AUB_DROME
ID AUB_DROME Reviewed; 866 AA.
AC O76922; A8DYZ0; K7WQ34; K7X543; K7XHY9; L0CPY1; L0CQ70; L0CRA0; L0CRA6;
AC L0CRP1; L0CRZ4; L0CS00;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein aubergine {ECO:0000312|EMBL:AGA18944.1};
DE AltName: Full=Protein sting {ECO:0000312|EMBL:AAD38655.1};
GN Name=aub; ORFNames=CG6137;
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:CAA64320.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S {ECO:0000312|EMBL:CAA64320.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:CAA64320.1};
RX PubMed=8676882; DOI=10.1007/bf02172530;
RA Schmidt A., Hollmann M., Schaefer U.;
RT "A newly identified Minute locus, M(2)32D, encodes the ribosomal protein L9
RT in Drosophila melanogaster.";
RL Mol. Gen. Genet. 251:381-387(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA64320.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S {ECO:0000312|EMBL:CAA64320.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:CAA64320.1};
RX PubMed=9927466; DOI=10.1093/genetics/151.2.749;
RA Schmidt A., Palumbo G., Bozzetti M.P., Tritto P., Pimpinelli S.,
RA Schafer U.;
RT "Genetic and molecular characterization of sting, a gene involved in
RT crystal formation and meiotic drive in the male germ line of Drosophila
RT melanogaster.";
RL Genetics 151:749-760(1999).
RN [3] {ECO:0000312|EMBL:AGA18944.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3846 {ECO:0000312|EMBL:AGA18946.1},
RC 3852 {ECO:0000312|EMBL:AGA18942.1}, 3853 {ECO:0000312|EMBL:AGA18945.1},
RC 3854 {ECO:0000312|EMBL:AGA18941.1}, 3892 {ECO:0000312|EMBL:AGA18940.1},
RC 3893 {ECO:0000312|EMBL:AGA18943.1}, and 3895 {ECO:0000312|EMBL:AGA18939.1};
RX PubMed=22997235; DOI=10.1534/genetics.112.145714;
RA Lee Y.C., Langley C.H.;
RT "Long-term and short-term evolutionary impacts of transposable elements on
RT Drosophila.";
RL Genetics 192:1411-1432(2012).
RN [4] {ECO:0000312|EMBL:AAF53046.1}
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 [5] {ECO:0000312|EMBL:AAF53046.1}
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 [6] {ECO:0000305, ECO:0000312|EMBL:AAD38655.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [7] {ECO:0000312|EMBL:AFX62835.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-847.
RA Fablet M., Akkouche A., Braman V., Vieira C.;
RT "Variability in the piRNA pathway induces a variable load of transposable
RT elements in wild type strains of Drosophila simulans.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1783295; DOI=10.1093/genetics/129.4.1119;
RA Schupbach T., Wieschaus E.;
RT "Female sterile mutations on the second chromosome of Drosophila
RT melanogaster. II. Mutations blocking oogenesis or altering egg
RT morphology.";
RL Genetics 129:1119-1136(1991).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8625849; DOI=10.1242/dev.122.5.1631;
RA Wilson J.E., Connell J.E., Macdonald P.M.;
RT "aubergine enhances oskar translation in the Drosophila ovary.";
RL Development 122:1631-1639(1996).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11526087; DOI=10.1242/dev.128.14.2823;
RA Harris A.N., Macdonald P.M.;
RT "Aubergine encodes a Drosophila polar granule component required for pole
RT cell formation and related to eIF2C.";
RL Development 128:2823-2832(2001).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=12154120; DOI=10.1101/gad.990802;
RA Kennerdell J.R., Yamaguchi S., Carthew R.W.;
RT "RNAi is activated during Drosophila oocyte maturation in a manner
RT dependent on aubergine and spindle-E.";
RL Genes Dev. 16:1884-1889(2002).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=12538514; DOI=10.1242/dev.00310;
RA Findley S.D., Tamanaha M., Clegg N.J., Ruohola-Baker H.;
RT "Maelstrom, a Drosophila spindle-class gene, encodes a protein that
RT colocalizes with Vasa and RDE1/AGO1 homolog, Aubergine, in nuage.";
RL Development 130:859-871(2003).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=15035984; DOI=10.1016/s0092-8674(04)00250-8;
RA Cook H.A., Koppetsch B.S., Wu J., Theurkauf W.E.;
RT "The Drosophila SDE3 homolog armitage is required for oskar mRNA silencing
RT and embryonic axis specification.";
RL Cell 116:817-829(2004).
