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Database: UniProt
Entry: A0A3P8YE60_ESOLU
LinkDB: A0A3P8YE60_ESOLU
Original site: A0A3P8YE60_ESOLU 
ID   A0A3P8YE60_ESOLU        Unreviewed;      1372 AA.
AC   A0A3P8YE60;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000256|ARBA:ARBA00026136};
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};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000014913.1, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000014913.1, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000014913.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   Ensembl; ENSELUT00000023844.2; ENSELUP00000014913.1; ENSELUG00000015067.2.
DR   GeneTree; ENSGT00940000157223; -.
DR   Proteomes; UP000265140; LG02.
DR   Bgee; ENSELUG00000015067; Expressed in camera-type eye and 15 other cell types or tissues.
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:SF902; UBIQUITIN-SPECIFIC PEPTIDASE 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   Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT   DOMAIN          174..547
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          114..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..988
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1372 AA;  155446 MW;  923DFF98D491E4B1 CRC64;
     MEMVPSEENQ LVTLPKETEN AAEEPRVLCI VQDTTNAKTV NERLTLNLPA STTLSKLFNE
     VAHKAGYVSG TFDLAWGKTT DVAPLDLSSE MSLTESGFEA GKRNFLQLTD KDGEQPQLAS
     DDLGTADSSG LDDSSHERLM GPLPRDCTVG CSSDYSSPSY SYSSILNKSD TGYVGLVNQA
     MTCYLNSLLQ TLFMTPEFRN ALYNWEFEES EEDPVTSIPY QLQRLFVLLQ TSKKRAIETT
     DVTRSFGWDS SEAWQQHDVQ ELCRVMFDAL EQKWKQTEQA DLINQLYQGK LKDYVRCLEC
     GYESWRIDTY LDIPLVIRPF GASQAYCSVE EALQAFVQPE TLDGANQYFC ERCKKKCDAR
     KGLRFLHFPY LLTLQLKRFD FDYTTMHRIK LNDRMSFPEE LDMSPFIDVE DEKSPQTESC
     TDSGAENEGS CHSDQMSNDF STDDGVDEGI CLDSASSTER VLKPKSSLTF ELFSVMVHSG
     SAAGGHYYAC IKSFSDGQWY SFNDQHVSKI TQEDIRKTYG GSSGNRGYYS SAFASSTNAY
     MLIYRLKDPS RNAKYLDCDN FPEHIKHLVQ REKESEEQEK RQKEIERNTC KIKLFCMHPV
     KMMMMENKLE VHKDKTLREA TEMAYKLMDI NGVVPMDCCR LVKYDEFHEY LERSYEGEED
     TTMGQLLGGV KSSYMFDLLL ETRRPEQVFQ PYKPGEVMVK VYVLDLNTET IAPPVSLRAY
     LNQSVTEFKQ LIAQATGLSA ETMRVVLERC YNDLRLLYVP NKTLKAEGFF RSNKVFVESS
     ESTDNEVAFT DSLLWKLLDR HANTIRLFVS LPEQSPGIHR TICQKVGCDP EESLENSKGS
     RKSVDAILEE STEKLKNLTL QQQQGSSTSD SQKSSDSSDF EHIKSPSPSQ EPNSVSSVSA
     VVAVDNRELE NRIQAASEGC GAVSGGASSD LETQFTGEER SDSEVNNDRS TSSVDSDILS
     SSHSSDTLCN ADSGPIQLVN GLDSHSITSS RRSKAREGKK ETWDTAEEDS GTDSEYDENG
     RSKTDSQYLY FRSEPYAQDD GSGEGQKCLL VHVDKRITLA AFKQNLEPFV GITSSQFKVF
     RVYANNQEFE SVRLNETLSS FSDDNKITIR LGRALKKGEY RVKVYQLLVN DAEPCKFLVD
     TVFAKGMTVK QSKEELLPQL RDQCKLDLSV DRFRLRKKTW KNPGTVFLDY HIYEEDINIS
     SNWEVFLEVL DGPEKMKSMS QLAVLTRRWT PAQMKLEPFQ EVVLESSTVE ELNEKLSEIS
     GIPLENLEFA KGRGTFPCDI SVLEIHQDLD WNPKVSTLNV WPLYICDDGA VVFYRDNTEE
     PMELSEDERN ELMKRESSRL LKTGHRVSYS PRKEKALKIY LDGGPAKDPG QD
//
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