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   27-MAR-2024, entry version 79.
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.ENSXETP00000048966; -.
DR   MEROPS; C19.055; -.
DR   PaxDb; 8364-ENSXETP00000029972; -.
DR   GeneID; 100036690; -.
DR   KEGG; xtr:100036690; -.
DR   AGR; Xenbase:XB-GENE-5760041; -.
DR   CTD; 55031; -.
DR   Xenbase; XB-GENE-5760041; usp47.
DR   eggNOG; KOG4598; Eukaryota.
DR   InParanoid; A1A5G2; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
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:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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
//