PIWI_DROME
ID PIWI_DROME Reviewed; 843 AA.
AC Q9VKM1; C0PTU6; K7WKS7; K7WKT2; K7WQ39; K7WS94; K7XHZ2; L0CPR8; L0CPS4;
AC L0CQ04; L0CR36; L0CRH9; L0CRI5; L0CRU0; O96674; O96675; Q6NNZ4; Q6NP34;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein piwi;
DE EC=3.1.26.- {ECO:0000250|UniProtKB:A8D8P8};
GN Name=piwi; ORFNames=CG6122;
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:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=9851978; DOI=10.1101/gad.12.23.3715;
RA Cox D.N., Chao A., Baker J., Chang L., Qiao D., Lin H.;
RT "A novel class of evolutionarily conserved genes defined by piwi are
RT essential for stem cell self-renewal.";
RL Genes Dev. 12:3715-3727(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3846, 3852, 3854, 3892, 3893, 3894, and 3895;
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 [3] {ECO:0000305}
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 [MRNA].
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 (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
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]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9199372; DOI=10.1242/dev.124.12.2463;
RA Lin H., Spradling A.C.;
RT "A novel group of pumilio mutations affects the asymmetric division of
RT germline stem cells in the Drosophila ovary.";
RL Development 124:2463-2476(1997).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10631171; DOI=10.1242/dev.127.3.503;
RA Cox D.N., Chao A., Lin H.;
RT "piwi encodes a nucleoplasmic factor whose activity modulates the number
RT and division rate of germline stem cells.";
RL Development 127:503-514(2000).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15817569; DOI=10.1093/nar/gki323;
RA Kalmykova A.I., Klenov M.S., Gvozdev V.A.;
RT "Argonaute protein PIWI controls mobilization of retrotransposons in the
RT Drosophila male germline.";
RL Nucleic Acids Res. 33:2052-2059(2005).
RN [11]
RP FUNCTION, INTERACTION WITH VAS; DCR-1 AND FMR1, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
RA Megosh H.B., Cox D.N., Campbell C., Lin H.;
RT "The role of PIWI and the miRNA machinery in Drosophila germline
RT determination.";
RL Curr. Biol. 16:1884-1894(2006).
RN [12]
RP FUNCTION, RNA-BINDING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16882972; DOI=10.1101/gad.1454806;
RA Saito K., Nishida K.M., Mori T., Kawamura Y., Miyoshi K., Nagami T.,
RA Siomi H., Siomi M.C.;
RT "Specific association of Piwi with rasiRNAs derived from retrotransposon
RT and heterochromatic regions in the Drosophila genome.";
RL Genes Dev. 20:2214-2222(2006).
RN [13]
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 [14]
RP FUNCTION, INTERACTION WITH CBX5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF VAL-30 AND VAL-130.
RX PubMed=17875665; DOI=10.1101/gad.1564307;
RA Brower-Toland B., Findley S.D., Jiang L., Liu L., Yin H., Dus M., Zhou P.,
RA Elgin S.C., Lin H.;
RT "Drosophila PIWI associates with chromatin and interacts directly with
RT HP1a.";
RL Genes Dev. 21:2300-2311(2007).
RN [15]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=17952056; DOI=10.1038/nature06263;
RA Yin H., Lin H.;
RT "An epigenetic activation role of Piwi and a Piwi-associated piRNA in
RT Drosophila melanogaster.";
RL Nature 450:304-308(2007).
RN [16]
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 [17]
RP RNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-614 AND ASP-685.
RX PubMed=19812547; DOI=10.1038/nature08501;
RA Saito K., Inagaki S., Mituyama T., Kawamura Y., Ono Y., Sakota E.,
RA Kotani H., Asai K., Siomi H., Siomi M.C.;
RT "A regulatory circuit for piwi by the large Maf gene traffic jam in
RT Drosophila.";
RL Nature 461:1296-1299(2009).
RN [18]
RP RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND METHYLATION.
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 [19]
RP FUNCTION, INTERACTION WITH ARMI AND FS(1)YB, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-54; THR-67 AND 327-TYR-TYR-328.
