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 24-JAN-2024, entry version 86.
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.1; -.
DR EPD; D9N129; -.
DR PaxDb; 6239-C08B6-7b; -.
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 AGR; WB:WBGene00007428; -.
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; VVCRGQA; -.
DR OrthoDB; 1513505at2759; -.
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 cell types or 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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR14107:SF16; AT02583P; 1.
DR PANTHER; PTHR14107; WD REPEAT PROTEIN; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 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
//
