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WDR20_CAEEL
ID   WDR20_CAEEL             Reviewed;         768 AA.
AC   D9N129; Q17818;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=WD repeat-containing protein 20 homolog {ECO:0000250|UniProtKB:Q8TBZ3};
GN   Name=wdr-20 {ECO:0000312|EMBL:CBO21933.1, ECO:0000312|WormBase:C08B6.7b};
GN   ORFNames=C08B6.7;
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] {ECO:0000305}
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-48, 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-48.
CC       {ECO:0000269|PubMed:24356955}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b {ECO:0000269|PubMed:9851916};
CC         IsoId=D9N129-1; Sequence=Displayed;
CC       Name=a {ECO:0000269|PubMed:9851916};
CC         IsoId=D9N129-2; Sequence=VSP_055505;
CC   -!- TISSUE SPECIFICITY: Expressed in several neurons in the head and tail.
CC       {ECO:0000269|PubMed:24356955}.
CC   -!- DISRUPTION PHENOTYPE: 25% decrease in glr-1 expression in the ventral
CC       nerve cord. Changed locomotion behavior with mutants displaying
CC       decreased reversal frequencies consistent with decreased glutamergic
CC       signaling. {ECO:0000269|PubMed:24356955}.
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DR   EMBL; Z72502; CAA96589.1; -; Genomic_DNA.
DR   EMBL; Z72502; CBO21933.1; -; Genomic_DNA.
DR   RefSeq; NP_001256184.1; NM_001269255.1.
DR   RefSeq; NP_001335505.1; NM_001348580.1.
DR   AlphaFoldDB; D9N129; -.
DR   SMR; D9N129; -.
DR   BioGRID; 44441; 1.
DR   STRING; 6239.C08B6.7b; -.
DR   EPD; D9N129; -.
DR   PaxDb; D9N129; -.
DR   PeptideAtlas; D9N129; -.
DR   EnsemblMetazoa; C08B6.7a.1; C08B6.7a.1; WBGene00007428.
DR   EnsemblMetazoa; C08B6.7a.2; C08B6.7a.2; WBGene00007428.
DR   EnsemblMetazoa; C08B6.7b.1; C08B6.7b.1; WBGene00007428. [D9N129-1]
DR   EnsemblMetazoa; C08B6.7b.2; C08B6.7b.2; WBGene00007428. [D9N129-1]
DR   GeneID; 179410; -.
DR   UCSC; C08B6.7; c. elegans.
DR   CTD; 179410; -.
DR   WormBase; C08B6.7a; CE51874; WBGene00007428; wdr-20.
DR   WormBase; C08B6.7b; CE45162; WBGene00007428; wdr-20. [D9N129-1]
DR   eggNOG; KOG2394; Eukaryota.
DR   GeneTree; ENSGT00390000007686; -.
DR   HOGENOM; CLU_005019_1_0_1; -.
DR   InParanoid; D9N129; -.
DR   OMA; NQFAFSP; -.
DR   OrthoDB; 907634at2759; -.
DR   PhylomeDB; D9N129; -.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   PRO; PR:D9N129; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00007428; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; D9N129; baseline and differential.
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   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
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..768
FT                   /note="WD repeat-containing protein 20 homolog"
FT                   /id="PRO_0000430079"
FT   REPEAT          224..264
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          302..342
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          345..384
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          454..497
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          646..683
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REGION          103..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         733..751
FT                   /note="SEQQLRSPNITSPSYRVSA -> T (in isoform a)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_055505"
SQ   SEQUENCE   768 AA;  83741 MW;  D0FF711E8BFE3F2F CRC64;
     MHQHMLGPST SLGGTNNSAL QSSVLSEGVL LSHSQPTREE IKKNFETREG VYRSVPSAEF
     SRPRPLPQYH MPPGIASAAA SQIAAAGSTV RVSFLNGAEK SVESPEAVAP TSSTYEHHKN
     EPNGARIDMV DEAQADKICF NVGKELYVFS YRGTQTETDL SRPIDKRVYK GTSPTYHAFN
     QESAKNGSCQ LLIGFTLGQL QIIDPLEKSS SSPFSRLYNE DRYIEKTSVT CIRWLPGDSN
     IFLASYVSGN LYVYDQRISA ASSNNNGSSQ PPPWTIHKEG DKFAIHTWKG KVQRNPVTRW
     QIGEGSIHQF SFSGSDGKMM ATVSHDGFLR IFNYHAQELL AVMKSYFGGL LTLSWSPDAK
     LIATGGEDDL LTVYSVAEKR VVCRGQAHKS WVSQVKFDPY LCTTEEDLEN NGIAMTSTFD
     DVAKDFSIRS GPVPSTSADL NSGVMNATST FSRCSLASFN TINGAPAGNS VRYRIGSVGH
     DTFLCLWDIT EDMLNQGNIR RHRNSTIIAP MTTLEVQTNS LVGRLEDLQE VSPGGAGVNA
     SSDSQSITNN HTTPRPEKQK KKKFTKRLGF SKFTSGSSSA TSNPVGGHKI GTLMNGASVN
     SESSKKQNPG LISQISCCNE TRMLGSKFCP GIRDVPMIEP LMCKKVSHDR LTVLEFREDC
     VVTACQEGYI CTWGRPGRYQ PKRDCINSPG TASPESGQKP SGSTSAMTSS YGYGSDALNG
     VPPSRSSSTY SNSEQQLRSP NITSPSYRVS AASTSVYHRP TYAWQNAN
 
 
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