RX PubMed=20966047; DOI=10.1101/gad.1989510;
RA Saito K., Ishizu H., Komai M., Kotani H., Kawamura Y., Nishida K.M.,
RA Siomi H., Siomi M.C.;
RT "Roles for the Yb body components Armitage and Yb in primary piRNA
RT biogenesis in Drosophila.";
RL Genes Dev. 24:2493-2498(2010).
RN [20]
RP INTERACTION WITH PAPI, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 7-ARG--ARG-9.
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 [21]
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HOP AND
RP HSP83, AND PHOSPHORYLATION.
RX PubMed=21186352; DOI=10.1038/ng.743;
RA Gangaraju V.K., Yin H., Weiner M.M., Wang J., Huang X.A., Lin H.;
RT "Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic
RT variation.";
RL Nat. Genet. 43:153-158(2011).
RN [23]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22065765; DOI=10.1073/pnas.1106676108;
RA Klenov M.S., Sokolova O.A., Yakushev E.Y., Stolyarenko A.D.,
RA Mikhaleva E.A., Lavrov S.A., Gvozdev V.A.;
RT "Separation of stem cell maintenance and transposon silencing functions of
RT Piwi protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18760-18765(2011).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 4-ASP--PRO-12; ASP-614
RP AND ASP-685.
RX PubMed=23159368; DOI=10.1016/j.cell.2012.10.040;
RA Sienski G., Donertas D., Brennecke J.;
RT "Transcriptional silencing of transposons by Piwi and maelstrom and its
RT impact on chromatin state and gene expression.";
RL Cell 151:964-980(2012).
RN [25]
RP FUNCTION.
RX PubMed=23434410; DOI=10.1016/j.devcel.2013.01.023;
RA Huang X.A., Yin H., Sweeney S., Raha D., Snyder M., Lin H.;
RT "A major epigenetic programming mechanism guided by piRNAs.";
RL Dev. Cell 24:502-516(2013).
RN [26]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 551-TYR--LYS-555.
RX PubMed=23392610; DOI=10.1101/gad.209841.112;
RA Le Thomas A., Rogers A.K., Webster A., Marinov G.K., Liao S.E.,
RA Perkins E.M., Hur J.K., Aravin A.A., Toth K.F.;
RT "Piwi induces piRNA-guided transcriptional silencing and establishment of a
RT repressive chromatin state.";
RL Genes Dev. 27:390-399(2013).
RN [27]
RP FUNCTION.
RX PubMed=23392609; DOI=10.1101/gad.209767.112;
RA Rozhkov N.V., Hammell M., Hannon G.J.;
RT "Multiple roles for Piwi in silencing Drosophila transposons.";
RL Genes Dev. 27:400-412(2013).
RN [28]
RP INTERACTION WITH ARX.
RX PubMed=23913921; DOI=10.1101/gad.221515.113;
RA Ohtani H., Iwasaki Y.W., Shibuya A., Siomi H., Siomi M.C., Saito K.;
RT "DmGTSF1 is necessary for Piwi-piRISC-mediated transcriptional transposon
RT silencing in the Drosophila ovary.";
RL Genes Dev. 27:1656-1661(2013).
RN [29]
RP INTERACTION WITH ARX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23913922; DOI=10.1101/gad.221150.113;
RA Doenertas D., Sienski G., Brennecke J.;
RT "Drosophila Gtsf1 is an essential component of the Piwi-mediated
RT transcriptional silencing complex.";
RL Genes Dev. 27:1693-1705(2013).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-614 AND ASP-685.
RX PubMed=23297219; DOI=10.1073/pnas.1213283110;
RA Darricarrere N., Liu N., Watanabe T., Lin H.;
RT "Function of Piwi, a nuclear Piwi/Argonaute protein, is independent of its
RT slicer activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1297-1302(2013).
RN [31]
RP INTERACTION WITH PANX.
RX PubMed=26472911; DOI=10.1126/science.aab0700;
RA Yu Y., Gu J., Jin Y., Luo Y., Preall J.B., Ma J., Czech B., Hannon G.J.;
RT "Panoramix enforces piRNA-dependent cotranscriptional silencing.";
RL Science 350:339-342(2015).
RN [32]
RP INTERACTION WITH PANX.
