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Database: UniProt
Entry: Q9VKM1
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Original site: Q9VKM1 
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   11-DEC-2019, entry version 138.
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; Holometabola; 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;
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;
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   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).
CC       {ECO:0000269|PubMed:10631171, ECO:0000269|PubMed:15817569,
CC       ECO:0000269|PubMed:16882972, ECO:0000269|PubMed:16949822,
CC       ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:17875665,
CC       ECO:0000269|PubMed:17952056, ECO:0000269|PubMed:20966047,
CC       ECO:0000269|PubMed:21186352, ECO:0000269|PubMed:22065765,
CC       ECO:0000269|PubMed:23159368, ECO:0000269|PubMed:23297219,
CC       ECO:0000269|PubMed:23392609, ECO:0000269|PubMed:23392610,
CC       ECO:0000269|PubMed:23434410, ECO:0000269|PubMed:26808625,
CC       ECO:0000269|PubMed:28472469, ECO:0000269|PubMed:9199372,
CC       ECO:0000269|PubMed:9851978}.
CC   -!- SUBUNIT: Interacts with vas; this interaction is RNA-independent
CC       (PubMed:16949822). Interacts with Dcr-1 and Fmr1; these interactions
CC       occur in polar granules (PubMed:16949822). Interacts (via N-terminal
CC       region) with CBX5 (via chromoshadow domain) (PubMed:17875665). Forms a
CC       complex with Hsp83 and Hop; probably Hop mediates the interaction
CC       between piwi and Hsp83 (PubMed:21186352). Forms a complex with Yb body
CC       components armi and fs(1)Yb; this interaction is required for proper
CC       piRNA loading and nuclear localization of piwi (PubMed:20966047).
CC       Interaction of Piwi and fs(1)Yb is likely to occur via armi
CC       (PubMed:20966047). Interacts (via the N-terminal region when
CC       unmethylated or symmetrically methylated at Arg-10) with papi (via
CC       Tudor domain) (PubMed:21447556, PubMed:29531043). Interacts with vret
CC       (PubMed:21831924). Interacts with Panx (PubMed:26472911,
CC       PubMed:26494711). Interacts with arx (PubMed:23913921,
CC       PubMed:23913922). Interacts with Tudor-SN (PubMed:26808625). Interacts
CC       with Nup358 (via N-terminus) (PubMed:29735528). Associates with the
CC       nuclear pore complex via interaction with Elys (PubMed:28472469).
CC       Interacts with thoc5; the interaction might be partly RNA-mediated
CC       (PubMed:28472469). Interacts with xmas-2 (PubMed:28472469).
CC       {ECO:0000269|PubMed:16949822, ECO:0000269|PubMed:17875665,
CC       ECO:0000269|PubMed:20966047, ECO:0000269|PubMed:21186352,
CC       ECO:0000269|PubMed:21447556, ECO:0000269|PubMed:21831924,
CC       ECO:0000269|PubMed:23913921, ECO:0000269|PubMed:23913922,
CC       ECO:0000269|PubMed:26472911, ECO:0000269|PubMed:26494711,
CC       ECO:0000269|PubMed:26808625, ECO:0000269|PubMed:28472469,
CC       ECO:0000269|PubMed:29531043, ECO:0000269|PubMed:29735528}.
CC   -!- INTERACTION:
CC       Q6J5K9:armi; NbExp=4; IntAct=EBI-3406276, EBI-2890374;
CC       Q9W2H9:Panx; NbExp=2; IntAct=EBI-3406276, EBI-184428;
CC       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}. Chromosome {ECO:0000269|PubMed:28472469}.
CC       Note=Component of polar granules. Present in the cytoplasm of the
CC       developing oocyte. At the mitotic cycle 11 translocates to the nucleus
CC       where it remains localized throughout germ-cell development and
CC       gonadogenesis. Localizes at genomic sites enriched for methylated H3K9.
CC       Interacts with chromatin at the nuclear pore complex (PubMed:28472469).
CC       {ECO:0000269|PubMed:28472469}.
CC   -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level)
CC       (PubMed:28472469). Expressed somatically in ovariole terminal filament
CC       cells, epithelial sheath cells, cap cells and follicle cells (at
CC       protein level). Expressed in nurse cells and oocytes in developing egg
CC       chambers (at protein level) (PubMed:29531043, PubMed:29735528). In
CC       embryos, accumulates in pole cells (at protein level). In larval and
CC       adult testis, expressed in a germinal proliferative center at the
CC       apical tip containing somatic hub cells and mitotically dividing germ
CC       stem cells (at protein level) (PubMed:26808625).
CC       {ECO:0000269|PubMed:10631171, ECO:0000269|PubMed:15817569,
CC       ECO:0000269|PubMed:16882972, ECO:0000269|PubMed:16949822,
CC       ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:17875665,
CC       ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:23297219,
CC       ECO:0000269|PubMed:26808625, ECO:0000269|PubMed:28472469,
CC       ECO:0000269|PubMed:29531043, ECO:0000269|PubMed:29735528,
CC       ECO:0000269|PubMed:9199372, 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};
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   PDBsum; 5YGD; -.
DR   PDBsum; 5YGF; -.
DR   SMR; Q9VKM1; -.
DR   BioGrid; 60588; 42.
DR   DIP; DIP-61694N; -.
DR   IntAct; Q9VKM1; 25.
DR   MINT; Q9VKM1; -.
DR   STRING; 7227.FBpp0079755; -.
DR   PaxDb; Q9VKM1; -.
DR   PRIDE; 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   eggNOG; KOG1042; Eukaryota.
DR   eggNOG; ENOG410XNRH; LUCA.
DR   InParanoid; Q9VKM1; -.
DR   KO; K02156; -.
DR   OMA; RMNPKQR; -.
DR   OrthoDB; 220258at2759; -.
DR   PhylomeDB; Q9VKM1; -.
DR   GenomeRNAi; 34521; -.
DR   PRO; PR:Q9VKM1; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0004872; Expressed in 9 organ(s), highest expression level in multi-cellular organism.
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; HDA:FlyBase.
DR   GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR   GO; GO:0043073; C:germ cell nucleus; IDA:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0031933; C:telomeric heterochromatin; IDA:FlyBase.
DR   GO; GO:0070725; C:Yb body; IPI:FlyBase.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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:0006342; P:chromatin silencing; IMP:FlyBase.
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: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:0070868; P:heterochromatin organization involved in chromatin silencing; 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:0031453; P:positive regulation of heterochromatin assembly; IMP:FlyBase.
DR   GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:FlyBase.
DR   GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR   GO; GO:0016441; P:posttranscriptional gene silencing; IMP:FlyBase.
DR   GO; GO:0016246; P:RNA interference; TAS: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   MOTIF           1..12
FT                   /note="Nuclear localization signal"
FT   ACT_SITE        614
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   ACT_SITE        685
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   METAL           589
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT   METAL           843
FT                   /note="Magnesium; via carboxylate"
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:0000244|PDB:5YGD"
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
//
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