ID M3WSE7_FELCA Unreviewed; 1376 AA.
AC M3WSE7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
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=USP47 {ECO:0000313|Ensembl:ENSFCAP00000017283.2,
GN ECO:0000313|VGNC:VGNC:66890};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000017283.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000017283.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017283.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000017283.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017283.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000017283.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017283.2};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04002890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006937165.1; XM_006937103.3.
DR STRING; 9685.ENSFCAP00000017283; -.
DR PaxDb; 9685-ENSFCAP00000000858; -.
DR Ensembl; ENSFCAT00000025356.4; ENSFCAP00000017283.2; ENSFCAG00000000922.6.
DR GeneID; 101090643; -.
DR CTD; 55031; -.
DR VGNC; VGNC:66890; USP47.
DR GeneTree; ENSGT00940000157223; -.
DR HOGENOM; CLU_002928_0_0_1; -.
DR InParanoid; M3WSE7; -.
DR OMA; FLCEWIV; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000011712; Chromosome D1.
DR Bgee; ENSFCAG00000000922; Expressed in testis and 10 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
DR GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT DOMAIN 188..564
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 425..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 157375 MW; 762F0F18F9AA6C29 CRC64;
MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVNERI
TLNLPASTPL RKLFEDVANK VGYINGTFDL VWGNGINTAD MAPLDHTSDK SLLDANFEPG
KKNFLHLTDK DGEQPQILLE DSSAGDDSVH DRFIGPLPRE GSVGSTSDYV SQNYSYSSIL
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEESEEDPVT SIPYQLQRLF
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMT FPEELDMSTF
IDVEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSNDDGV DEGICLESNS GTEKISKPGL
EKNSLIYELF SVMVHSGSAA GGHYYACIKS FSDEQWYSFN DQHVSRITQE DIKKTHGGSS
GSRGYYSSAF ASSTNAYMLI YRLKDPARNA KFLEVDEYPE HIKNLVQRER ELEEQEKRQR
EIERNTCKIK LFCLHPVKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEEV IPMDCCRLVK
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQVFQSYK PGEVMVKVHV
VDLKAESVAA PVTVRAYLNQ TVTEFKQLIS KAIHLPAETM RIVLERCHND LRLLTVPSKT
LKAEGFFRSN KVFVESSETL DYQMAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT
ACQKAGGDSG GNVDDDCDRV KGPVGSLKSV EAILEESTEK LKSLSLQQQQ DGDNGDSSKS
TETSDFENIE SPLNERDSSA SVDNRELEQH IQTSDPENFQ SEERSDSDVN NDRSTSSVDS
DILSSSHSSD TLCNADNAQI PLANGLDSHS ITSSRRTKAN EGKKETWDTA EEDSGTDSEY
DESGKSRGEI QYMYFKAEPY AADEGSGEGH KWLMVHVDKR ITLAAFKQHL EPFVGALSSH
FKVFRVYASN QEFESVRLNE TLSSFSDDNK ITIRLGRALK KGEYRVKVYQ LLVNEQEPCK
FLLDAVFAKG MTVRQSKEEL IPQLREQCGL ELSTDRFRLR KKTWKNPGTV FLDYHIYEED
INISSNWEVF LEVLDGVEKM KSMSQLAVLS RRWRPSEMKL DPFQEVVLES SSVDELREKL
CEISGIPLED IEFAKGRGTF PCDISVLDIH QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD
KTEELMELTD EQRNELMKKE SSRLQKTGHR VTYSPRKEKA LKIYLDGAPN KDLTQD
//