RX PubMed=26494711; DOI=10.1101/gad.271908.115;
RA Sienski G., Batki J., Senti K.A., Doenertas D., Tirian L., Meixner K.,
RA Brennecke J.;
RT "Silencio/CG9754 connects the Piwi-piRNA complex to the cellular
RT heterochromatin machinery.";
RL Genes Dev. 29:2258-2271(2015).
RN [33]
RP FUNCTION, INTERACTION WITH TUDOR-SN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26808625; DOI=10.1371/journal.pgen.1005813;
RA Ku H.Y., Gangaraju V.K., Qi H., Liu N., Lin H.;
RT "Tudor-SN Interacts with Piwi Antagonistically in Regulating
RT Spermatogenesis but Synergistically in Silencing Transposons in
RT Drosophila.";
RL PLoS Genet. 12:E1005813-E1005813(2016).
RN [34]
RP FUNCTION, ASSOCIATION WITH NUCLEAR PORE COMPLEX, INTERACTION WITH ELYS;
RP THOC5 AND XMAS-2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28472469; DOI=10.1093/nar/gkx355;
RA Ilyin A.A., Ryazansky S.S., Doronin S.A., Olenkina O.M., Mikhaleva E.A.,
RA Yakushev E.Y., Abramov Y.A., Belyakin S.N., Ivankin A.V., Pindyurin A.V.,
RA Gvozdev V.A., Klenov M.S., Shevelyov Y.Y.;
RT "Piwi interacts with chromatin at nuclear pores and promiscuously binds
RT nuclear transcripts in Drosophila ovarian somatic cells.";
RL Nucleic Acids Res. 45:7666-7680(2017).
RN [35]
RP INTERACTION WITH NUP358, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29735528; DOI=10.1074/jbc.ac118.003264;
RA Parikh R.Y., Lin H., Gangaraju V.K.;
RT "A critical role for nucleoporin 358 (Nup358) in transposon silencing and
RT piRNA biogenesis in Drosophila.";
RL J. Biol. Chem. 293:9140-9147(2018).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2; PANX AND NXT1, AND TISSUE SPECIFICITY.
RX PubMed=31368590; DOI=10.15252/embj.2019102870;
RA Murano K., Iwasaki Y.W., Ishizu H., Mashiko A., Shibuya A., Kondo S.,
RA Adachi S., Suzuki S., Saito K., Natsume T., Siomi M.C., Siomi H.;
RT "Nuclear RNA export factor variant initiates piRNA-guided co-
RT transcriptional silencing.";
RL EMBO J. 38:E102870-E102870(2019).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP WITH NXF2; PANX AND NXT1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31384064; DOI=10.1038/s41594-019-0270-6;
RA Batki J., Schnabl J., Wang J., Handler D., Andreev V.I., Stieger C.E.,
RA Novatchkova M., Lampersberger L., Kauneckaite K., Xie W., Mechtler K.,
RA Patel D.J., Brennecke J.;
RT "The nascent RNA binding complex SFiNX licenses piRNA-guided
RT heterochromatin formation.";
RL Nat. Struct. Mol. Biol. 26:720-731(2019).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 4-12, IDENTIFICATION BY MASS
RP SPECTROMETRY, INTERACTION WITH PAPI, METHYLATION AT ARG-7; ARG-9; ARG-10
RP AND ARG-11, AND MUTAGENESIS OF GLN-5; 7-ARG--ARG-11; ARG-7; GLY-8; ARG-9;
RP ARG-10; ARG-11; PRO-12; 51-ARG--ARG-54 AND 61-ARG--ARG-62.
RX PubMed=29531043; DOI=10.1073/pnas.1717116115;
RA Zhang Y.H., Liu W.W., Li R.H., Gu J.Q., Wu P., Peng C., Ma J.B., Wu L.G.,
RA Yu Y., Huang Y.;
RT "Structural insights into the sequence-specific recognition of Piwi by
RT Drosophila Papi.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3374-3379(2018).
