UBP47_XENTR
ID UBP47_XENTR Reviewed; 1354 AA.
AC A1A5G2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; BC128636; AAI28637.1; -; mRNA.
DR RefSeq; NP_001090710.1; NM_001097241.1.
DR AlphaFoldDB; A1A5G2; -.
DR SMR; A1A5G2; -.
DR STRING; 8364.ENSXETP00000029972; -.
DR MEROPS; C19.055; -.
DR PaxDb; A1A5G2; -.
DR PRIDE; A1A5G2; -.
DR GeneID; 100036690; -.
DR KEGG; xtr:100036690; -.
DR CTD; 55031; -.
DR Xenbase; XB-GENE-5760041; usp47.
DR eggNOG; KOG4598; Eukaryota.
DR InParanoid; A1A5G2; -.
DR OrthoDB; 77113at2759; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
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:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
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; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1354
FT /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT /id="PRO_0000408359"
FT DOMAIN 174..549
FT /note="USP"
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 488
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1354 AA; 153719 MW; E59BABE209E22310 CRC64;
MRPGEESHLV PKEIENAADE PRVLCIVQDT TSCKNINERI TLNLPASTSV KQLYEDVSSK
AGYVSGTFSL MWGNGASNMV DMAALDPTPD RTLQEAGFEA GKKNFLHLTD KNGEQPQLAS
DESGTADSSG LDDSTQEKFI GPLPREESVA CTSDYVSQNY SYSSLLSKSD TGYVGLVNQA
MTCYLNSLLQ TLFMTPEFRN ALYKWEFEES EEDPVSSIPY QLQRLFVLLQ TSKKRAIETT
DVTRSFGWDS SEAWQQHDVQ ELCRVMFDAL EQKWKQTEQA DLINQLYQGK LKDYVKCLEC
GYESWRIDTF LDIPLVIRPF GSNTAFGSME EALQAFIQPE TLDGPNQYFC ERCKRKCDAR
KGLKFLHFPY LLTLQLKRFD FDYTSMHRIK LNDRMTFPDE LDMSPFIDVE DEKSPQTDSC
TDSGAENEGS CHSDQMSNDF STDDAVDEGI CLETNSNIEK LNKSVSEKNS LYELFSVMVH
SGSAAGGHYY ACIKSFADGQ WYSFNDQHVS RITQEDIKKT YGGSTGNRGY YSSAFASSTN
AYMLMYRLKN PARNAKFPEA IEFPEHIKLL VQKEQEQEEQ EKRQREIERN TCKLKLFCMH
PVKQIMMESK LEVHKDKTMK EAVEIAHKLM DLEGVISLDC CRLVKYDEFH DYLERSYEDE
EDRTMGYLLG GVKSSYMFDL LLETKRSDQV FQSYKPGEVM VKVYVVDLKT ETVAPPVSVR
AYLSQTIIEF KQLISKSVDL LPDTMRVVLE RCYNDLRLLN VANKTLKAEG FFRSNKVFVE
SSDSLDYQLV FTDSHLWKLL DRHANTIRLY VSLPEHTPQT ARSVGPKGGG DSNLSEDYCS
RVKGNVKSVD AILEESTEKL KSLSLQQHQD GGNGDSSKST EGSDFENIDS PLNEADSGSA
DNRELENRIL PADPENNFQP EERSDSDVNN DRSTSSVDSD ILSSSHSSDT LCNADSAPIP
LANGLDSHSI TSSRRSKAND GKKETWDTAE EDSGTDSEYD ESGKSRGEAQ YMYFKAEPHA
GEGCLGEGNK CLLVSVDKRI TLAAFKQQLE SFVGVSSSQF KVFRVYASNQ EFESVRLNET
LSSFSDDNKI TIRLGRALKK GEYRVKIFQL LVNEPEPCKF LLDAVFSKGM TVRQSKEELL
PLLRDQCGLD LSIDRFRLRK KTWKNPGTVF LDYHVYENES ISSSWEVFLE ALDETEKMKS
MSQLSLFTKR WRPSELKLDP FKEIVMESNS VDELRDKICD ISAIPLENLE FAKGRGTFPC
DISVLEIHQD LDWNPKVSTL NAWPLYISDD GAVIFYRDKM EELVELTDEQ RNDLAKKESS
RLQKTGHRVT YSPRKEKALK IYLDGPSNKD SSQD
