PIWL4_MOUSE
ID PIWL4_MOUSE Reviewed; 848 AA.
AC Q8CGT6; A6P4B9; A6X963; A6X964; Q8CC75;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Piwi-like protein 4;
DE Short=mAgo5;
GN Name=Piwil4; Synonyms=Miwi2 {ECO:0000303|PubMed:18381894};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=12414724; DOI=10.1101/gad.1026102;
RA Carmell M.A., Xuan Z., Zhang M.Q., Hannon G.J.;
RT "The Argonaute family: tentacles that reach into RNAi, developmental
RT control, stem cell maintenance, and tumorigenesis.";
RL Genes Dev. 16:2733-2742(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18381894; DOI=10.1101/gad.1640708;
RA Kuramochi-Miyagawa S., Watanabe T., Gotoh K., Totoki Y., Toyoda A.,
RA Ikawa M., Asada N., Kojima K., Yamaguchi Y., Ijiri T.W., Hata K., Li E.,
RA Matsuda Y., Kimura T., Okabe M., Sakaki Y., Sasaki H., Nakano T.;
RT "DNA methylation of retrotransposon genes is regulated by Piwi family
RT members MILI and MIWI2 in murine fetal testes.";
RL Genes Dev. 22:908-917(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 667-848 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17395546; DOI=10.1016/j.devcel.2007.03.001;
RA Carmell M.A., Girard A., van de Kant H.J.G., Bourc'his D., Bestor T.H.,
RA de Rooij D.G., Hannon G.J.;
RT "MIWI2 is essential for spermatogenesis and repression of transposons in
RT the mouse male germline.";
RL Dev. Cell 12:503-514(2007).
RN [6]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18922463; DOI=10.1016/j.molcel.2008.09.003;
RA Aravin A.A., Sachidanandam R., Bourc'his D., Schaefer C., Pezic D.,
RA Toth K.F., Bestor T., Hannon G.J.;
RT "A piRNA pathway primed by individual transposons is linked to de novo DNA
RT methylation in mice.";
RL Mol. Cell 31:785-799(2008).
RN [7]
RP METHYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH TDRD1; TDRKH AND
RP TDRD9.
RX PubMed=19584108; DOI=10.1101/gad.1814809;
RA Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT "Proteomic analysis of murine Piwi proteins reveals a role for arginine
RT methylation in specifying interaction with Tudor family members.";
RL Genes Dev. 23:1749-1762(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19465913; DOI=10.1038/nsmb.1615;
RA Reuter M., Chuma S., Tanaka T., Franz T., Stark A., Pillai R.S.;
RT "Loss of the Mili-interacting Tudor domain-containing protein-1 activates
RT transposons and alters the Mili-associated small RNA profile.";
RL Nat. Struct. Mol. Biol. 16:639-646(2009).
RN [9]
RP INTERACTION WITH MOV10L1.
RX PubMed=20534472; DOI=10.1073/pnas.1003953107;
RA Zheng K., Xiol J., Reuter M., Eckardt S., Leu N.A., McLaughlin K.J.,
RA Stark A., Sachidanandam R., Pillai R.S., Wang P.J.;
RT "Mouse MOV10L1 associates with Piwi proteins and is an essential component
RT of the Piwi-interacting RNA (piRNA) pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11841-11846(2010).
RN [10]
RP INTERACTION WITH MOV10L1.
RX PubMed=20547853; DOI=10.1073/pnas.1007158107;
RA Frost R.J., Hamra F.K., Richardson J.A., Qi X., Bassel-Duby R., Olson E.N.;
RT "MOV10L1 is necessary for protection of spermatocytes against
RT retrotransposons by Piwi-interacting RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11847-11852(2010).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ASP-688.
RX PubMed=22020280; DOI=10.1038/nature10547;
RA De Fazio S., Bartonicek N., Di Giacomo M., Abreu-Goodger C., Sankar A.,
RA Funaya C., Antony C., Moreira P.N., Enright A.J., O'Carroll D.;
RT "The endonuclease activity of Mili fuels piRNA amplification that silences
RT LINE1 elements.";
RL Nature 480:259-263(2011).