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
CC (PubMed:26808625, PubMed:15817569, PubMed:17346786). Directly binds
CC piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a
CC Dicer-independent mechanism and are primarily derived from transposons
CC and other repeated sequence elements (PubMed:16882972). In ovarian
CC somatic cells, mediates silencing of transposable elements at the
CC transcriptional level in a mael-dependent manner (PubMed:23159368,
CC PubMed:28472469). Involved in silencing of long terminal repeat (LTR)
CC retrotransposons in male germline (PubMed:15817569). In testis,
CC regulates spermatogenesis together with Tudor-SN (PubMed:26808625). In
CC germ cells, mediates silencing at both transcriptional and post-
CC transcriptional levels and is involved in the maintenance of
CC populations of primary and secondary piRNAs. Piwi-mediated
CC transcriptional silencing is accompanied by the formation of His3 'Lys-
CC 9' trimethylated (H3K9me3) euchromatin and heterochromatin
CC (PubMed:23434410, PubMed:23392610). In ovary, associates predominantly
CC with antisense piRNAs that contain uridine at their 5' end. Association
CC with sense piRNAs is also observed but to a lesser extent. Mediates a
CC somatic signaling mechanism required for the maintenance of germline
CC stem cells to produce and maintain a daughter germline stem cell
CC (PubMed:9851978, PubMed:10631171, PubMed:9199372, PubMed:16949822). It
CC is not essential for the further differentiation of the committed
CC daughter cell (PubMed:9851978). Acts cell autonomously to promote
CC germline stem cell division (PubMed:9851978, PubMed:10631171). Its role
CC in stem cell maintenance does not seem to require nuclear localization.
CC Required maternally for the posterior localization of osk and vas and
CC for pole cell formation during oogenesis and early embryogenesis
CC (PubMed:16949822). Together with Hop and Hsp83, mediates canalization,
CC also known as developmental robustness, likely via epigenetic silencing
CC of existing genetic variants and suppression of transposon-induced new
CC genetic variation (PubMed:21186352). Shows RNA cleavage activity,
CC although is not required for any of its known functions
CC (PubMed:9199372, PubMed:16882972, PubMed:23297219). In the ovaries,
CC forms a complex with nxf2, Panx and Nxt1 which acts as effectors of
CC cotranscriptional transposon silencing (PubMed:31368590,
CC PubMed:31384064). {ECO:0000269|PubMed:10631171,
CC ECO:0000269|PubMed:15817569, ECO:0000269|PubMed:16882972,
CC ECO:0000269|PubMed:16949822, ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:17952056,
CC ECO:0000269|PubMed:20966047, ECO:0000269|PubMed:21186352,
CC ECO:0000269|PubMed:22065765, ECO:0000269|PubMed:23159368,
CC ECO:0000269|PubMed:23297219, ECO:0000269|PubMed:23392609,
CC ECO:0000269|PubMed:23392610, ECO:0000269|PubMed:23434410,
CC ECO:0000269|PubMed:26808625, ECO:0000269|PubMed:28472469,
CC ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064,
CC ECO:0000269|PubMed:9199372, ECO:0000269|PubMed:9851978}.
CC -!- SUBUNIT: In the ovaries, part of a complex composed of at least Panx,
CC nxf2, piwi and Nxt1 (PubMed:26472911, PubMed:26494711, PubMed:31368590,
CC PubMed:31384064). The complex is knowns as Panx-induced co-
CC transcriptional silencing (PICTS) complex, Panx-nxf2-dependent TAP/p15
CC silencing (Pandas complex), SFiNX (silencing factor interacting nuclear
CC export variant) or piwi-Panx-nxf2-p15 (PPNP) complex (PubMed:26472911,
CC PubMed:26494711, PubMed:31368590, PubMed:31384064). Interacts with vas;
CC this interaction is RNA-independent (PubMed:16949822). Interacts with
CC Dcr-1 and Fmr1; these interactions occur in polar granules
CC (PubMed:16949822). Interacts (via N-terminal region) with CBX5 (via
CC chromoshadow domain) (PubMed:17875665). Forms a complex with Hsp83 and
CC Hop; probably Hop mediates the interaction between piwi and Hsp83
CC (PubMed:21186352). Forms a complex with Yb body components armi and
CC fs(1)Yb; this interaction is required for proper piRNA loading and
CC nuclear localization of piwi (PubMed:20966047). Interaction of Piwi and
CC fs(1)Yb is likely to occur via armi (PubMed:20966047). Interacts (via
CC the N-terminal region when unmethylated or symmetrically methylated at
CC Arg-10) with papi (via Tudor domain) (PubMed:21447556,
CC PubMed:29531043). Interacts with vret (PubMed:21831924). Interacts with
CC Panx (PubMed:26472911, PubMed:26494711). Interacts with arx
CC (PubMed:23913921, PubMed:23913922). Interacts with Tudor-SN
CC (PubMed:26808625). Interacts with Nup358 (via N-terminus)
CC (PubMed:29735528). Associates with the nuclear pore complex via
CC interaction with Elys (PubMed:28472469). Interacts with thoc5; the
CC interaction might be partly RNA-mediated (PubMed:28472469). Interacts
CC with xmas-2 (PubMed:28472469). {ECO:0000269|PubMed:16949822,
CC ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:20966047,
CC ECO:0000269|PubMed:21186352, ECO:0000269|PubMed:21447556,
CC ECO:0000269|PubMed:21831924, ECO:0000269|PubMed:23913921,
CC ECO:0000269|PubMed:23913922, ECO:0000269|PubMed:26472911,
CC ECO:0000269|PubMed:26494711, ECO:0000269|PubMed:26808625,
CC ECO:0000269|PubMed:28472469, ECO:0000269|PubMed:29531043,
CC ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064}.
