EXU_DROME
ID EXU_DROME Reviewed; 532 AA.
AC P28750; A4UZR1; Q9V967;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Maternal protein exuperantia;
GN Name=exu; ORFNames=CG8994;
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], AND MUTAGENESIS OF ARG-339.
RX PubMed=1756733; DOI=10.1002/j.1460-2075.1991.tb05004.x;
RA Marcey D., Watkins W.S., Hazelrigg T.;
RT "The temporal and spatial distribution pattern of maternal exuperantia
RT protein: evidence for a role in establishment but not maintenance of bicoid
RT mRNA localization.";
RL EMBO J. 10:4259-4266(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1752438; DOI=10.1101/gad.5.12b.2455;
RA Macdonald P.M., Luk S.K.-S., Kilpatrick M.;
RT "Protein encoded by the exuperantia gene is concentrated at sites of bicoid
RT mRNA accumulation in Drosophila nurse cells but not in oocytes or
RT embryos.";
RL Genes Dev. 5:2455-2466(1991).
RN [3]
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 [4]
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 [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 IN COMPLEX WITH ME31B; EXU AND YPS, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=11546740; DOI=10.1242/dev.128.17.3233;
RA Nakamura A., Amikura R., Hanyu K., Kobayashi S.;
RT "Me31B silences translation of oocyte-localizing RNAs through the formation
RT of cytoplasmic RNP complex during Drosophila oogenesis.";
RL Development 128:3233-3242(2001).
RN [7]
RP IDENTIFICATION IN THE OSK RNP COMPLEX.
RX PubMed=10662770; DOI=10.1083/jcb.148.3.427;
RA Wilhelm J.E., Mansfield J., Hom-Booher N., Wang S., Turck C.W.,
RA Hazelrigg T., Vale R.D.;
RT "Isolation of a ribonucleoprotein complex involved in mRNA localization in
RT Drosophila oocytes.";
RL J. Cell Biol. 148:427-440(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Ensures the proper localization of the mRNA of the bicoid
CC gene to the anterior regions of the oocyte thus playing a fundamental
CC role in the establishment of the polarity of the oocyte. May bind the
CC bcd mRNA.
CC -!- SUBUNIT: Component of the osk RNP complex, which is composed of at
CC least exuperantia (exu), ypsilon schachtel (yps), aret (bruno), cup,
CC and the mRNA of osk (PubMed:10662770). In the sponge body, forms a
CC ribonucleoprotein complex (RNP) containing at least me31B, exu, yps and
CC the mRNA of osk; interactions with exu and yps are RNA dependent
CC (PubMed:11546740). {ECO:0000269|PubMed:10662770,
CC ECO:0000269|PubMed:11546740}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000269|PubMed:11546740}.
CC -!- DEVELOPMENTAL STAGE: Expressed in stage 6 egg chambers.
CC {ECO:0000269|PubMed:11546740}.
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DR EMBL; S72757; AAB20673.1; -; Genomic_DNA.
DR EMBL; S72363; AAB20670.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57429.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57430.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68399.1; -; Genomic_DNA.
DR EMBL; AY051739; AAK93163.1; -; mRNA.
DR PIR; S18643; S18643.
DR RefSeq; NP_001163218.1; NM_001169747.2.
DR RefSeq; NP_725995.1; NM_166410.3.
DR RefSeq; NP_725996.1; NM_166411.3.
DR RefSeq; NP_725997.1; NM_166412.3.
DR PDB; 5L7Z; X-ray; 2.37 A; A=1-333.
DR PDB; 5L80; X-ray; 2.80 A; A/B=1-197, A/B=256-406.
DR PDBsum; 5L7Z; -.
DR PDBsum; 5L80; -.
DR AlphaFoldDB; P28750; -.
DR SMR; P28750; -.
DR BioGRID; 62994; 23.
DR DIP; DIP-21145N; -.
DR IntAct; P28750; 8.
DR MINT; P28750; -.
DR STRING; 7227.FBpp0291491; -.
