ID A0A1S3KX52_SALSA Unreviewed; 956 AA.
AC A0A1S3KX52;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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_013983189.1,
GN ECO:0000313|RefSeq:XP_013983190.1};
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_013983190.1};
RN [1] {ECO:0000313|RefSeq:XP_013983189.1, ECO:0000313|RefSeq:XP_013983190.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013983189.1,
RC ECO:0000313|RefSeq:XP_013983190.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
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DR RefSeq; XP_013983189.1; XM_014127714.1.
DR RefSeq; XP_013983190.1; XM_014127715.1.
DR STRING; 8030.ENSSSAP00000063073; -.
DR PaxDb; 8030-ENSSSAP00000063073; -.
DR GeneID; 106562719; -.
DR KEGG; sasa:106562719; -.
DR OMA; VIRISYP; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR Bgee; ENSSSAG00000046345; Expressed in actinopterygian pyloric caecum and 13 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; 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:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 6..109
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 162..729
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 731..824
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 833..935
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 275..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 106329 MW; AC8CC744808A6A15 CRC64;
MCDQGDICPH LNSIGEVTKE ELLQKSKGSC QSCGVGGPNL WACLQSECQY VGCGETFSDH
STLHAQANKH NLTVNLTTFR IWCYVCEREV FLEQRPAVVP AMSATHTPHH CKAKEHQVRH
RTKDAVHQPV SHHHPLKAVP IAVAEEEWSE SEEDALKPRG LTGMKNIGNS CYMNAALQAL
SNCPPLTQFF LDCSGLVRTD KKPALCKSYQ KLISELWHKK RPSYVVPTSL SQGIKLVNPM
FRGYAQQVGA SSQQDTQEFL RCLMDQLHEE LKEPLAECGG EGDDRRDGGD RSPSEDEFLS
CDSGASSDRG EGGGLGEPEL LIQDECGVGP RVGGGGTGTG GGVGTGGPIS EKERLKEKRV
LGSPLHRGSQ EMDEDADVDT TAAEEGGLER GAEEEGTPPS PRPQGPSQTQ GQTQSNSTPE
PDNEALMQKR PQSRPCSPVC TVQELHPKLS PNPTRSSPFR SAGPAYSFKK AQLFLGAKKQ
KQSRYRSVIS DIFDGSILSL VQCLTCDRVS TTVETFQDLS LPIPGKEDLA KLHSSIHQNL
PAKTGVSLDV YGSQGWITYI MDSIRRFVVS CIPSWFWGPM VTLEDCLAAF FAADELKGDN
MYSCERCKKL RNGVKYCKVL RLPEILCIHL KRFRHEVMYS FKINSHVAFP LEGLELRPFL
AKDSPSQITT YDLLSLICHH GTAGSGHYIA YCQNVINGQW YEFDDQYVTE VHETVVQNAE
AYVLFYRKSS EESVRERQKV VDLASMKEPS LLQFYISREW LNKFNTFTEP GPISNHTFLC
QHGGIPPNKY HYIDDLVVIL PQNVWEYLYN SFGGGPAVNH LYVCAICQVE LEALAKRRKV
EIDTFIRLNK EFQAEEAPTV ILCISMQWFR EWESFVKGKD NEPPGPIDNS KIGVMKGGHV
QLKQGADYGQ ISEETWQYLL GIYSGGPEIA VRQTVLATDT DSLHGERKIE AETRAL
//
