WDR48_XENTR
ID WDR48_XENTR Reviewed; 678 AA.
AC Q05B17;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=WD repeat-containing protein 48;
DE AltName: Full=USP1-associated factor 1;
GN Name=wdr48; Synonyms=uaf1;
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 (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of deubiquitinating complexes, which acts as a
CC strong activator of usp1, usp12 and usp46. Enhances the usp1-mediated
CC deubiquitination of fancd2; usp1 being almost inactive by itself.
CC Activates deubiquitination by increasing the catalytic turnover without
CC increasing the affinity of deubiquitinating enzymes for the substrate.
CC Also activates deubiquitinating activity of complexes containing usp12.
CC Together with rad51ap1, promotes DNA repair by stimulating rad51-
CC mediated homologous recombination. Binds single-stranded DNA (ssDNA)
CC and double-stranded DNA (dsDNA). DNA-binding is required both for usp1-
CC mediated deubiquitination of fancd2 and stimulation of rad51-mediated
CC homologous recombination: both wdr48/uaf1 and rad51ap1 have coordinated
CC role in DNA-binding during these processes. Together with atad5 and by
CC regulating usp1 activity, has a role in pcna-mediated translesion
CC synthesis (TLS) by deubiquitinating monoubiquitinated pcna. Together
CC with atad5, has a role in recruiting rad51 to stalled forks during
CC replication stress. {ECO:0000250|UniProtKB:Q8TAF3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAF3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TAF3}. Lysosome
CC {ECO:0000250|UniProtKB:Q8TAF3}. Late endosome
CC {ECO:0000250|UniProtKB:Q8TAF3}. Note=Mainly in cytoplasmic
CC compartments. {ECO:0000250|UniProtKB:Q8TAF3}.
CC -!- DOMAIN: The WD repeats are required for the interaction with
CC deubiquitinating enzymes USP1, USP12 and USP46.
CC {ECO:0000250|UniProtKB:Q8TAF3}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR48 family. {ECO:0000305}.
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DR EMBL; BC123017; AAI23018.1; -; mRNA.
DR RefSeq; NP_001072858.1; NM_001079390.1.
DR AlphaFoldDB; Q05B17; -.
DR SMR; Q05B17; -.
DR STRING; 8364.ENSXETP00000009249; -.
DR PaxDb; Q05B17; -.
DR PRIDE; Q05B17; -.
DR Ensembl; ENSXETT00000009249; ENSXETP00000009249; ENSXETG00000004247.
DR GeneID; 780319; -.
DR KEGG; xtr:780319; -.
DR CTD; 57599; -.
DR Xenbase; XB-GENE-976371; wdr48.
DR eggNOG; KOG0308; Eukaryota.
DR HOGENOM; CLU_014960_0_1_1; -.
DR InParanoid; Q05B17; -.
DR OMA; NWFNVDL; -.
DR OrthoDB; 261328at2759; -.
DR PhylomeDB; Q05B17; -.
DR TreeFam; TF315205; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000004247; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; Q05B17; baseline.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035800; F:deubiquitinase activator activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR021772; WDR48/Bun107.
DR Pfam; PF11816; DUF3337; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA damage; DNA repair; DNA-binding; Endosome; Lysosome;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..678
FT /note="WD repeat-containing protein 48"
FT /id="PRO_0000378973"
FT REPEAT 28..67
FT /note="WD 1"
FT REPEAT 73..112
FT /note="WD 2"
FT REPEAT 115..154
FT /note="WD 3"
FT REPEAT 166..205
FT /note="WD 4"
FT REPEAT 208..247
FT /note="WD 5"
FT REPEAT 250..289
FT /note="WD 6"
FT REPEAT 292..334
FT /note="WD 7"
FT REPEAT 358..397
FT /note="WD 8"
FT REGION 608..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76353 MW; FA7B901F03F398C4 CRC64;
MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR DSIIRIWNVN
QHKQDPYIAS MEHHTDWVND IVLCCNGKTL ISASSDTTVK VWNAHKGFCM STLRTHKDYV
KALAYAKDKE LVASAGLDRQ IFLWDVNTLT ALTASNNTVT TSSLSGNKDS IYSLAMNQMG
TVIVSGSTEK VLRVWDPRTC QKLMKLKGHT DNVKALLLNR DGTQCLSGSS DGTIRLWSLG
QQRCIATYRV HDEGVWALQV NEGFTHVYSG GRDRKIYCTD LRNPDIRLLI CEEKAPVLKM
ELDRSADPPL ALWVATTKSS VNKWPIKGIL NFRSSGDYEN DCSTPLSPIC SQPDQVIKGG
ASIIQCNILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK VDFEEEIKKR FKMVYVPNWF
SVDLKTGMLT ITLDESDCFA AWVSAKDAGF SSPDGSDPKL NLGGLLLQAL LEFWPRTHIN
PMEEEENEVN HVANGEQENR IQKGNGYFQV PPHTPVIFGE AGGRTLFRLL CRDSGGETES
MLLNETVPQW VIDITVDKNM PKFNKIPFYL QPHSSSGAKT LKKDRLSASD MLQVRKVMEH
VYEKIINVDT ESQTTSSSNN EKPGEQEKEE DIAVLAEEKI ELLCQDQILD PNMDLRTVKH
FIWKSGGDLT LHYRQKST
