WDR48_CHICK
ID WDR48_CHICK Reviewed; 678 AA.
AC Q5F3K4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=WD repeat-containing protein 48;
DE AltName: Full=USP1-associated factor 1;
GN Name=WDR48; Synonyms=UAF1; ORFNames=RCJMB04_14o15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 -!- 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; AJ851646; CAH65280.1; -; mRNA.
DR RefSeq; NP_001026135.1; NM_001030964.1.
DR AlphaFoldDB; Q5F3K4; -.
DR SMR; Q5F3K4; -.
DR STRING; 9031.ENSGALP00000030646; -.
DR PaxDb; Q5F3K4; -.
DR Ensembl; ENSGALT00000031283; ENSGALP00000030646; ENSGALG00000006052.
DR GeneID; 420427; -.
DR KEGG; gga:420427; -.
DR CTD; 57599; -.
DR VEuPathDB; HostDB:geneid_420427; -.
DR eggNOG; KOG0308; Eukaryota.
DR GeneTree; ENSGT00920000149157; -.
DR HOGENOM; CLU_014960_0_1_1; -.
DR InParanoid; Q5F3K4; -.
DR OMA; NWFNVDL; -.
DR OrthoDB; 261328at2759; -.
DR PhylomeDB; Q5F3K4; -.
DR TreeFam; TF315205; -.
DR Reactome; R-GGA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-GGA-5689880; Ub-specific processing proteases.
DR Reactome; R-GGA-6783310; Fanconi Anemia Pathway.
DR PRO; PR:Q5F3K4; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000006052; Expressed in spermatid and 14 other tissues.
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:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:1902525; P:regulation of protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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 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_0000051403"
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 608..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76314 MW; 3EA3E0009DDEA18E CRC64;
MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR DSIIRIWSVN
QHKQDPYIAS MEHHTDWVND IVLCCNGKTL ISASSDTTVK VWNAHKGFCM STLRTHKDYV
KALAYAKDKE LVASAGLDRQ IFLWDVNTLT ALTASNNTVT TSSLSGNKDS IYSLAMNQMG
TVIVSGSTEK VLRVWDPRTC AKLMKLKGHT DNVKALLLNR DGTQCLSGSS DGTIRLWSLG
QQRCIATYRV HDEGVWALQV NEAFTHVYSG GRDRKIYCTD LRNPDIRVLI CEEKAPVLKM
ELDRSADPPP AIWVATTKSS VNKWTLKGIH NFRASGDYDN DCTNPIPPLC TQPDQVIKGG
ASIIQCHILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK VDFEEEIKKR FKMVYVPNWF
SVDLKTGMLT ITLDESDCFA AWVSAKDAGF SSPDGSDPKL NLGGLLLQAL LEYWPRTHIN
PMDEEENEIN HAVNGEQENR VQKGNGYFQV PPHTPVIFGE AGGRTLFRLL CRDSGGETES
MLLNETVPQW VIDITVDKNM PKFNKIPFYL QPHSSSGAKT LKKDRLSASD MLQVRKVMEH
VYEKIINLDN ESQTTSSSNN EKAGEQEKEE DIAVLAEEKI ELLCQDQVLD PNMDLRTVKH
FIWKSGGDLT LHYRQKST
