ID A0A1S3PSV2_SALSA Unreviewed; 1380 AA.
AC A0A1S3PSV2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000256|ARBA:ARBA00026136};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 47 {ECO:0000256|ARBA:ARBA00030277};
DE AltName: Full=Ubiquitin thioesterase 47 {ECO:0000256|ARBA:ARBA00029910};
DE AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000256|ARBA:ARBA00032453};
GN Name=LOC106587191 {ECO:0000313|RefSeq:XP_014030767.1};
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_014030767.1};
RN [1] {ECO:0000313|RefSeq:XP_014030767.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014030767.1};
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};
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DR RefSeq; XP_014030767.1; XM_014175292.1.
DR GeneID; 106587191; -.
DR CTD; 55031; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|RefSeq:XP_014030767.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 172..558
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 83..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 155947 MW; 5964D3C4F5DB37B8 CRC64;
MEMVPSEENQ LVPKEIENAA EEPRVLCIVQ DTTNAKTVNE RLTLNLPAST TLSKLFEDVA
HKASYVNGTF DLAWGKTGDM GSLDPSSEMS LTESGFEPGK RNFLQLTDKD GEQPQIASDE
SGTAGSSGLD DSSQERFIGP LPRDGTVGCS SDYSSPSYSY SSILNKSDTG YVGLVNQAMT
CYLNSLLQTL FMTPEFRNAL YNWEFEESEE DPVTSIPYQL QRLFLLLQTS KKRAIETTDV
TRSFGWDSSE AWQQHDVQEL CRVMFDALEQ KWKQTEQQQF SPLTADLINQ LYQGKLKDYV
RCLECGYESW RIDTYLDIPL VIRPFGASQA YSSVEEALQA FVQPETLDGA NQYFCERCKK
KCDARKGLRF LHFPYLLTLQ LKRFDFDYTT MHRIKLNDRM SFPEELDMGP FIDVEDEKSP
QTESCTDSGA ENEGSCHSDQ MSNDFSADDG VDEGICLDSA SSTERVLKPK VPSLNTSSLT
FELFSVMVHS GSAAGGHYYA CIKSFSDGQW YSFNDQHVSK ITQEDIRKTY GGSSGSRGYY
SSAFASSTNA YMLIYRLKDP SRNAKYLDCD DFPEHIKHLV QREKESEEQE KRQREIERNT
CKIKLFCMHP VKTMALMENK LEVHKDKTLR KATEMAYKLM ELDGVVPLDC CRLVKYDEFH
EYLERSYEGE DDTPMGLLLG GVKSSYMFDL LLETRRPEQI FQPYKPGEVM VKVHVVDLKT
DTIAPPVSIR AYLNQSITEF KQLIAQATEL SAETMRVVLE RCYNDLRLLY VPNKTLKAEG
FFRSNKVFVE SSESPDHQVT FTDSLLWKLL DRHGNTIRLF VSLPVQSPGT NRTICPKVGG
DTEECSEGSK GNRNSVEAIL EESTEKLKNL SLQQQQGSST SDSQKSSDTS DFEHIESPSP
SQEPDSSVSA VVAVDNRELE NRIRAASGGS GGGTYSDPET QFPGEERSDS EVNNDRSTSS
VDSDILSSSH SSDTLCNADS GPIQLANGLD SHSITSSRRS KANEGKKETW DTAEEDSGTD
SEYDENGKSK AESYYLYFRA EPYAQEDGSG EGGQKCVLVH VDKRITLSAF KQNLEPFVGV
TSTQFKVFRV YANNQEFESV RLNETLSSFS DDNKVTIRLG RALKKGEYRV KVYQLLVNDA
EPCKFLVDTV FAKGMTVKQS KEELMPQLKD QCKLDLNIDK FRLRKKTWKN PGTVFLDYHV
YEEDINISSN WEVFLEVLDG PEKMKSMSQL AVLTRRWTPA QMKLEPFQEV VLESSSVEEL
KEKLSEISGI PLENLEFAKG RGTFPCDISV LEIHQDLDWN PKVSTLNVWP LYICDDGAVV
FYRDSTEEPM EQSEDERNEL MKKESSRLLK TGHRVSYSPR KEKALKIYLD GGPVKDPGQD
//
