UBP47_XENLA
ID UBP47_XENLA Reviewed; 1350 AA.
AC Q5U252;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) 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; BC086278; AAH86278.1; -; mRNA.
DR RefSeq; NP_001088634.1; NM_001095165.1.
DR AlphaFoldDB; Q5U252; -.
DR SMR; Q5U252; -.
DR BioGRID; 105766; 1.
DR IntAct; Q5U252; 1.
DR MEROPS; C19.055; -.
DR GeneID; 495686; -.
DR KEGG; xla:495686; -.
DR CTD; 495686; -.
DR Xenbase; XB-GENE-5760104; usp47.L.
DR OrthoDB; 77113at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 495686; Expressed in testis and 19 other tissues.
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; IPR029071; Ubiquitin-like_domsf.
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 SUPFAM; SSF54236; SSF54236; 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..1350
FT /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT /id="PRO_0000408358"
FT DOMAIN 173..548
FT /note="USP"
FT REGION 111..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 487
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1350 AA; 153261 MW; EEABB140B02AF3AE CRC64;
MRPGEESQLV PKEIENAADE PRVLCIVQDT TNCKSVNERI TLNLPASTSV KQLYEDVSNK
AGYVSSTFSL MWGNGASNTD MAALDPTPDR TLQEAGFEAG KKNFLHLTDK DGEQPQLTSD
ESGTADSSGL DDSSQEKFIG PLPREESVAG TSNYVSQNYS YSSLLSKSDT GYVGLVNQAM
TCYLNSLLQT LFMTPEFRNA LYKWEFEESE EDPVSSIPYQ LQRLFVLLQT SKKRAIETTD
VTRSFGWDSS EAWQQHDVQE LCRVMFDALE QKWKQTEQAD LINQLYQGKL KDYVKCLECG
YESWRIDTFL DIPLVIRPYG SNTAFGSMEE ALHAFIQPET LDGPNQYFCE RCKRKCDARK
GLKFLHFPYL LTLQLKRFDF DYTSMHRIKL NDRMTFPDEL DMSPFIDMED EKSPQTDSCT
DSGAENEGSC HSDQMSNDFS TDDAVDEGIC LETNSNIEKL NKSVAEKNSL YELFSVMVHS
GSAAGGHYYA CIKSFADGQW YSFNDQHVSR ITQEDIKKTY GGATGNRGYY SSAFASSTNA
YMLMYRLKNP ARNAQFLEAS EFPEHIKLLV QKEQEQEEQE KRQREIERNT CKLKLFCMHP
VKQIMMESKL EVHKDKTMKE AVEIANKLMD LEGVIPLDCC RLVKYDEFHD YLERSYEDEE
DRTMGYLLGG VKSSYMFDLL LETKRPDQVF QSYKPGEVMV KVYVVDLKTE TVASPVSVRA
YLSQTIIEFK QLISKSVDLP PDSMRVILER CYNDLRLLNV ANKTLKAEGF FRSNKVFVES
SDSLDHQLVF TDSHLWKLLD RHANTIKLYV SLPEHPRPTA RSVGPKGGGD MNPQEDYCSR
AKSVDAILEE STEKLKSLSL QQHQDGGNGD SSKSTEGSDF ENIDSPLNEV DSSGSADNRE
LENRILPADP ENNFQPEERS DSDVNNDRST SSVDSDILSS SHSSDTLCNA DGTPIPLANG
LDSHSITSSR RSKANDGKKE TWDTAEEDSG TDSEYDESGK SRGEAQYMYF KAEPHAGEGC
LAEGSKCLLV NVDKRITLAA FKQQLESFVG VPSSQFKVFR VYASNQEFES VRLNETLSSF
SDDNKITIRL GRALKKGEYR VKIFQLLVNE PEPCKFVLDA VFSKGMTVRQ SKEELLPLLR
EQCGLDLSID RFRLRKKTWK NPGTVFLDSH VYENESISSC WEVLLEALDE TEKMKSMSQL
SLFTKRWRPS ELKLDPFKEV VLESNSVEEL RDKICEISAI PLENLEFAKG RGTFPCDISV
LEIHQDLDWN PKVSTLNAWP LYISDDGAVI FYRDKTEEVM ELTDEQRNEL VKKESSRLQK
TGHRVTYSPR KEKALKIYLD GPTNKDSAQD