RN [12]
RP INTERACTION WITH TDRKH.
RX PubMed=23714778; DOI=10.1038/emboj.2013.121;
RA Saxe J.P., Chen M., Zhao H., Lin H.;
RT "Tdrkh is essential for spermatogenesis and participates in primary piRNA
RT biogenesis in the germline.";
RL EMBO J. 32:1869-1885(2013).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=25038252; DOI=10.1093/nar/gku620;
RA Keam S.P., Young P.E., McCorkindale A.L., Dang T.H., Clancy J.L.,
RA Humphreys D.T., Preiss T., Hutvagner G., Martin D.I., Cropley J.E.,
RA Suter C.M.;
RT "The human Piwi protein Hiwi2 associates with tRNA-derived piRNAs in
RT somatic cells.";
RL Nucleic Acids Res. 42:8984-8995(2014).
RN [14]
RP FUNCTION.
RX PubMed=26669262; DOI=10.1016/j.molcel.2015.11.009;
RA Yang Z., Chen K.M., Pandey R.R., Homolka D., Reuter M., Janeiro B.K.,
RA Sachidanandam R., Fauvarque M.O., McCarthy A.A., Pillai R.S.;
RT "PIWI slicing and EXD1 drive biogenesis of nuclear piRNAs from cytosolic
RT targets of the mouse piRNA pathway.";
RL Mol. Cell 61:138-152(2016).
RN [15]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=32381626; DOI=10.1101/gad.335489.119;
RA Yang F., Lan Y., Pandey R.R., Homolka D., Berger S.L., Pillai R.S.,
RA Bartolomei M.S., Wang P.J.;
RT "TEX15 associates with MILI and silences transposable elements in male germ
RT cells.";
RL Genes Dev. 34:745-750(2020).
RN [16]
RP INTERACTION WITH TEX15, AND SUBCELLULAR LOCATION.
RX PubMed=32719317; DOI=10.1038/s41467-020-17372-5;
RA Schoepp T., Zoch A., Berrens R.V., Auchynnikava T., Kabayama Y.,
RA Vasiliauskaite L., Rappsilber J., Allshire R.C., O'Carroll D.;
RT "TEX15 is an essential executor of MIWI2-directed transposon DNA
RT methylation and silencing.";
RL Nat. Commun. 11:3739-3739(2020).
RN [17]
RP INTERACTION WITH SPOCD1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=32674113; DOI=10.1038/s41586-020-2557-5;
RA Zoch A., Auchynnikava T., Berrens R.V., Kabayama Y., Schoepp T., Heep M.,
RA Vasiliauskaite L., Perez-Rico Y.A., Cook A.G., Shkumatava A.,
RA Rappsilber J., Allshire R.C., O'Carroll D.;
RT "SPOCD1 is an essential executor of piRNA-directed de novo DNA
RT methylation.";
RL Nature 584:635-639(2020).
CC -!- FUNCTION: Plays a central role during spermatogenesis by repressing
CC transposable elements and preventing their mobilization, which is
CC essential for the germline integrity (PubMed:17395546, PubMed:18381894,
CC PubMed:18922463, PubMed:26669262, PubMed:22020280). Acts via the piRNA
CC metabolic process, which mediates the repression of transposable
CC elements during meiosis by forming complexes composed of piRNAs and
CC Piwi proteins and governs the methylation and subsequent repression of
CC transposons (PubMed:17395546, PubMed:18381894, PubMed:18922463,
CC PubMed:26669262, PubMed:22020280). Directly binds piRNAs, a class of 24
CC to 30 nucleotide RNAs that are generated by a Dicer-independent
CC mechanism and are primarily derived from transposons and other repeated
CC sequence elements. Associates with secondary piRNAs antisense and
CC PIWIL2/MILI is required for such association (PubMed:17395546,
CC PubMed:18381894, PubMed:18922463, PubMed:26669262, PubMed:22020280).