CC -!- INTERACTION:
CC Q9VKM1; Q6J5K9: armi; NbExp=4; IntAct=EBI-3406276, EBI-2890374;
CC Q9VKM1; Q9W2H9: Panx; NbExp=2; IntAct=EBI-3406276, EBI-184428;
CC Q9VKM1; Q9VQ91: papi; NbExp=3; IntAct=EBI-3406276, EBI-6915287;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26808625,
CC ECO:0000269|PubMed:29735528}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10631171}. Nucleus {ECO:0000269|PubMed:26808625,
CC ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31384064}. Chromosome
CC {ECO:0000269|PubMed:28472469}. Note=Component of polar granules.
CC Present in the cytoplasm of the developing oocyte. At the mitotic cycle
CC 11 translocates to the nucleus where it remains localized throughout
CC germ-cell development and gonadogenesis. Localizes at genomic sites
CC enriched for methylated H3K9. Interacts with chromatin at the nuclear
CC pore complex (PubMed:28472469). {ECO:0000269|PubMed:28472469}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level)
CC (PubMed:28472469, PubMed:31368590, PubMed:31384064). Expressed
CC somatically in ovariole terminal filament cells, epithelial sheath
CC cells, cap cells and follicle cells (at protein level). Expressed in
CC nurse cells and oocytes in developing egg chambers (at protein level)
CC (PubMed:29531043, PubMed:29735528). In embryos, accumulates in pole
CC cells (at protein level). In larval and adult testis, expressed in a
CC germinal proliferative center at the apical tip containing somatic hub
CC cells and mitotically dividing germ stem cells (at protein level)
CC (PubMed:26808625). {ECO:0000269|PubMed:10631171,
CC ECO:0000269|PubMed:15817569, ECO:0000269|PubMed:16882972,
CC ECO:0000269|PubMed:16949822, ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:23297219, ECO:0000269|PubMed:26808625,
CC ECO:0000269|PubMed:28472469, ECO:0000269|PubMed:29531043,
CC ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31368590,
CC ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:9199372,
CC ECO:0000269|PubMed:9851978}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in the germarium, at low levels during oogenesis stages 1-6,
CC at a lower level during stages 7-9, strongly at stage 10, eventually
CC accumulates in early embryos and later in development the expression
CC decreases (at protein level). {ECO:0000269|PubMed:16882972,
CC ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:17875665,
CC ECO:0000269|PubMed:26808625, ECO:0000269|PubMed:9851978}.
CC -!- PTM: Symmetrically dimethylated, most likely by csul (PubMed:19377467,
CC PubMed:29531043). Methylation at Arg-10 enhances binding to papi
CC whereas methylation at Arg-7, Arg-9 or Arg-11 reduces binding affinity
CC to papi (PubMed:29531043). {ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:29531043}.
CC -!- PTM: Phosphorylated on serine and tyrosine residues in an Hsp83-
CC dependent manner. {ECO:0000269|PubMed:21186352}.