DR iPTMnet; P28750; -.
DR PaxDb; P28750; -.
DR PRIDE; P28750; -.
DR DNASU; 37345; -.
DR EnsemblMetazoa; FBtr0086242; FBpp0085555; FBgn0000615.
DR EnsemblMetazoa; FBtr0086243; FBpp0085556; FBgn0000615.
DR EnsemblMetazoa; FBtr0086244; FBpp0085557; FBgn0000615.
DR EnsemblMetazoa; FBtr0302285; FBpp0291491; FBgn0000615.
DR GeneID; 37345; -.
DR KEGG; dme:Dmel_CG8994; -.
DR UCSC; CG8994-RA; d. melanogaster.
DR CTD; 37345; -.
DR FlyBase; FBgn0000615; exu.
DR VEuPathDB; VectorBase:FBgn0000615; -.
DR eggNOG; ENOG502QVAD; Eukaryota.
DR HOGENOM; CLU_034404_1_0_1; -.
DR InParanoid; P28750; -.
DR OMA; FLNWLEM; -.
DR OrthoDB; 744143at2759; -.
DR PhylomeDB; P28750; -.
DR SignaLink; P28750; -.
DR BioGRID-ORCS; 37345; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37345; -.
DR PRO; PR:P28750; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000615; Expressed in testis and 24 other tissues.
DR ExpressionAtlas; P28750; baseline and differential.
DR Genevisible; P28750; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:FlyBase.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IGI:FlyBase.
DR GO; GO:0045450; P:bicoid mRNA localization; IMP:UniProtKB.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; HMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; TAS:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IGI:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; TAS:FlyBase.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR037998; Exu.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR040941; SAM_Exu.
DR PANTHER; PTHR12384; PTHR12384; 1.
DR Pfam; PF18609; SAM_Exu; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..532
FT /note="Maternal protein exuperantia"
FT /id="PRO_0000087145"
FT REGION 206..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 223
FT /note="M -> I"
FT MUTAGEN 339
FT /note="R->S: In PJ42 mutant; loss of exu function in
FT female."
FT /evidence="ECO:0000269|PubMed:1756733"
FT CONFLICT 176
FT /note="K -> Q (in Ref. 1; AAB20673)"
FT /evidence="ECO:0000305"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5L7Z"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5L80"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 261..277
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5L7Z"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5L7Z"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:5L7Z"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:5L80"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:5L80"
FT HELIX 336..351
FT /evidence="ECO:0007829|PDB:5L80"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:5L80"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:5L80"
FT HELIX 383..394
FT /evidence="ECO:0007829|PDB:5L80"
SQ SEQUENCE 532 AA; 57975 MW; 50BD15B712A62C4E CRC64;
MVADNIDAGV AIAVADQSSS PVGDKVELPA GNYILVGVDI DTTGRRLMDE IVQLAAYTPT
DHFEQYIMPY MNLNPAARQR HQVRVISIGF YRMLKSMQTY KIIKSKSEIA ALKDFLNWLE
QLKTKAGPSS DGIVLIYHEE RKFIPYMILE SLKKYGLLER FTASVKSFAN SINLAKASIG
DANIKNYSLR KLSKILSTTK EEDAACSAST SGSGSGLGSG SSMVSDSVSI SPRDSTVTNG
DDKQSSKNAV QGKRELFDGN ASVRAKLAFD VALQLSNSDG KPEPKSSEAL ENMFNAIRPF
AKLVVSDVLE LDIQIENLER QNSFRPVFLN YFKTTLYHRV RAVKFRIVLA ENGFDLNTLS
AIWAEKNIEG LDIALQSIGR LKSKDKAELL ELLDSYFDPK KTTVKPVVKG NSNNNNNYRR
RNRRGGRQSV KDARPSSSPS ASTEFGAGGD KSRSVSSLPD STTKTPSPNK PRMHRKRNSR
QSLGATPNGL KVAAEISSSG VSELNNSAPP AVTISPVVAQ PSPTPVAITA SN