CC The piRNA process acts upstream of known mediators of DNA methylation
CC (PubMed:17395546, PubMed:18381894, PubMed:18922463, PubMed:26669262,
CC PubMed:22020280). Does not show endonuclease activity
CC (PubMed:22020280). Plays a key role in the piRNA amplification loop,
CC also named ping-pong amplification cycle, by acting as a 'slicer-
CC incompetent' component that loads cleaved piRNAs from the 'slicer-
CC competent' component PIWIL2 and target them on genomic transposon loci
CC in the nucleus (PubMed:22020280). In addition to its role in germline,
CC PIWIL4 also plays a role in the regulation of somatic cells activities.
CC Plays a role in pancreatic beta cell function and insulin secretion (By
CC similarity). Involved in maintaining cell morphology and functional
CC integrity of retinal epithelial through Akt/GSK3alpha/beta signaling
CC pathway (By similarity). {ECO:0000250|UniProtKB:Q4G033,
CC ECO:0000250|UniProtKB:Q7Z3Z4, ECO:0000269|PubMed:17395546,
CC ECO:0000269|PubMed:18381894, ECO:0000269|PubMed:18922463,
CC ECO:0000269|PubMed:22020280, ECO:0000269|PubMed:26669262}.
CC -!- SUBUNIT: Interacts with PRMT5 and WDR77 (PubMed:19584108). Interacts
CC (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2 and
CC TDRD9 (PubMed:19584108, PubMed:23714778). Interacts with MOV10L1
CC (PubMed:20534472, PubMed:20547853). Interacts with TEX15
CC (PubMed:32719317). Interacts with SPOCD1 (PubMed:32674113).
CC {ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20534472,
CC ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:23714778,
CC ECO:0000269|PubMed:32674113, ECO:0000269|PubMed:32719317}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922463,
CC ECO:0000269|PubMed:32381626, ECO:0000269|PubMed:32674113,
CC ECO:0000269|PubMed:32719317}. Cytoplasm {ECO:0000269|PubMed:18922463,
CC ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}.
CC Note=Probable component of the meiotic nuage, also named P granule, a
CC germ-cell-specific organelle required to repress transposon activity
CC during meiosis. PIWIL2/MILI is required for nuclear localization.
CC {ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19465913,
CC ECO:0000269|PubMed:19584108}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CGT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGT6-2; Sequence=VSP_018376;
CC Name=3;
CC IsoId=Q8CGT6-3; Sequence=VSP_036666;
CC -!- TISSUE SPECIFICITY: Detected in male germ cells beginning around 14.5-
CC 15.5 dpc but is absent from female germ cells (PubMed:18922463,
CC PubMed:25038252). From 15.5 dpc and until birth, it is present in male
CC germ cells. Not detected in somatic cells of the embryonic gonad.
CC Expression declines soon after birth, reaching undetectable levels in 4
CC day-old mice (at protein level). {ECO:0000269|PubMed:18922463,
CC ECO:0000269|PubMed:25038252}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in male embryonic germ cells at
CC embryonic day 16.5 and expression decreases by postnatal day 2.5.
CC {ECO:0000269|PubMed:32381626, ECO:0000269|PubMed:32674113}.
CC -!- PTM: Arginine methylation by PRMT5 is required for the interaction with
CC Tudor domain-containing protein (TDRD1, TDRKH/TDRD2 and TDRD9) and
CC subsequent localization to the meiotic nuage, also named P granule.
CC {ECO:0000269|PubMed:19584108}.
CC -!- DISRUPTION PHENOTYPE: Males show spermatogenesis defects due to
CC demethylation and subsequent derepression of transposable elements.
CC Meiotic-progression is impaired during early prophase of meiosis I,
CC followed by a marked and progressive loss of germ cells with age.
CC {ECO:0000269|PubMed:17395546, ECO:0000269|PubMed:18381894}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN75583.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC28462.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAO77951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY135692; AAN75583.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB258534; BAF65667.1; -; mRNA.
DR EMBL; CT030247; CAO77949.1; -; Genomic_DNA.
DR EMBL; CT030247; CAO77951.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK033746; BAC28462.1; ALT_FRAME; mRNA.
DR CCDS; CCDS22824.2; -. [Q8CGT6-1]
DR RefSeq; NP_808573.2; NM_177905.3.
DR AlphaFoldDB; Q8CGT6; -.