CC -!- DISRUPTION PHENOTYPE: Female mutants show normal ovarian development up
CC to third instar larval stage (PubMed:9851978, PubMed:9199372,
CC PubMed:26808625). However, adult mutant ovarioles contain germaria
CC lacking germline cells and containing two normal or abnormal egg
CC chambers as result of the failure of germline stem cell maintenance
CC (PubMed:9851978, PubMed:9199372, PubMed:26808625). In adult testis,
CC results in deregulation of transposon silencing (PubMed:26808625).
CC {ECO:0000269|PubMed:26808625, ECO:0000269|PubMed:9199372,
CC ECO:0000269|PubMed:9851978}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR82763.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAR82805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACN43727.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF104354; AAD08704.1; -; mRNA.
DR EMBL; AF104355; AAD08705.1; -; Genomic_DNA.
DR EMBL; KC116149; AGA18878.1; -; Genomic_DNA.
DR EMBL; KC116150; AGA18879.1; -; Genomic_DNA.
DR EMBL; KC116151; AGA18880.1; -; Genomic_DNA.
DR EMBL; KC116152; AGA18881.1; -; Genomic_DNA.
DR EMBL; KC116153; AGA18882.1; -; Genomic_DNA.
DR EMBL; KC116154; AGA18883.1; -; Genomic_DNA.
DR EMBL; KC116155; AGA18884.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53043.1; -; Genomic_DNA.
DR EMBL; BT011097; AAR82763.1; ALT_INIT; mRNA.
DR EMBL; BT011138; AAR82805.1; ALT_INIT; mRNA.
DR EMBL; BT071791; ACN43727.1; ALT_INIT; mRNA.
DR EMBL; JX656897; AFX62837.1; -; mRNA.
DR EMBL; JX656898; AFX62838.1; -; mRNA.
DR EMBL; JX656899; AFX62839.1; -; mRNA.
DR EMBL; JX656901; AFX62841.1; -; mRNA.
DR EMBL; JX656902; AFX62842.1; -; mRNA.
DR RefSeq; NP_001285825.1; NM_001298896.1.
DR RefSeq; NP_476875.1; NM_057527.4.
DR PDB; 5YGD; X-ray; 1.55 A; D=4-14.
DR PDB; 5YGF; X-ray; 1.70 A; D=4-12.
DR PDB; 6KR6; X-ray; 2.90 A; A=34-843.
DR PDBsum; 5YGD; -.
DR PDBsum; 5YGF; -.
DR PDBsum; 6KR6; -.
DR AlphaFoldDB; Q9VKM1; -.
DR SMR; Q9VKM1; -.
DR BioGRID; 60588; 56.
DR DIP; DIP-61694N; -.
DR IntAct; Q9VKM1; 25.
DR MINT; Q9VKM1; -.
DR STRING; 7227.FBpp0079755; -.
DR PaxDb; Q9VKM1; -.
DR EnsemblMetazoa; FBtr0080166; FBpp0079755; FBgn0004872.
DR EnsemblMetazoa; FBtr0340227; FBpp0309202; FBgn0004872.
DR GeneID; 34521; -.
DR KEGG; dme:Dmel_CG6122; -.
DR CTD; 34521; -.
DR FlyBase; FBgn0004872; piwi.
DR VEuPathDB; VectorBase:FBgn0004872; -.
DR eggNOG; KOG1042; Eukaryota.
DR HOGENOM; CLU_008813_0_0_1; -.
DR InParanoid; Q9VKM1; -.
DR OMA; LDRWAVI; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; Q9VKM1; -.
DR SignaLink; Q9VKM1; -.
DR BioGRID-ORCS; 34521; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34521; -.
DR PRO; PR:Q9VKM1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004872; Expressed in ovary and 16 other tissues.
DR ExpressionAtlas; Q9VKM1; baseline and differential.