RN [14] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15090597; DOI=10.1242/jcs.01059;
RA Snee M.J., Macdonald P.M.;
RT "Live imaging of nuage and polar granules: evidence against a precursor-
RT product relationship and a novel role for Oskar in stabilization of polar
RT granule components.";
RL J. Cell Sci. 117:2109-2120(2004).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=15372228; DOI=10.1007/s00438-004-1061-1;
RA Reiss D., Josse T., Anxolabehere D., Ronsseray S.;
RT "aubergine mutations in Drosophila melanogaster impair P cytotype
RT determination by telomeric P elements inserted in heterochromatin.";
RL Mol. Genet. Genomics 272:336-343(2004).
RN [16] {ECO:0000305}
RP FUNCTION.
RX PubMed=14752161; DOI=10.1126/science.1092653;
RA Pal-Bhadra M., Leibovitch B.A., Gandhi S.G., Rao M., Bhadra U.,
RA Birchler J.A., Elgin S.C.R.;
RT "Heterochromatic silencing and HP1 localization in Drosophila are dependent
RT on the RNAi machinery.";
RL Science 303:669-672(2004).
RN [17] {ECO:0000305}
RP FUNCTION.
RX PubMed=16452506; DOI=10.1101/gad.370206;
RA Savitsky M., Kwon D., Georgiev P., Kalmykova A., Gvozdev V.;
RT "Telomere elongation is under the control of the RNAi-based mechanism in
RT the Drosophila germline.";
RL Genes Dev. 20:345-354(2006).
RN [18] {ECO:0000305}
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17346786; DOI=10.1016/j.cell.2007.01.043;
RA Brennecke J., Aravin A.A., Stark A., Dus M., Kellis M., Sachidanandam R.,
RA Hannon G.J.;
RT "Discrete small RNA-generating loci as master regulators of transposon
RT activity in Drosophila.";
RL Cell 128:1089-1103(2007).
RN [19] {ECO:0000305}
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17872506; DOI=10.1261/rna.744307;
RA Nishida K.M., Saito K., Mori T., Kawamura Y., Nagami-Okada T., Inagaki S.,
RA Siomi H., Siomi M.C.;
RT "Gene silencing mechanisms mediated by Aubergine piRNA complexes in
RT Drosophila male gonad.";
RL RNA 13:1911-1922(2007).
RN [20] {ECO:0000305}
RP FUNCTION, AND RNA-BINDING.
RX PubMed=17322028; DOI=10.1126/science.1140494;
RA Gunawardane L.S., Saito K., Nishida K.M., Miyoshi K., Kawamura Y.,
RA Nagami T., Siomi H., Siomi M.C.;
RT "A slicer-mediated mechanism for repeat-associated siRNA 5' end formation
RT in Drosophila.";
RL Science 315:1587-1590(2007).
RN [21] {ECO:0000305}
RP FUNCTION, INTERACTION WITH VAS AND TUD, AND SUBCELLULAR LOCATION.
RX PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
RA Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
RT "Isolation of new polar granule components in Drosophila reveals P body and
RT ER associated proteins.";
RL Mech. Dev. 125:865-873(2008).
RN [22] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=19395009; DOI=10.1016/j.cell.2009.04.027;
RA Li C., Vagin V.V., Lee S., Xu J., Ma S., Xi H., Seitz H., Horwich M.D.,
RA Syrzycka M., Honda B.M., Kittler E.L., Zapp M.L., Klattenhoff C.,
RA Schulz N., Theurkauf W.E., Weng Z., Zamore P.D.;
RT "Collapse of germline piRNAs in the absence of Argonaute3 reveals somatic
RT piRNAs in flies.";
RL Cell 137:509-521(2009).
