WDS_DROME
ID WDS_DROME Reviewed; 361 AA.
AC Q9V3J8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein will die slowly;
GN Name=wds; Synonyms=l(1)3Ad, l(1)zw8; ORFNames=CG17437;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R;
RX PubMed=12471440; DOI=10.1007/s00438-002-0768-0;
RA Hollmann M., Simmerl E., Schaefer U., Schaefer M.A.;
RT "The essential Drosophila melanogaster gene wds (will die slowly) codes for
RT a WD-repeat protein with seven repeats.";
RL Mol. Genet. Genomics 268:425-433(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATAC COMPLEX,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18327268; DOI=10.1038/nsmb.1397;
RA Suganuma T., Gutierrez J.L., Li B., Florens L., Swanson S.K.,
RA Washburn M.P., Abmayr S.M., Workman J.L.;
RT "ATAC is a double histone acetyltransferase complex that stimulates
RT nucleosome sliding.";
RL Nat. Struct. Mol. Biol. 15:364-372(2008).
RN [7]
RP IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21694722; DOI=10.1038/emboj.2011.194;
RA Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.;
RT "Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with
RT role in transcription.";
RL EMBO J. 30:2817-2828(2011).
RN [8]
RP IDENTIFICATION IN THE SET1 AND MLL3/4 COMPLEXES.
RX PubMed=21875999; DOI=10.1128/mcb.06092-11;
RA Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
RA Florens L., Eissenberg J.C., Shilatifard A.;
RT "The COMPASS family of H3K4 methylases in Drosophila.";
RL Mol. Cell. Biol. 31:4310-4318(2011).
RN [9]
RP INTERACTION WITH SET1.
RX PubMed=22048023; DOI=10.1534/genetics.111.135863;
RA Hallson G., Hollebakken R.E., Li T., Syrzycka M., Kim I., Cotsworth S.,
RA Fitzpatrick K.A., Sinclair D.A., Honda B.M.;
RT "dSet1 is the main H3K4 di- and tri-methyltransferase throughout Drosophila
RT development.";
RL Genetics 190:91-100(2012).
RN [10]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=25310983; DOI=10.1016/j.celrep.2014.09.002;
RA Pascual-Garcia P., Jeong J., Capelson M.;
RT "Nucleoporin Nup98 associates with Trx/MLL and NSL histone-modifying
RT complexes and regulates Hox gene expression.";
RL Cell Rep. 9:433-442(2014).
RN [11]
RP FUNCTION, INTERACTION WITH TET, AND DISRUPTION PHENOTYPE.
RX PubMed=30078725; DOI=10.1016/j.molcel.2018.07.005;
RA Yao B., Li Y., Wang Z., Chen L., Poidevin M., Zhang C., Lin L., Wang F.,
RA Bao H., Jiao B., Lim J., Cheng Y., Huang L., Phillips B.L., Xu T., Duan R.,
RA Moberg K.H., Wu H., Jin P.;
RT "Active N6-Methyladenine Demethylation by DMAD Regulates Gene Expression by
RT Coordinating with Polycomb Protein in Neurons.";
RL Mol. Cell 71:848-857.e6(2018).
CC -!- FUNCTION: Contributes to histone modification. May position the N-
CC terminus of histone H3 for efficient trimethylation at 'Lys-4'
CC (PubMed:25310983). In neurons and together with DNA N6-methyl adenine
CC demethylase Tet, plays a role in the maintenance of transcriptional
CC activation for specific sets of genes (PubMed:30078725).
CC {ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:30078725}.
CC -!- SUBUNIT: Core component of several methyltransferase-containing
CC complexes. Component of the SET1 complex, composed at least of the
CC catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1, hcf
CC and Dpy-30L1 (PubMed:21694722). Interacts with Set1 (PubMed:21694722,
CC PubMed:21875999, PubMed:22048023). Component of the MLL3/4 complex
CC composed at least of the catalytic subunit trr, ash2, Rbbp5, Dpy-30L1,
CC wds, hcf, ptip, Pa1, Utx, Lpt and Ncoa6 (PubMed:21875999). Component of
CC the Ada2a-containing (ATAC) complex composed of at least Ada2a, Atac1,
CC Hcf, Ada3, Gcn5, Mocs2B, Charac-14, Atac3, Atac2, NC2beta and wds
CC (PubMed:18327268). Interacts with Nup98 (PubMed:25310983). Interacts
CC (via WD repeats) with Tet (via C-terminus) (PubMed:30078725).
CC {ECO:0000269|PubMed:18327268, ECO:0000269|PubMed:21694722,
CC ECO:0000269|PubMed:21875999, ECO:0000269|PubMed:22048023,
CC ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:30078725}.
CC -!- INTERACTION:
CC Q9V3J8; Q9VAF4: dgt1; NbExp=5; IntAct=EBI-90899, EBI-120581;
CC Q9V3J8; A4V2Z1: nsl1; NbExp=8; IntAct=EBI-90899, EBI-9630827;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18327268,
CC ECO:0000269|PubMed:21694722}.