DR Genevisible; Q9VKM1; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0010369; C:chromocenter; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0043073; C:germ cell nucleus; IDA:FlyBase.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0070725; C:Yb body; IMP:FlyBase.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034584; F:piRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IMP:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
DR GO; GO:0000335; P:negative regulation of transposition, DNA-mediated; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
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; 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; Chromosome; Cytoplasm; Developmental protein; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Methylation; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..843
FT /note="Protein piwi"
FT /id="PRO_0000194067"
FT DOMAIN 262..372
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 538..829
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..257
FT /note="Interaction with CBX5 and papi"
FT /evidence="ECO:0000269|PubMed:17875665"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..12
FT /note="Nuclear localization signal"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 614
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 685
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT BINDING 589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT BINDING 843
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT MOD_RES 7
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:29531043"
FT MOD_RES 9
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:29531043"
FT MOD_RES 10
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:29531043"
FT MOD_RES 11
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 4..12
FT /note="Missing: Largely prevents nuclear accumulation.
FT Affects repression activity of soma- and germline-specific
FT transposable elements and fertility."
FT /evidence="ECO:0000269|PubMed:23159368"
FT MUTAGEN 5
FT /note="Q->A: Reduced binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 7..11
FT /note="RGRRR->AGAAA: Abolishes binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 7..9
FT /note="RGR->KGK: Abolishes binding to papi."
FT /evidence="ECO:0000269|PubMed:21447556"
FT MUTAGEN 7
FT /note="R->A: Large decrease in binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 7
FT /note="R->K: Large decrease in binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 8
FT /note="G->V: Highly significant decrease in binding to
FT papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 9
FT /note="R->A: Decreased binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 9
FT /note="R->K: Decreased binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 10
FT /note="R->A: Abolishes binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 10
FT /note="R->K: Abolishes binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 11
FT /note="R->A: Decreased binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 11
FT /note="R->K: Decreased binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 12
FT /note="P->A: No significant effect on binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 30
FT /note="V->A: Abolishes binding to CBX5; when associated
FT with or without A-130. Fails to rescue dominant defects in
FT white reporter silencing produced by the piwi2 mutation."
FT /evidence="ECO:0000269|PubMed:17875665"
FT MUTAGEN 51..54
FT /note="RERR->AEAA: No effect on binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 54
FT /note="R->G: Confers RNAi insensitivity; when associated
FT with P-67."
FT /evidence="ECO:0000269|PubMed:20966047"
FT MUTAGEN 61..62
FT /note="RR->AA: No effect on binding to papi."
FT /evidence="ECO:0000269|PubMed:29531043"
FT MUTAGEN 67
FT /note="T->P: Confers RNAi insensitivity; when associated
FT with G-54."
FT /evidence="ECO:0000269|PubMed:20966047"
FT MUTAGEN 130
FT /note="V->A: Abolishes binding to CBX5; when associated
FT with A-30."
FT /evidence="ECO:0000269|PubMed:17875665"
FT MUTAGEN 327..328
FT /note="YY->AA: Promotes accumulation in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:20966047"
FT MUTAGEN 551..555
FT /note="YSSIK->LSSIE: Abolishes binding to piRNAs. Reduces
FT localization to the nucleus. Does not affect chromatin
FT binding. Affects fertility and ovary morphology."
FT /evidence="ECO:0000269|PubMed:23392610"
FT MUTAGEN 614
FT /note="D->A: Does not affect nuclear localization,
FT repression activity of soma- and germline-specific
FT transposable elements, fertility and piRNA loading; when
FT associated with or without A-685."
FT /evidence="ECO:0000269|PubMed:19812547,
FT ECO:0000269|PubMed:23159368, ECO:0000269|PubMed:23297219"
FT MUTAGEN 685
FT /note="D->A: Does not affect nuclear localization,
FT repression activity of soma- and germline-specific
FT transposable elements, fertility and piRNA loading; when
FT associated with or without A-614."