RN [23] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, RNA-BINDING, INTERACTION
RP WITH TUD AND AGO3, ACETYLATION AT MET-1, AND METHYLATION AT ARG-11; ARG-13
RP AND ARG-15.
RX PubMed=19959991; DOI=10.1038/emboj.2009.365;
RA Nishida K.M., Okada T.N., Kawamura T., Mituyama T., Kawamura Y.,
RA Inagaki S., Huang H., Chen D., Kodama T., Siomi H., Siomi M.C.;
RT "Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway
RT in Drosophila germlines.";
RL EMBO J. 28:3820-3831(2009).
RN [24] {ECO:0000305}
RP RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, METHYLATION, AND
RP MUTAGENESIS OF 11-ARG--ARG-17.
RX PubMed=19377467; DOI=10.1038/ncb1872;
RA Kirino Y., Kim N., de Planell-Saguer M., Khandros E., Chiorean S.,
RA Klein P.S., Rigoutsos I., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for
RT Ago3 and Aub stability.";
RL Nat. Cell Biol. 11:652-658(2009).
RN [25] {ECO:0000305}
RP FUNCTION, RNA-BINDING, INTERACTION WITH SMG; TWIN AND AGO3, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20953170; DOI=10.1038/nature09465;
RA Rouget C., Papin C., Boureux A., Meunier A.C., Franco B., Robine N.,
RA Lai E.C., Pelisson A., Simonelig M.;
RT "Maternal mRNA deadenylation and decay by the piRNA pathway in the early
RT Drosophila embryo.";
RL Nature 467:1128-1132(2010).
RN [26] {ECO:0000305}
RP INTERACTION WITH TUD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP METHYLATION, AND MUTAGENESIS OF 11-ARG--ARG-17.
RX PubMed=19926723; DOI=10.1261/rna.1869710;
RA Kirino Y., Vourekas A., Sayed N., de Lima Alves F., Thomson T., Lasko P.,
RA Rappsilber J., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Aubergine mediates Tudor binding and germ plasm
RT localization.";
RL RNA 16:70-78(2010).
RN [27] {ECO:0000305}
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20980675; DOI=10.1261/rna.2270710;
RA Nagao A., Mituyama T., Huang H., Chen D., Siomi M.C., Siomi H.;
RT "Biogenesis pathways of piRNAs loaded onto AGO3 in the Drosophila testis.";
RL RNA 16:2503-2515(2010).
RN [28] {ECO:0000305}
RP INTERACTION WITH PAPI, AND SUBCELLULAR LOCATION.
RX PubMed=21447556; DOI=10.1242/dev.059287;
RA Liu L., Qi H., Wang J., Lin H.;
RT "PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in
RT the nuage to silence transposition.";
RL Development 138:1863-1873(2011).
RN [29]
RP INTERACTION WITH VRET.
RX PubMed=21831924; DOI=10.1242/dev.069187;
RA Zamparini A.L., Davis M.Y., Malone C.D., Vieira E., Zavadil J.,
RA Sachidanandam R., Hannon G.J., Lehmann R.;
RT "Vreteno, a gonad-specific protein, is essential for germline development
RT and primary piRNA biogenesis in Drosophila.";
RL Development 138:4039-4050(2011).
RN [30] {ECO:0000305}
RP FUNCTION, RNA-BINDING, AND INTERACTION WITH RUMP.
RX PubMed=20937269; DOI=10.1016/j.ydbio.2010.10.002;
RA Becalska A.N., Kim Y.R., Belletier N.G., Lerit D.A., Sinsimer K.S.,
RA Gavis E.R.;
RT "Aubergine is a component of a nanos mRNA localization complex.";
RL Dev. Biol. 349:46-52(2011).
RN [31] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLU-721.
RX PubMed=23267055; DOI=10.1534/genetics.112.147561;
RA Gell S.L., Reenan R.A.;
RT "Mutations to the piRNA pathway component Aubergine enhance meiotic drive
RT of segregation distorter in Drosophila melanogaster.";
RL Genetics 193:771-784(2013).
