGVGTGGPI SEKERLKEKR VLGSPLHRGS
QEMDEDADVD TTAAEEGGLE RGAEEEGTPP SPRPQGPSQT QGQTQSNSTP EPDNEALMQK
RPQSRPCSPV CTVQELHPKL SPNPTRSSPF RSAGPAYSFK KAQLFLGAKK QKQSRYRSVI
SDIFDGSILS LVQCLTCDRV STTVETFQDL SLPIPGKEDL AKLHSSIHQN LPAKTGVSLD
VYGSQGWITY IMDSIRRFVV SCIPSWFWGP MVTLEDCLAA FFAADELKGD NMYSCERCKK
LRNGVKYCKV LRLPEILCIH LKRFRHEVMY SFKINSHVAF PLEGLELRPF LAKDSPSQIT
TYDLLSLICH HGTAGSGHYI AYCQNVINGQ WYEFDDQYVT EVHETVVQNA EAYVLFYRKS
SEESVRERQK VVDLASMKEP SLLQFYISRE WLNKFNTFTE PGPISNHTFL CQHGGIPPNK
YHYIDDLVVI LPQNVWEYLY NSFGGGPAVN HLYVCAICQV ELEALAKRRK VEIDTFIRLN
KEFQAEEAPT VILCISMQWF REWESFVKGK DNEPPGPIDN SKIGVMKGGH VQLKQGADYG
QISEETWQYL LGIYSGGPEI AVRQTVLATD TDSLHGERKI EAETRAL
//
