ID A0A1S3NUM6_SALSA Unreviewed; 1623 AA.
AC A0A1S3NUM6;
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=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC106581527 {ECO:0000313|RefSeq:XP_014019108.1};
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_014019108.1};
RN [1] {ECO:0000313|RefSeq:XP_014019108.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014019108.1};
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_014019108.1; XM_014163633.1.
DR GeneID; 106581527; -.
DR CTD; 84669; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
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 Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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; IPR028135; Ub_USP-typ.
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; PF06337; DUSP; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00972; USP_1; 1.
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_014019108.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 228..263
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 264..299
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 369..599
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 748..1586
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 458..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 181128 MW; E3BF6233D259AB2C CRC64;
MGAKESRIGF LSYDEAIKRV TDVELKRLKD AFKRTSGLSY YMAQQCFYRE VLGDGVPPKV
AEVIYNSFGG TSKGLHFNNL IIGLVLLTRG RDGEKAKYLF SLFASESGGY AARDDMEAVL
RALDGEVPPS LRKCFSEGEK VNYERFKNWL LQNKEAFTFS RWLLSGGVCV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF VPLVSPPIHA SLSEGLFHAF
DENRDNHIDF KEISCGLSAC CRGPVAERQK FCFKVFDVDR DGVLSRAEIH EMVAALLEVW
KDNRTDTLPE LLTNVSDIVE GILKLHDTTK LGHLTLEDYQ IWSVNSALAN EFLNLLFQVC
HIVLGLRPAT AEEEGQIIRG WLEREGRHGL QPGENWFLIS SQWWMLWKDY VKYDHKSIVV
DQPSILSSLR NPQASATVGP APLEPGVGVR WVGDGLGVPS PASASEERSP DAVSSASEAT
ETHSTVVTPQ AGPSATEICF ARQHNMSDNN QCFSGANGHI PSLSQSQSQL AAQRPGAIDN
QPLVNTDPMK APSLTMEGGR LKQSLQLVAG RDFETVPEPV WRALFHWYGA NLSLPRPVIQ
QTKTGRAELE LFPRYLLFLR QQPATRTPQS NIWVNMGNVP SPNAPLKRVL AYTGCFSRVG
TIKDIHLYLS RRLRIKDEDM RLWLYNSENY LTLLDDEDHT LEGLKIQDEQ HLVIEVRNKD
MSWPEEMSFI ANSSKMDRHK VATEKGATGL SNLGNTCFMN SSIQCVSNTT PLTDYFISGR
HLYELNRTNP IGMRGHMAKC YGDLLMELWS GTQKNVAPLK LRWTIAKYAP RFNGFQQQDS
QELLAFLLDG LHEDLNRVHE KPYVELKDSN GRPDWEVALE AWENHLRRNR SIVVDLFHGQ
LKSQVKCKTC GHISARFDPF NFLSLPLPMD SSMHLEITVI MLDGSTPVRF GLRLNMDDKY
ICLKKQLSEL CSLKPEQILL AEVHTSNIKN FPQDNQKVRL SVNGFLCAFE IPVPCSPTSL
TSPTQTDITP VPMANGVAVA AKARPDGKPG LISNGMPSTV VHCRETTERS LANGGVGVPN
GHVSPVQDSP LIGYIIAMHR KMMRTELYFL SSQKNRASLF GMPLIVPCTV HTRQKDLYDA
VWIQVVRLAS PLPPQEASNH AQDCDDSMGY QYPFTLRVVG KDGNSCAWCP WYRFCRGCAV
DCTEDRASVG NACIAVDWDP TALHLRYQTS QERIVEEHCS VQQSRRAQAE PISLDSCLKA
FTSEEELGED ELYYCSKCKT HRLATKKLDL WRLPPILIVH LKRFQFVNGR WIKSQKIVQF
PRERFDPSVY LAPREAGLNG LHSVQSRSEG EELLRIGGGE TVSSISAPAG FLNILKASPA
SGRKSAPPSS ISCTSSPCSS PKTGGGSGGA GHRQTHLRLP QLGSRHRLSN SKENLEGSTR
EGGSDSDTEP REGRLQADTE GGLVGVRSEP EMSTTDALSS LSDVIVMNGD SGGHSNGPQR
TEASTAPSMN LETATALLHQ RDNSLENIYN LYAISCHSGI MGGGHYVTYA KNPNNKWYCY
NDSSCKEVHS EEMDTDSAYI LFYEQQAVDY SQFLPKTDGK KMADTTSMDE DFESDYKKYC
VLQ
//