RN [32] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23559253; DOI=10.1126/science.1231965;
RA Perrat P.N., DasGupta S., Wang J., Theurkauf W., Weng Z., Rosbash M.,
RA Waddell S.;
RT "Transposition-driven genomic heterogeneity in the Drosophila brain.";
RL Science 340:91-95(2013).
RN [33]
RP INTERACTION WITH ME31B.
RX PubMed=28945271; DOI=10.1002/1873-3468.12854;
RA DeHaan H., McCambridge A., Armstrong B., Cruse C., Solanki D.,
RA Trinidad J.C., Arkov A.L., Gao M.;
RT "An in vivo proteomic analysis of the Me31B interactome in Drosophila germ
RT granules.";
RL FEBS Lett. 591:3536-3547(2017).
RN [34] {ECO:0000305, ECO:0000312|PDB:3NTI}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-18 IN COMPLEX WITH TUD,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND METHYLATION AT ARG-11; ARG-13
RP AND ARG-15.
RX PubMed=20713507; DOI=10.1101/gad.1956010;
RA Liu H., Wang J.Y., Huang Y., Li Z., Gong W., Lehmann R., Xu R.M.;
RT "Structural basis for methylarginine-dependent recognition of Aubergine by
RT Tudor.";
RL Genes Dev. 24:1876-1881(2010).
CC -!- FUNCTION: Acts via the piwi-interacting RNA (piRNA) metabolic process,
CC which mediates the repression of transposable elements during meiosis
CC by forming complexes composed of piRNAs and Piwi proteins and governs
CC the methylation and subsequent repression of transposons. Directly
CC binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by
CC a Dicer-independent mechanism and are primarily derived from
CC transposons and other repeated sequence elements. In ovary, associates
CC predominantly with antisense piRNAs that contain uridine at their 5'
CC end. In testis, associates with Su(Ste) antisense piRNAs (most abundant
CC class of piRNAs found in complex with aub in testes) and negatively
CC regulates Ste expression, most likely by cleaving its transcripts. Also
CC in testis, may repress translation of vas when associated with a piRNA
CC derived from chromosome X, termed AT-chX-1, whose sequence shows strong
CC complementarity to vas mRNA. Aub-piRNA complexes from ovary and testis
CC possess RNA cleavage activity. Involved in telomere regulation by
CC repressing specialized telomeric retroelements HeT-A and TART;
CC Drosophila telomeres being maintained by transposition of specialized
CC telomeric retroelements. Also involved in telomeric trans-silencing, a
CC repression mechanism by which a transposon or a transgene inserted in
CC subtelomeric heterochromatin has the capacity to repress in trans, in
CC the female germline, a homologous transposon, or transgene located in
CC euchromatin. Involved in the suppression of meiotic drive of sex
CC chromosomes and autosomes. Involved in transposon silencing in the
CC adult brain. Required for dorsal-ventral as well as anterior-posterior
CC patterning of the egg. Required during oogenesis for primordial germ
CC cell formation and activation of RNA interference. During early
CC oogenesis, required for osk mRNA silencing and polarization of the
CC microtubule cytoskeleton. During mid-oogenesis, required for osk mRNA
CC localization to the posterior pole and efficient translation of osk and
CC grk. During embryogenesis, required for posterior localization of nos
CC mRNA, independently of osk, and pole cell formation. Essential for the
CC formation and/or structural integrity of perinuclear nuage particles.
CC Required for the localization of Mael to the meiotic nuage. Forms a
CC complex with smg, twin, AGO3 and specific piRNAs that targets nos mRNA
CC (and probably other maternal mRNAS) for deadenylation promoting its
CC decay during early embryogenesis. {ECO:0000269|PubMed:11526087,
CC ECO:0000269|PubMed:12154120, ECO:0000269|PubMed:12538514,
CC ECO:0000269|PubMed:14752161, ECO:0000269|PubMed:15035984,
CC ECO:0000269|PubMed:15090597, ECO:0000269|PubMed:15372228,
CC ECO:0000269|PubMed:16452506, ECO:0000269|PubMed:17322028,
CC ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:1783295,
CC ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:18590813,
CC ECO:0000269|PubMed:19959991, ECO:0000269|PubMed:20937269,
CC ECO:0000269|PubMed:20953170, ECO:0000269|PubMed:20980675,
CC ECO:0000269|PubMed:23267055, ECO:0000269|PubMed:23559253,
CC ECO:0000269|PubMed:8625849, ECO:0000269|PubMed:9927466}.