CC -!- TISSUE SPECIFICITY: Expressed in imaginal disks, larval brain, nurse
CC cells, spermatogonia and spermatocytes. {ECO:0000269|PubMed:12471440}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC {ECO:0000269|PubMed:12471440}.
CC -!- DISRUPTION PHENOTYPE: Larval lethal (PubMed:12471440). Conditional
CC RNAi-mediated knockdown in larval wing imaginal disks results in
CC reduced levels of trimethylated 'Lys-4' in histone H3
CC (PubMed:25310983). RNAi-mediated knockdown in neurons, does not affect
CC mushroom bodies alpha lobe development (PubMed:30078725). Simultaneous
CC RNAi-mediated knockdown of wds and Tet results in enhanced mushroom
CC body alpha lobe development defects compared to the single Tet
CC knockdown (PubMed:30078725). {ECO:0000269|PubMed:12471440,
CC ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:30078725}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR5/wds family. {ECO:0000305}.
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DR EMBL; AF233288; AAF43418.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45791.1; -; Genomic_DNA.
DR EMBL; AL138972; CAB72292.1; -; Genomic_DNA.
DR EMBL; AY118386; AAM48415.1; -; mRNA.
DR RefSeq; NP_001245503.1; NM_001258574.2.
DR RefSeq; NP_524984.1; NM_080245.5.
DR PDB; 4CY3; X-ray; 1.40 A; A=50-361.
DR PDB; 4CY5; X-ray; 2.30 A; A=50-361.
DR PDBsum; 4CY3; -.
DR PDBsum; 4CY5; -.
DR AlphaFoldDB; Q9V3J8; -.
DR SMR; Q9V3J8; -.
DR BioGRID; 72718; 29.
DR ELM; Q9V3J8; -.
DR IntAct; Q9V3J8; 9.
DR MINT; Q9V3J8; -.
DR STRING; 7227.FBpp0300790; -.
DR PaxDb; Q9V3J8; -.
DR PRIDE; Q9V3J8; -.
DR DNASU; 53428; -.
DR EnsemblMetazoa; FBtr0070438; FBpp0070422; FBgn0040066.
DR EnsemblMetazoa; FBtr0308566; FBpp0300790; FBgn0040066.
DR GeneID; 53428; -.
DR KEGG; dme:Dmel_CG17437; -.
DR CTD; 53428; -.
DR FlyBase; FBgn0040066; wds.
DR VEuPathDB; VectorBase:FBgn0040066; -.
DR eggNOG; KOG0266; Eukaryota.
DR GeneTree; ENSGT00940000154143; -.
DR HOGENOM; CLU_000288_57_1_1; -.
DR InParanoid; Q9V3J8; -.
DR OMA; RLWNYHT; -.
DR OrthoDB; 957291at2759; -.
DR PhylomeDB; Q9V3J8; -.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-8951664; Neddylation.
DR SignaLink; Q9V3J8; -.
DR BioGRID-ORCS; 53428; 1 hit in 3 CRISPR screens.
DR ChiTaRS; wds; fly.
DR GenomeRNAi; 53428; -.
DR PRO; PR:Q9V3J8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0040066; Expressed in ovary and 16 other tissues.
DR ExpressionAtlas; Q9V3J8; baseline and differential.
DR Genevisible; Q9V3J8; DM.
DR GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR GO; GO:0044665; C:MLL1/2 complex; ISS:FlyBase.
DR GO; GO:0044666; C:MLL3/4 complex; IDA:FlyBase.
DR GO; GO:0044545; C:NSL complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0001654; P:eye development; IGI:UniProtKB.
DR GO; GO:0007482; P:haltere development; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
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 Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..361
FT /note="Protein will die slowly"
FT /id="PRO_0000051433"
FT REPEAT 62..100
FT /note="WD 1"
FT REPEAT 104..142
FT /note="WD 2"
FT REPEAT 146..184
FT /note="WD 3"
FT REPEAT 188..226
FT /note="WD 4"
FT REPEAT 230..269
FT /note="WD 5"
FT REPEAT 273..314
FT /note="WD 6"
FT REPEAT 318..358
FT /note="WD 7"
FT REGION 7..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:4CY3"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4CY3"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4CY3"
SQ SEQUENCE 361 AA; 39041 MW; B2A64127F1E0292D CRC64;
MVPIGAVHGG HPGVVHPPQQ PLPTAPSGPN SLQPNSVGQP GATTSSNSSA SNKSSLSVKP
NYTLKFTLAG HTKAVSAVKF SPNGEWLASS SADKLIKIWG AYDGKFEKTI SGHKLGISDV
AWSSDSRLLV SGSDDKTLKV WELSTGKSLK TLKGHSNYVF CCNFNPQSNL IVSGSFDESV
RIWDVRTGKC LKTLPAHSDP VSAVHFNRDG SLIVSSSYDG LCRIWDTASG QCLKTLIDDD
NPPVSFVKFS PNGKYILAAT LDNTLKLWDY SKGKCLKTYT GHKNEKYCIF ANFSVTGGKW
IVSGSEDNMV YIWNLQSKEV VQKLQGHTDT VLCTACHPTE NIIASAALEN DKTIKLWKSD
T
