ID WDR82_DROME Reviewed; 317 AA.
AC Q9VLN1;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=WD repeat-containing protein 82 {ECO:0000250|UniProtKB:Q6UXN9};
GN Name=Wdr82 {ECO:0000303|PubMed:26577379, ECO:0000312|FlyBase:FBgn0032030};
GN ORFNames=CG17293;
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] {ECO:0000312|EMBL:AAF52654.1}
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 [2] {ECO:0000312|EMBL:AAF52654.1}
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 [3] {ECO:0000312|EMBL:AAL39226.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, 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 [5] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN THE SET1 COMPLEX.
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 [6]
RP INTERACTION WITH MSL COMPLEX.
RX PubMed=23295261; DOI=10.1038/nsmb.2477;
RA Wang C.I., Alekseyenko A.A., LeRoy G., Elia A.E., Gorchakov A.A.,
RA Britton L.M., Elledge S.J., Kharchenko P.V., Garcia B.A., Kuroda M.I.;
RT "Chromatin proteins captured by ChIP-mass spectrometry are linked to dosage
RT compensation in Drosophila.";
RL Nat. Struct. Mol. Biol. 20:202-209(2013).
RN [7]
RP FUNCTION, AND INTERACTION WITH SU(SABLE).
RX PubMed=26577379; DOI=10.1261/rna.048819.114;
RA Brewer-Jensen P., Wilson C.B., Abernethy J., Mollison L., Card S.,
RA Searles L.L.;
RT "Suppressor of sable [Su(s)] and Wdr82 down-regulate RNA from heat-shock-
RT inducible repetitive elements by a mechanism that involves transcription
RT termination.";
RL RNA 22:139-154(2016).
CC -!- FUNCTION: Component of the SET1 complex that specifically di- and
CC trimethylates 'Lys-4' of histone H3 (PubMed:21694722, PubMed:21875999).
CC Together with su(sable), part of a transcription termination checkpoint
CC that promotes transcription termination of aberrant RNAs and their
CC subsequent degradation by the nuclear exosome (PubMed:26577379).
CC {ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999,
CC ECO:0000269|PubMed:26577379}.
CC -!- SUBUNIT: 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, PubMed:21875999). Interacts with male-
CC specific lethal (MSL) histone acetyltransferase complex at least
CC composed of mof, msl-1, msl-2 and msl-3 (PubMed:23295261). Interacts
CC with su(sable) (PubMed:26577379). {ECO:0000269|PubMed:21694722,
CC ECO:0000269|PubMed:21875999, ECO:0000269|PubMed:23295261,
CC ECO:0000269|PubMed:26577379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21694722}.
CC -!- SIMILARITY: Belongs to the WD repeat SWD2 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014134; AAF52654.1; -; Genomic_DNA.
DR EMBL; AY069081; AAL39226.1; -; mRNA.
DR RefSeq; NP_609217.1; NM_135373.3.
DR AlphaFoldDB; Q9VLN1; -.
DR SMR; Q9VLN1; -.
DR BioGRID; 60277; 28.
DR ComplexPortal; CPX-2798; COMPASS complex.
DR IntAct; Q9VLN1; 4.
DR STRING; 7227.FBpp0079266; -.
DR PaxDb; 7227-FBpp0079266; -.
DR DNASU; 34153; -.
DR EnsemblMetazoa; FBtr0079650; FBpp0079266; FBgn0032030.
DR GeneID; 34153; -.
DR KEGG; dme:Dmel_CG17293; -.
DR UCSC; CG17293-RA; d. melanogaster.
DR AGR; FB:FBgn0032030; -.
DR CTD; 80335; -.
DR FlyBase; FBgn0032030; Wdr82.
DR VEuPathDB; VectorBase:FBgn0032030; -.
DR eggNOG; KOG1446; Eukaryota.
DR GeneTree; ENSGT00530000063965; -.
DR HOGENOM; CLU_044117_0_0_1; -.
DR InParanoid; Q9VLN1; -.
DR OMA; HNEGYIR; -.
DR OrthoDB; 176818at2759; -.
DR PhylomeDB; Q9VLN1; -.
DR Reactome; R-DME-9772755; Formation of WDR5-containing histone-modifying complexes.
DR BioGRID-ORCS; 34153; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34153; -.
DR PRO; PR:Q9VLN1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032030; Expressed in eye disc (Drosophila) and 27 other cell types or tissues.
DR Genevisible; Q9VLN1; DM.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-KW.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0071027; P:nuclear RNA surveillance; IDA:UniProtKB.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037867; Swd2/WDR82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19861:SF0; WD REPEAT-CONTAINING PROTEIN 82; 1.
DR PANTHER; PTHR19861; WD40 REPEAT PROTEIN SWD2; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transcription termination; WD repeat.
FT CHAIN 1..317
FT /note="WD repeat-containing protein 82"
FT /id="PRO_0000429380"
FT REPEAT 21..60
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 107..146
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 148..186
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 194..233
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 238..278
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 282..317
FT /note="WD 6"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 35355 MW; FAE08A606ED23CAD CRC64;
MKIKLIDSVV RSFKVAKIFR ENTDKINAID FAPNGEHLIS CSEDDQIVIY DCEKGTQSRT
VNSKKYGVDL IHFTHANNTA IHSSTKVDDT IRYLSLHDNK YLRYFPGHTK KVISLCISPV
EDTFLSGSLD KTLRLWDLRS PNCQGLMHLS GRPIAAYDPE GLIFAAGVNS ESIKLYDLRS
FDKGPFVTFK LNQEKECDWT GLKFSRDGKT ILISTNGSVI RLVDAFHGTP LQTFTGYPNN
KGIPIEASFS PDSQFIFSGS TDGRVHIWNA DTGNKVSVLN GDHPGPVQCV QFNPKYMMLA
SACTNMAFWL PTSEEGL
//