CC -!- SUBUNIT: Interacts with vas and AGO3 (PubMed:18590813,
CC PubMed:19959991). Interacts (when methylated on arginine residues) with
CC tud (PubMed:18590813, PubMed:19926723, PubMed:19959991,
CC PubMed:20713507). Forms a complex with smg, twin, AGO3, nos mRNA and
CC piRNAs that targets the nos 3'-untranslated region, in early embryos
CC (PubMed:20953170). Interacts with nos mRNA and rump (in an RNA-
CC dependent manner) (PubMed:20937269). Interacts with papi and vret
CC (PubMed:21447556, PubMed:21831924). Interacts with me31B
CC (PubMed:28945271). {ECO:0000269|PubMed:18590813,
CC ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:19959991,
CC ECO:0000269|PubMed:20713507, ECO:0000269|PubMed:20937269,
CC ECO:0000269|PubMed:20953170, ECO:0000269|PubMed:21447556,
CC ECO:0000269|PubMed:21831924, ECO:0000269|PubMed:28945271}.
CC -!- INTERACTION:
CC O76922; P25823: tud; NbExp=7; IntAct=EBI-98862, EBI-498741;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11526087,
CC ECO:0000269|PubMed:15090597, ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:19926723,
CC ECO:0000269|PubMed:20713507, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:21447556,
CC ECO:0000269|PubMed:28945271}. Note=Component of the meiotic nuage, also
CC named P granule, a germ-cell-specific organelle required to repress
CC transposon activity during meiosis. In the oocyte and later in the
CC embryo, concentrates at the posterior pole as a component of polar
CC granules. In the cytoplasm of syncytial embryos, accumulates in
CC discrete foci. {ECO:0000269|PubMed:11526087,
CC ECO:0000269|PubMed:15090597, ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:19926723,
CC ECO:0000269|PubMed:20713507, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:21447556,
CC ECO:0000269|PubMed:28945271}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:12537572, ECO:0000269|PubMed:22997235,
CC ECO:0000269|PubMed:8676882, ECO:0000269|PubMed:9927466,
CC ECO:0000269|Ref.7};
CC IsoId=O76922-1; Sequence=Displayed;
CC Name=C {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537572,
CC ECO:0000269|Ref.7};
CC IsoId=O76922-2; Sequence=VSP_047356;
CC -!- TISSUE SPECIFICITY: Expressed in ovary. In the germarium, found in
CC germline stem and cyst cells. In egg chambers from stage 6, expressed
CC both in nurse cells and oocytes. In embryos, accumulates in the pole
CC cells, although low expression is detected throughout the entire
CC embryo. In testis, expressed in germline stem cells, gonialblast and
CC spermatogonia cells (at protein level). In the adult brain, expressed
CC in the ellipsoid body, the mushroom body subdivision in the peduncle
CC and the cell body layer. Expressed specifically in alpha'/beta' and
CC gamma neurons. {ECO:0000269|PubMed:11526087,
CC ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:17872506,
CC ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19926723,
CC ECO:0000269|PubMed:20713507, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:23559253,
CC ECO:0000269|PubMed:9927466}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in oocytes and 0-6 hours old
CC embryos (at protein level). {ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:9927466}.
CC -!- PTM: Symmetrical dimethylation on Arg-11, Arg-13 and/or Arg-15, most
CC likely by csul, is required for binding to tud, localization to the
CC pole plasm and association with the correct piRNAs.
CC {ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19926723,
CC ECO:0000269|PubMed:19959991, ECO:0000269|PubMed:20713507,
CC ECO:0000303|PubMed:19959991}.
CC -!- DISRUPTION PHENOTYPE: Female sterility, consequence of a maternal
CC lethal effect. Approximately 2% of the embryos from aub mutant females
CC are fertilized and secrete a recognizable cuticle, while all of them
CC lack abdominal segments. Male sterility accompanied by production of
CC Ste protein crystals in primary spermatocytes and by meiotic non-
CC disjunction and drive of sex chromosomes and autosomes.
