UBP47_CHICK
ID UBP47_CHICK Reviewed; 1375 AA.
AC E1C1R4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 47;
DE AltName: Full=Ubiquitin thioesterase 47;
DE AltName: Full=Ubiquitin-specific-processing protease 47;
GN Name=USP47;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Ubiquitin-specific protease that specifically deubiquitinates
CC monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby
CC playing a role in base-excision repair (BER). {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP47 subfamily.
CC {ECO:0000305}.
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DR EMBL; AADN02030606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02030607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C1R4; -.
DR SMR; E1C1R4; -.
DR STRING; 9031.ENSGALP00000008918; -.
DR PaxDb; E1C1R4; -.
DR VEuPathDB; HostDB:geneid_423032; -.
DR eggNOG; KOG4598; Eukaryota.
DR InParanoid; E1C1R4; -.
DR PhylomeDB; E1C1R4; -.
DR TreeFam; TF314142; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1375
FT /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT /id="PRO_0000408357"
FT DOMAIN 187..563
FT /note="USP"
FT REGION 425..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 502
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1375 AA; 157247 MW; E5929D1809146267 CRC64;
MKEFVSMRLL PEDMFWSCRQ STLAEMKKKF AQVESAAEEP RVLCIIQDTT NSKTVNERVT
LNVPASTPLK KLFEDVASKV GYVNGTFDLV WGNGDNVTDM TPIDQNSDKT ILDAGFEPGK
KNFLHLTDKD GEQPHIMQEE SGTTEDSAQD RFIGPLPREG SVGCTNDYVS QSYSYSSVLS
KSETGYVGLV NQAMTCYLNS LLQTLFMTPE FRNALYKWEF EESEEDPVTS IPYQLQRLFV
LLQTSKKRAI ETTDVTRSFG WDSSEAWQQH DVQELCRVMF DALEQKWKQT EQADLINQLY
QGKLKDYVRC LECGYEGWRI DTYLDIPLVI RPYGSNQAFA SVEEALHAFI QPEILDGPNQ
YFCERCKKKC DARKGLRFLH FPYLLTLQLK RFDFDYTTMH RIKLNDRMTF PEELDMSIFI
DVEDEKSPQT ESCTDSGAEN EGSCHSDQMS NDFSNDDGVD EGICLESNSA AERIAKVGSE
KNSLLYELFS VMVHSGSAAG GHYYACIKSF SDDQWYSFND QHVSKITQED IKKTYGGSSG
SRGYYSSAFA SSTNAYMLIY RLKDPARNAK FLESHEYPDH IKQLVQKERE LEEQEKRQRE
IERNTCKIKL FCMHPTKQIM MENKLEVHKD RTLKEAVGIA YKLMDLEEAV PLDCCRLVKY
DEFHDYLERS YEGEEDTPMG LLLGGVKSTY MFDLLLETRR PDQIFQCYKP GEVMVKVHVV
DLKTESVAPP ISVRAYLNQT VSEFKQLISK ATHLPAETMR VVLERCYNDL RLLTVSSKTL
KAEGFFRSNK VFIESSESLD RHVAYTDSHL WKLLDRHANT IRLYVSLPEQ SPGSQFRRSI
YQKPSGDLGN LDEACERVKG PAGNMKSVEA ILEESTEKLK SLSLQQQQQE GDNGDSSKST
EASDFENIES PSNEIDSSAS VENRELENQI QISDPENLQS EERSDSDVNN DRSTSSVDSD
ILSSSHSSDT LCNVDNAPIP LANGLDSHSI TSSRRSKANQ GKKETWDTAE EDSGTDSEYD
ESGKSRGETQ YMYFKSEPYT ADEGSGEGQK WLMVHVDKRI TLSAFKQQLE PFVGVPSSHF
KVFRVYASNQ EFESVRLNET LSSFSDDNKI TIRLGRALKK GEYRVKVYQL LVNEPEPCKF
LLDAVFAKGM TVRQSKEELL PQLREQCGLD LTIDRFRLRK KTWKNPGTVF LDYHIYEEDI
NISSNWEVFL EILDGVEKMK SMSQLAVLSR RWRPSEMKLD SFQEVVLESS SVEELKEKLS
ELSGIPLENI EFAKGRGTFP CDISVLEIHQ DLDWNPKVST LNVWPLYICD DGAVIFYRDK
TEELMELTDE QRNELMKKES SRLQKTGHRV TYSPRKEKAL KIYLDGAPNK DLTQD
