WDR48_PONAB
ID WDR48_PONAB Reviewed; 677 AA.
AC Q5RAW8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=WD repeat-containing protein 48;
DE AltName: Full=USP1-associated factor 1;
GN Name=WDR48; Synonyms=UAF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 Docks at the distal end of the USP12 fingers domain and induces a
CC cascade of structural changes leading to the activation of the enzyme.
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 -!- SUBUNIT: Interacts with USP46. Interacts with USP1. Interacts with
CC USP12. Component of the USP12-WDR20-WDR48 deubiquitinating complex.
CC Interacts with PHLPP1. Interacts with RAD51AP1; the interaction is
CC direct and promotes formation of a trimeric complex with RAD51 via
CC RAD51AP1. Interacts with ATAD5; the interaction regulates USP1-mediated
CC PCNA deubiquitination. Interacts with RAD51; the interaction is
CC enhanced under 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; CR858893; CAH91092.1; -; mRNA.
DR RefSeq; NP_001125636.1; NM_001132164.2.
DR AlphaFoldDB; Q5RAW8; -.
DR SMR; Q5RAW8; -.
DR STRING; 9601.ENSPPYP00000015661; -.
DR Ensembl; ENSPPYT00000016282; ENSPPYP00000015661; ENSPPYG00000014001.
DR GeneID; 100172554; -.
DR KEGG; pon:100172554; -.
DR CTD; 57599; -.
DR eggNOG; KOG0308; Eukaryota.
DR GeneTree; ENSGT00920000149157; -.
DR HOGENOM; CLU_014960_0_1_1; -.
DR InParanoid; Q5RAW8; -.
DR OMA; NWFNVDL; -.
DR OrthoDB; 261328at2759; -.
DR TreeFam; TF315205; -.
DR Proteomes; UP000001595; Chromosome 3.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA damage; DNA repair; DNA-binding; Endosome;
KW Lysosome; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..677
FT /note="WD repeat-containing protein 48"
FT /id="PRO_0000051402"
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..452
FT /note="WD 8"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH57"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAF3"
FT MOD_RES 578
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH57"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAF3"
SQ SEQUENCE 677 AA; 76223 MW; 3A5E28880EC4883D CRC64;
MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR DSIIRIWSVN
QHKQDPYIAS MEHHTDWVND IVLCCNGKTL ISASSDTTVK VWNAHKGFCM STLRTHKDYV
KALAYAKDKE LVASAGLDRQ IFLWDVNTLT ALTASNNTVT TSSLSGNKDS IYSLAMNQLG
TIIVSGSTEK VLRVWDPRTC AKLMKLKGHT DNVKALLLNR DGTQCLSGSS DGTIRLWSLG
QQRCIATYRV HDEGVWALQV NDAFTHVYSG GRDRKIYCTD LRNPDIRVLI CEEKAPVLKM
ELDRSADPPP AIWVATTKST VNKWILKGIH NFRASGDYDN DCTNPITPLC TQPDQVIKGG
ASIIQCHILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK VDFEDEIKKR FKMVYVPNWF
SVDLKTGMLT ITLDESDCFA AWVSAKDAGF SSPDGSDPKL NLGGLLLQAL LEYWPRTHVN
PMDEEENEVN HVNGEQENRV QKGNGYFQVP PHTPVIFGEA GGRTLFRLLC RDSGGETESM
LLNETVPQWV IDITVDKNMP KFNKIPFYLQ PHASSGAKTL KKDRLSASDM LQVRKVMEHV
YEKIINLDNE SQTTSSSNNE KPGEQEKEED IAVLAEEKIE LLCQDQVLDP NMDLRTVKHF
IWKSGGDLTL HYRQKST