DR SMR; Q8CGT6; -.
DR BioGRID; 237040; 1.
DR iPTMnet; Q8CGT6; -.
DR PhosphoSitePlus; Q8CGT6; -.
DR PeptideAtlas; Q8CGT6; -.
DR PRIDE; Q8CGT6; -.
DR DNASU; 330890; -.
DR UCSC; uc009oet.1; mouse. [Q8CGT6-1]
DR UCSC; uc009oev.1; mouse. [Q8CGT6-3]
DR MGI; MGI:3041167; Piwil4.
DR VEuPathDB; HostDB:ENSMUSG00000036912; -.
DR HOGENOM; CLU_008813_2_0_1; -.
DR InParanoid; Q8CGT6; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; Q8CGT6; -.
DR TreeFam; TF354206; -.
DR BioGRID-ORCS; 330890; 3 hits in 61 CRISPR screens.
DR PRO; PR:Q8CGT6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CGT6; protein.
DR Genevisible; Q8CGT6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0071547; C:piP-body; IDA:UniProtKB.
DR GO; GO:0034584; F:piRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Meiosis; Methylation; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Spermatogenesis; Translation regulation.
FT CHAIN 1..848
FT /note="Piwi-like protein 4"
FT /id="PRO_0000234573"
FT DOMAIN 263..379
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 541..834
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 761
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18381894"
FT /id="VSP_036666"
FT VAR_SEQ 811..848
FT /note="GLISVPAPCQYAHKLTFLVAQSVHKEPSLELANNLFYL -> SCHGIQAALK
FT PVTVPLPQLLSTGTMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018376"
FT MUTAGEN 688
FT /note="D->A: In DAH mutant; does not lead to arrest in
FT meiotic prophase and failure of transposon piRNA
FT amplification."
FT /evidence="ECO:0000269|PubMed:22020280"
FT CONFLICT 644
FT /note="W -> R (in Ref. 2; BAF65667)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="N -> D (in Ref. 2; BAF65667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 95773 MW; 907DB987D47947FD CRC64;
MSGRARVRAR GITTGHSARE VGRSSRDLMV TSASPGDSEA GGGTSVISQP YELGVSSGDG
GRTFMERRGK GRQDFEELGV CTREKLTHVK DCKTGSSGIP VRLVTNLFNL DLPQDWQLYQ
YHVTYSPDLA SRRLRIALLY NHSILSDKAK AFDGASLFLS EKLDQKVTEL TSETQRGETI
KITLTLTSKL FPNSPVCIQF FNVIFRKILK NLSMYQIGRN FYKPSEPVEI PQYKLSLWPG
FAISVSHFES KLLFNADVNY KVLRNETVLD FMTDLCLRTG MSCFTEMCHK QLVGLVVLTR
YNNKTYRIDD IDWSVKPTQA FQKRDGSEVT YVDYYKQQYD ITLSDLNQPV LVSLLKRKRN
DNSEPQMVHL MPELCFLTGL SSQATSDFRL MKAVAEETRL SPVGRQQQLA RLVDDIQRNP
VARFELETWG LHFGSQLSLT GRVVPSEKIL LQDHTCQPAF AADWSKDMRS CKVLSSQPLN
RWLIVCCNRA EHLIEAFLSC LRRVGGSMGF NVGYPKIIKV DETPAAFLRA IQVHGDPDVQ
LVMCILPSNQ KNYYDSIKKY LSSDCPVPSQ CVLTRTLNKQ GTMLSVATKI AMQMTCKLGG
ELWSVEIPLK SLMVVGIDIC RDALNKNVVV VGFVASINSR ITRWFSRCVL QRTAADIADC
LKVCMTGALN RWYRHNHDLP ARIVVYRDGV GNGQLKAVLE YEVPQLLKSV TECGSDARSC
RLSVVVVRKR CLLRLFASTD HTVQNPPLGT VVDSEATRPE WYDFYLISQT ANRGTVSPTH
YNVIYDDNAL KPDHMQRLTF KLCHLYYNWQ GLISVPAPCQ YAHKLTFLVA QSVHKEPSLE
LANNLFYL