CC {ECO:0000269|PubMed:1783295, ECO:0000269|PubMed:20980675,
CC ECO:0000269|PubMed:8625849, ECO:0000269|PubMed:9927466}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
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; X94613; CAA64320.1; -; Genomic_DNA.
DR EMBL; KC116210; AGA18939.1; -; Genomic_DNA.
DR EMBL; KC116211; AGA18940.1; -; Genomic_DNA.
DR EMBL; KC116212; AGA18941.1; -; Genomic_DNA.
DR EMBL; KC116213; AGA18942.1; -; Genomic_DNA.
DR EMBL; KC116214; AGA18943.1; -; Genomic_DNA.
DR EMBL; KC116215; AGA18944.1; -; Genomic_DNA.
DR EMBL; KC116216; AGA18945.1; -; Genomic_DNA.
DR EMBL; KC116217; AGA18946.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53046.1; -; Genomic_DNA.
DR EMBL; AE014134; ABV53667.1; -; Genomic_DNA.
DR EMBL; AF145680; AAD38655.1; -; mRNA.
DR EMBL; JX656893; AFX62833.1; -; mRNA.
DR EMBL; JX656894; AFX62834.1; -; mRNA.
DR EMBL; JX656895; AFX62835.1; -; mRNA.
DR RefSeq; NP_001097144.1; NM_001103674.3. [O76922-2]
DR RefSeq; NP_476734.1; NM_057386.5. [O76922-1]
DR PDB; 3NTH; X-ray; 2.80 A; C=10-15.
DR PDB; 3NTI; X-ray; 2.80 A; C=6-18.
DR PDB; 7CFD; X-ray; 2.70 A; I/J/K/L/M/N/O/Z=6-18.
DR PDBsum; 3NTH; -.
DR PDBsum; 3NTI; -.
DR PDBsum; 7CFD; -.
DR AlphaFoldDB; O76922; -.
DR SMR; O76922; -.
DR BioGRID; 60589; 73.
DR ComplexPortal; CPX-3181; aubergine-tudor complex.
DR IntAct; O76922; 4.
DR MINT; O76922; -.
DR STRING; 7227.FBpp0079754; -.
DR iPTMnet; O76922; -.
DR PaxDb; O76922; -.
DR PRIDE; O76922; -.
DR EnsemblMetazoa; FBtr0080165; FBpp0079754; FBgn0000146. [O76922-1]
DR EnsemblMetazoa; FBtr0112793; FBpp0111705; FBgn0000146. [O76922-2]
DR GeneID; 34524; -.
DR KEGG; dme:Dmel_CG6137; -.
DR UCSC; CG6137-RA; d. melanogaster. [O76922-1]
DR UCSC; CG6137-RC; d. melanogaster.
DR CTD; 34524; -.
DR FlyBase; FBgn0000146; aub.
DR VEuPathDB; VectorBase:FBgn0000146; -.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR InParanoid; O76922; -.
DR OMA; WYVITPR; -.
DR PhylomeDB; O76922; -.
DR SignaLink; O76922; -.
DR BioGRID-ORCS; 34524; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; O76922; -.
DR GenomeRNAi; 34524; -.
DR PRO; PR:O76922; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000146; Expressed in ovariole (Drosophila) and 17 other tissues.
DR ExpressionAtlas; O76922; baseline and differential.
DR Genevisible; O76922; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:FlyBase.
DR GO; GO:0034584; F:piRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0046594; P:maintenance of pole plasm mRNA location; TAS:FlyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; TAS:FlyBase.
DR GO; GO:0001556; P:oocyte maturation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IDA:ComplexPortal.
DR GO; GO:1903863; P:P granule assembly; IDA:ComplexPortal.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:FlyBase.
DR GO; GO:0007277; P:pole cell development; IDA:ComplexPortal.
DR GO; GO:0007279; P:pole cell formation; IDA:ComplexPortal.
DR GO; GO:0007318; P:pole plasm protein localization; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR GO; GO:0046012; P:positive regulation of oskar mRNA translation; TAS:FlyBase.
