VLS_DROME
ID VLS_DROME Reviewed; 367 AA.
AC Q9VIP8; Q95SA0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein valois;
DE AltName: Full=MEP50 homolog;
GN Name=vls; Synonyms=vsl; ORFNames=CG10728;
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 [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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary, and Testis;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15634703; DOI=10.1242/dev.01590;
RA Cavey M., Hijal S., Zhang X., Suter B.;
RT "Drosophila valois encodes a divergent WD protein that is required for Vasa
RT localization and Oskar protein accumulation.";
RL Development 132:459-468(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH CSUL AND TUD.
RX PubMed=15800004; DOI=10.1242/dev.01809;
RA Anne J., Mechler B.M.;
RT "Valois, a component of the nuage and pole plasm, is involved in assembly
RT of these structures, and binds to Tudor and the methyltransferase
RT Capsuleen.";
RL Development 132:2167-2177(2005).
CC -!- FUNCTION: Involved in specific localization of cytoplasmic proteins
CC during the formation of pole plasm. Required for synthesis and/or
CC stability of oskar protein (osk) and localization of tudor (tud) in
CC both the nuage and posterior pole of the oocyte. Required for normal
CC posterior localization of osk in later stages of oogenesis and for
CC posterior localization of the vasa (vas) protein during the entire
CC process of pole plasm assembly. May act by regulating the complex that
CC contains the arginine N-methyltransferase csul.
CC {ECO:0000269|PubMed:15634703, ECO:0000269|PubMed:15800004}.
CC -!- SUBUNIT: Interacts with csul and tud. {ECO:0000269|PubMed:15800004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15634703,
CC ECO:0000269|PubMed:15800004}.
CC -!- TISSUE SPECIFICITY: In oocytes, localizes to pole plasm and nuage (at
CC protein level). Expressed stronger in the germline than in somatic
CC cells. In the germarium it sometimes concentrates in perinuclear
CC aggregates that disappear by stage 2 of oogenesis. At later stages, it
CC is uniformly distributed in the nurse cells and oocyte, as well as in
CC young embryos, with no particular enrichment at the posterior or inside
CC the pole cells (at protein level). {ECO:0000269|PubMed:15634703,
CC ECO:0000269|PubMed:15800004}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Abundant in ovaries, early embryos and adult females, but reduced in
CC adult males. {ECO:0000269|PubMed:15634703,
CC ECO:0000269|PubMed:15800004}.
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DR EMBL; AE014134; AAF53868.1; -; Genomic_DNA.
DR EMBL; AY060895; AAL28443.1; -; mRNA.
DR EMBL; AY094647; AAM11000.1; -; mRNA.
DR RefSeq; NP_610019.2; NM_136175.5.
DR AlphaFoldDB; Q9VIP8; -.
DR SMR; Q9VIP8; -.
DR BioGRID; 61260; 5.
DR IntAct; Q9VIP8; 1.
DR STRING; 7227.FBpp0080879; -.
DR PaxDb; Q9VIP8; -.
DR PRIDE; Q9VIP8; -.
DR DNASU; 35289; -.
DR EnsemblMetazoa; FBtr0081347; FBpp0080879; FBgn0003978.
DR GeneID; 35289; -.
DR KEGG; dme:Dmel_CG10728; -.
DR UCSC; CG10728-RA; d. melanogaster.
DR CTD; 35289; -.
DR FlyBase; FBgn0003978; vls.
DR VEuPathDB; VectorBase:FBgn0003978; -.
DR eggNOG; KOG0284; Eukaryota.
DR HOGENOM; CLU_064378_0_0_1; -.
DR InParanoid; Q9VIP8; -.
DR OMA; FALATNH; -.
DR OrthoDB; 774546at2759; -.
DR PhylomeDB; Q9VIP8; -.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR SignaLink; Q9VIP8; -.
DR BioGRID-ORCS; 35289; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35289; -.
DR PRO; PR:Q9VIP8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003978; Expressed in wing disc and 52 other tissues.
DR ExpressionAtlas; Q9VIP8; baseline and differential.
DR Genevisible; Q9VIP8; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0034709; C:methylosome; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0045495; C:pole plasm; IDA:FlyBase.
DR GO; GO:0007349; P:cellularization; HMP:FlyBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0007309; P:oocyte axis specification; IBA:GO_Central.
DR GO; GO:0007315; P:pole plasm assembly; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
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 SMART; SM00320; WD40; 2.
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 Cytoplasm; Developmental protein; Differentiation; Oogenesis;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..367
FT /note="Protein valois"
FT /id="PRO_0000051332"
FT REPEAT 101..139
FT /note="WD 1"
FT REPEAT 152..192
FT /note="WD 2"
FT REPEAT 198..238
FT /note="WD 3"
FT REGION 309..367
FT /note="Interaction with csul"
FT CONFLICT 179
FT /note="L -> I (in Ref. 3; AAL28443/AAM11000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40608 MW; 320DDF4437B99517 CRC64;
MFPQRSSELY RTPVTHQPPP ALELAGNLEY PNLNIADLNA RLENLSPRLH DCWDSIAIND
HNHLALATNR REGRQWWGML FGYGRDQMHH MSVDSANFKL QAEHTVNIVR YAEDDFLLVA
LGDTRLQAWS TYSKVRDSQS PYCLFLVGES SAHPTPISQL SVFKADPRTA VSGSADSTLN
VWDLSGADMV STYRSRSSHT DKLTGLATPA ASVDKFVTCD RGGCARLWDV RAAAPSSTCL
YADASHVLSF TSAAWAAASE LQGDNHIYLG DYDGKVHTLD IRVPRKLAET REYFDKGHVA
QLLINGPHLA AMSNLPASVK VANVQAGHEF IYTHQDTHSR LTDAVWTDDS TLITIGHGRK
MVTHAIK
