WDR48_CAEEL
ID WDR48_CAEEL Reviewed; 683 AA.
AC Q20059; B3GWA7; Q9U3G8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=WD repeat-containing protein 48 homolog;
GN Name=wdr-48; ORFNames=F35G12.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, INTERACTION WITH USP-46, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24356955; DOI=10.1074/jbc.m113.507541;
RA Dahlberg C.L., Juo P.;
RT "The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
RT deubiquitinating enzyme USP-46 to promote the abundance of the glutamate
RT receptor GLR-1 in the ventral nerve cord of Caenorhabditis elegans.";
RL J. Biol. Chem. 289:3444-3456(2014).
CC -!- FUNCTION: Together with wdr-20, binds to and stimulates the activity of
CC the deubiquitinating enzyme usp-46, leading to deubiquitination and
CC stabilization of the glr-1 glutamate receptor.
CC {ECO:0000269|PubMed:24356955}.
CC -!- SUBUNIT: Interacts with usp-46; the interaction increases the catalytic
CC activity of usp-46 in the presence of wdr-20.
CC {ECO:0000269|PubMed:24356955}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q20059-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q20059-2; Sequence=VSP_006793;
CC Name=c;
CC IsoId=Q20059-3; Sequence=VSP_037627;
CC -!- TISSUE SPECIFICITY: Expressed in several head neurons and cells in the
CC tail including the anal depressor cell. {ECO:0000269|PubMed:24356955}.
CC -!- DISRUPTION PHENOTYPE: Changed locomotion behavior with mutants
CC displaying decreased reversal frequencies consistent with decreased
CC glutamergic signaling. {ECO:0000269|PubMed:24356955}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR48 family. {ECO:0000305}.
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DR EMBL; Z46242; CAA86335.2; -; Genomic_DNA.
DR EMBL; Z46242; CAA86338.2; -; Genomic_DNA.
DR EMBL; Z46242; CAQ58416.1; -; Genomic_DNA.
DR PIR; T21808; T21808.
DR PIR; T21810; T21810.
DR RefSeq; NP_001129837.1; NM_001136365.2. [Q20059-3]
DR RefSeq; NP_497930.2; NM_065529.6. [Q20059-1]
DR RefSeq; NP_497931.2; NM_065530.5. [Q20059-2]
DR AlphaFoldDB; Q20059; -.
DR SMR; Q20059; -.
DR BioGRID; 40836; 6.
DR STRING; 6239.F35G12.4c; -.
DR EPD; Q20059; -.
DR PaxDb; Q20059; -.
DR PeptideAtlas; Q20059; -.
DR EnsemblMetazoa; F35G12.4a.1; F35G12.4a.1; WBGene00009441. [Q20059-1]
DR EnsemblMetazoa; F35G12.4b.1; F35G12.4b.1; WBGene00009441. [Q20059-2]
DR EnsemblMetazoa; F35G12.4c.1; F35G12.4c.1; WBGene00009441. [Q20059-3]
DR GeneID; 175600; -.
DR KEGG; cel:CELE_F35G12.4; -.
DR UCSC; F35G12.4b; c. elegans. [Q20059-1]
DR CTD; 175600; -.
DR WormBase; F35G12.4a; CE31501; WBGene00009441; wdr-48. [Q20059-1]
DR WormBase; F35G12.4b; CE31502; WBGene00009441; wdr-48. [Q20059-2]
DR WormBase; F35G12.4c; CE42674; WBGene00009441; wdr-48. [Q20059-3]
DR eggNOG; KOG0308; Eukaryota.
DR GeneTree; ENSGT00920000149157; -.
DR InParanoid; Q20059; -.
DR OMA; NWFNVDL; -.
DR OrthoDB; 261328at2759; -.
DR PhylomeDB; Q20059; -.
DR Reactome; R-CEL-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR PRO; PR:Q20059; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00009441; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:1903003; P:positive regulation of protein deubiquitination; IPI:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA: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; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome; Repeat; Ubl conjugation pathway;
KW WD repeat.
FT CHAIN 1..683
FT /note="WD repeat-containing protein 48 homolog"
FT /id="PRO_0000051506"
FT REPEAT 27..82
FT /note="WD 1"
FT REPEAT 88..130
FT /note="WD 2"
FT REPEAT 133..167
FT /note="WD 3"
FT REPEAT 176..215
FT /note="WD 4"
FT REPEAT 218..257
FT /note="WD 5"
FT REPEAT 260..299
FT /note="WD 6"
FT REPEAT 302..343
FT /note="WD 7"
FT REPEAT 389..428
FT /note="WD 8"
FT REGION 341..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 630
FT /note="D -> DGKVFRNKKILMVFE (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_037627"
FT VAR_SEQ 631..633
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_006793"
SQ SEQUENCE 683 AA; 76674 MW; 5EF022847B1953A1 CRC64;
MSSCVNTSQT GPKKKISFII RDEHEYSNRS AVSALQYDAQ NGRLFTGGSD TIIRTWSVPH
HKDAFSARGG VRSPGKNSPV QYQGSLEQHT DWVNDMILCG HGKILISASN DTTVKVWNIE
RDNKHGFIDC IRTHKDYVSC LAYAPIVEKA VSASFDHNIF VYDINANFKT VNNLIGCKDS
IYSLATTPNL SLVLGAGTEK CIRLFDPRTN EKIMKLRGHT DNVRALVVND DGTRALSAGS
DATIRLWDIG QQRCIATCIA HEEGVWTLQV DSSFTTVYSA GKDKMVVKTP LYDFTKSQLL
FKEEAPVKKL LLSEKDNPVS LWVGTWKSDI KRWSIRPSAQ LSIGGDEDGP STSNANHSVS
ASSSPPVTFK YIRVKDQKGQ QSTPELVIPG APAIKKHAML SDKRHVLTRD SDGNVALYDV
LAARKIKDYG KRIFEEVVDE NSRQVYIPSW FVVDSKSGML QITLDELDAL SSWLSSKDAG
FDDNDRETKL NYGGMMLRSL FERWPPCKMT NVDAADADDV QKATLNFISL PEHTPLIICE
GNGRPLYRLL VGDAGKEFEA NELAQIAPMW VIDAIERNQL PKFNKMPFYL LPHPSTNPKQ
PKKDRLSATE MLQVKKVMEH VYEKILSTND DITVGSIPLN QIHTKMEMYC NDQRLEPDMD
LRTVKHLYWK QSGELLLHYK PVK