DR GO; GO:1900370; P:positive regulation of post-transcriptional gene silencing by RNA; IDA:ComplexPortal.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0046011; P:regulation of oskar mRNA translation; TAS:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0035282; P:segmentation; IGI:FlyBase.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR032474; Argonaute_N.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Methylation; Oogenesis;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..866
FT /note="Protein aubergine"
FT /id="PRO_0000422915"
FT DOMAIN 274..383
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 555..852
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:19959991"
FT MOD_RES 11
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:19959991,
FT ECO:0000269|PubMed:20713507"
FT MOD_RES 13
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:19959991,
FT ECO:0000269|PubMed:20713507"
FT MOD_RES 15
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:19959991,
FT ECO:0000269|PubMed:20713507"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_047356"
FT MUTAGEN 11..17
FT /note="RGRGRGR->KGKGKGK: Abolishes methylation and
FT interaction with tud. Does not affect piRNA binding."
FT /evidence="ECO:0000269|PubMed:19377467,
FT ECO:0000269|PubMed:19926723"
FT MUTAGEN 721
FT /note="E->A: Putative catalytic mutant. Enhances meiotic
FT drive."
FT /evidence="ECO:0000269|PubMed:23267055"
FT CONFLICT 8
FT /note="V -> G (in Ref. 3; AGA18939/AGA18942)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="F -> S (in Ref. 7; AFX62835)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="N -> T (in Ref. 3; AGA18939/AGA18941/AGA18942 and 7;
FT AFX62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="D -> G (in Ref. 7; AFX62833)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="N -> K (in Ref. 7; AFX62833/AFX62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="D -> G (in Ref. 7; AFX62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="K -> R (in Ref. 7; AFX62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="A -> S (in Ref. 3; AGA18946)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="I -> T (in Ref. 7; AFX62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="S -> T (in Ref. 3; AGA18940/AGA18942/AGA18946 and 7;
FT AFX62833/AFX62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="M -> T (in Ref. 7; AFX62833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 866 AA; 98559 MW; 8F84CF1B0B89103B CRC64;
MNLPPNPVIA RGRGRGRKPN NVEANRGFAP SLGQKSDPSH SEGNQASGGN GGGGDAQVGP
SIEKSSLSAV QMHKSEGDPR GSVRGRRLIT DLVYSRPPGM TSKKGVVGTH ITVQANYFKV
LKRPNWTIYQ YRVDFTPDVE ATRLRRSFLY EHKGILGGYI FDGTNMFCIN QFKAVQDSPY
VLELVTKSRA GENIEIKIKA VGSVQSTDAE QFQVLNLILR RAMEGLDLKL VSRYYYDPQA
KINLENFRMQ LWPGYQTSIR QHENDILLCS EICHKVMRTE TLYNILSDAI RDSDDYQSTF
KRAVMGMVIL TDYNNKTYRI DDVDFQSTPL CKFKTNDGEI SYVDYYKKRY NIIIRDLKQP
LVMSRPTDKN IRGGNDQAIM IIPELARATG MTDAMRADFR TLRAMSEHTR LNPDRRIERL
RMFNKRLKSC KQSVETLKSW NIELDSALVE IPARVLPPEK ILFGNQKIFV CDARADWTNE
FRTCSMFKNV HINRWYVITP SRNLRETQEF VQMCIRTASS MKMNICNPIY EEIPDDRNGT
YSQAIDNAAA NDPQIVMVVM RSPNEEKYSC IKKRTCVDRP VPSQVVTLKV IAPRQQKPTG
LMSIATKVVI QMNAKLMGAP WQVVIPLHGL MTVGFDVCHS PKNKNKSYGA FVATMDQKES
FRYFSTVNEH IKGQELSEQM SVNMACALRS YQEQHRSLPE RILFFRDGVG DGQLYQVVNS
EVNTLKDRLD EIYKSAGKQE GCRMTFIIVS KRINSRYFTG HRNPVPGTVV DDVITLPERY
DFFLVSQAVR IGTVSPTSYN VISDNMGLNA DKLQMLSYKM THMYYNYSGT IRVPAVCHYA
HKLAFLVAES INRAPSAGLQ NQLYFL