FT /evidence="ECO:0000269|PubMed:19812547,
FT ECO:0000269|PubMed:23159368, ECO:0000269|PubMed:23297219"
FT CONFLICT 33
FT /note="F -> S (in Ref. 7; AFX62841/AFX62842)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="R -> G (in Ref. 2; AGA18878/AGA18879/AGA18881/
FT AGA18882/AGA18883/AGA18884, 5; AAR82805 and 7; AFX62837/
FT AFX62838/AFX62839/AFX62841/AFX62842)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="T -> P (in Ref. 1; AAD08704, 2; AGA18878/AGA18879/
FT AGA18880/AGA18881/AGA18882/AGA18883/AGA18884, 5; AAR82805
FT and 7; AFX62837/AFX62838/AFX62839/AFX62841/AFX62842)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="N -> D (in Ref. 2; AGA18882/AGA18883 and 5;
FT AAR82805)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> V (in Ref. 1; AAD08704, 2; AGA18878/AGA18879/
FT AGA18880/AGA18881/AGA18882/AGA18883/AGA18884, 5; AAR82805
FT and 7; AFX62837/AFX62838/AFX62839/AFX62841/AFX62842)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..124
FT /note="EPS -> VPT (in Ref. 1; AAD08704, 2; AGA18880/
FT AGA18881/AGA18882/AGA18883 and 5; AAR82805)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> I (in Ref. 2; AGA18884)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="F -> L (in Ref. 7; AFX62841)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="I -> V (in Ref. 7; AFX62841)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="S -> L (in Ref. 7; AFX62842)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="V -> L (in Ref. 5; AAR82805)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="I -> V (in Ref. 7; AFX62837/AFX62838)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="S -> P (in Ref. 7; AFX62837/AFX62838)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="L -> P (in Ref. 7; AFX62837/AFX62838)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="K -> R (in Ref. 7; AFX62839)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..577
FT /note="NR -> KPY (in Ref. 1; AAD08705)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="G -> R (in Ref. 5; AAR82763)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="R -> G (in Ref. 7; AFX62839)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="K -> E (in Ref. 7; AFX62842)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:5YGD"
FT STRAND 94..107
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:6KR6"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:6KR6"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6KR6"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 231..243
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 248..260
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 395..411
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 413..421
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6KR6"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:6KR6"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 487..504
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 521..532
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 539..545
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 548..559
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 579..593
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 606..617
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 625..632
FT /evidence="ECO:0007829|PDB:6KR6"
FT TURN 634..637
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 641..647
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 658..673
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 692..713
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 720..728
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 749..752
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 774..781
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 787..797
FT /evidence="ECO:0007829|PDB:6KR6"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 812..826
FT /evidence="ECO:0007829|PDB:6KR6"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:6KR6"
SQ SEQUENCE 843 AA; 97177 MW; 9B4A95E688E9D9B7 CRC64;
MADDQGRGRR RPLNEDDSST SRGSGDGPRV KVFRGSSSGD PRADPRIEAS RERRALEEAP
RREGGPTERK PWGDQYDYLN TRPAELVSKK GTDGVPVMLQ TNFFRLKTKP EWRIVHYHVE
FEPSIENPRV RMGVLSNHAN LLGSGYLFDG LQLFTTRKFE QEITVLSGKS KLDIEYKISI
KFVGFISCAE PRFLQVLNLI LRRSMKGLNL ELVGRNLFDP RAKIEIREFK MELWPGYETS
IRQHEKDILL GTEITHKVMR TETIYDIMRR CSHNPARHQD EVRVNVLDLI VLTDYNNRTY
RINDVDFGQT PKSTFSCKGR DISFVEYYLT KYNIRIRDHN QPLLISKNRD KALKTNASEL
VVLIPELCRV TGLNAEMRSN FQLMRAMSSY TRMNPKQRTD RLRAFNHRLQ NTPESVKVLR
DWNMELDKNV TEVQGRIIGQ QNIVFHNGKV PAGENADWQR HFRDQRMLTT PSDGLDRWAV
IAPQRNSHEL RTLLDSLYRA ASGMGLRIRS PQEFIIYDDR TGTYVRAMDD CVRSDPKLIL
CLVPNDNAER YSSIKKRGYV DRAVPTQVVT LKTTKNRSLM SIATKIAIQL NCKLGYTPWM
IELPLSGLMT IGFDIAKSTR DRKRAYGALI ASMDLQQNST YFSTVTECSA FDVLANTLWP
MIAKALRQYQ HEHRKLPSRI VFYRDGVSSG SLKQLFEFEV KDIIEKLKTE YARVQLSPPQ
LAYIVVTRSM NTRFFLNGQN PPPGTIVDDV ITLPERYDFY LVSQQVRQGT VSPTSYNVLY
SSMGLSPEKM QKLTYKMCHL YYNWSGTTRV PAVCQYAKKL ATLVGTNLHS IPQNALEKKF
YYL
