ID A0A1S3T2Y2_SALSA Unreviewed; 1242 AA.
AC A0A1S3T2Y2;
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=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC106613358 {ECO:0000313|RefSeq:XP_014070956.1};
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_014070956.1};
RN [1] {ECO:0000313|RefSeq:XP_014070956.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014070956.1};
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_014070956.1; XM_014215481.1.
DR AlphaFoldDB; A0A1S3T2Y2; -.
DR STRING; 8030.ENSSSAP00000062089; -.
DR KEGG; sasa:106613358; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 1.
DR CDD; cd02257; Peptidase_C19; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|RefSeq:XP_014070956.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 113..148
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 149..184
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 254..476
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 379..1205
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 321..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 137811 MW; C93C934DB8013B5D CRC64;
MEAVLRAVDG EVPPSLRKCF SEGEKVNYER FKNWLLQNTE AFTFSRWLLS GGVCVTLTDD
NDTPTFYQTL AGVTHLEESD IIDLEKRYWL LKAQSRTGRF DLETFVPLVS PPIHASLSKG
LFHAFDENRD NHIDFKEISC GLSACCRGPV AERQKFCFKV FDVDRDGVLS RDEIHEMVVA
LLEVWKDNRT HTLPELLTNV SDIVEGILKM HDTTKLGHLT LEDYQIWSVT SALANEFLNL
LFQVSHIVLG LRPATPEEEG QIIRGWLERE GRHGLQPGEN RFLISSQWWK LWKDYVRYDH
KSIVVDQPSI LSSLRNPQAS ATVEPAPLKP GVGGSLGVPS PASPSEDRSP NALSSASEAT
ETHNTVVTTQ TGPSATEICF ARQHNNQCFS GSNGHIPSLS QSQSQLAAQR PGAIDNQPLV
NTDPMKVCVC LPYHIYCLWT IAKYAPRFNG FQQQDSQELL AFLLDGLHED LNRVHEKPYV
ELKDSNGRPD WEVASEAWEN HLRRNRSIVV DLFHGQLKSQ VKCKTCGHIS ARFDPFNFLS
LPLPMDSSMH LEITVIMLDG STPVRFGLRL NIDDKYIGLK KQLSELCSLK PDQILLAEVH
TSNIKNFPQD NQKVRLSVNG FLCAFEIPVP GSPTSLSSPT QTGISPVPMA NGVAVTAEGH
LAGKPGLIPN GVPSAVVPCR EAAERALVDG GLWVSPVQDS PFIGYIIAMH RKMMRTELYF
LSSQKNRTSL FGMPLIVPCT VHTSQKDLYD AVWIQVTRLA SPLPPQEASN HAQDCDDSMG
YQYPFTLRVV GKDGNSCAWC PWYRFCRGCA VDCTEDRASV GNAYIAVDWD PTALHLRYQT
SQERIVEEHC SVQQSRRAQA EPISLDSCLK AFTSEEELGE DELYYCSKCK THRLATKKLD
LWRLPPILIV HLKRFQFVNG RWIKSQKIVQ FPRESFDPSV YLAPREAGLN GLHSVQSRSE
GEGLLRIGGG ETVSSVSAPA GFLNILKASP ASGRKSAPPS FISRTSSPGS SPKTGGGSPG
GTGNRQTRLR LPQLASRHRL SNSKENLEGS TRERGSSPDT EPREGAPQAD TDGGLVGVTR
GGFGEVRVRS GPEMSTTDVS SSLSNVIVMN GVSGGHSNEV LSTEPSTDPE TTATAQLHRR
DNSLENIYNL YAISCHSGIM GGGHYVTYAK NPNNKWYCYN DSSCKEVHSE EMDTDSAYIL
FYEQQGVDFS QFLPKTDGKK MADTTSMDED FESDYKKYCV LQ
//
