TDRD1_MOUSE
ID TDRD1_MOUSE Reviewed; 1172 AA.
AC Q99MV1; A2VDG6; Q6F3G0; Q8CDN7; Q8K1G3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Tudor domain-containing protein 1;
GN Name=Tdrd1;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Fetal gonad, and Testis;
RX PubMed=14550528; DOI=10.1016/s0925-4773(03)00181-3;
RA Chuma S., Hiyoshi M., Yamamoto A., Hosokawa M., Takamune K., Nakatsuji N.;
RT "Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
RT bodies/nuages in male germ cells and forms a complex with snRNPs.";
RL Mech. Dev. 120:979-990(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ICR; TISSUE=Testis;
RX PubMed=17038506; DOI=10.1073/pnas.0601878103;
RA Chuma S., Hosokawa M., Kitamura K., Kasai S., Fujioka M., Hiyoshi M.,
RA Takamune K., Noce T., Nakatsuji N.;
RT "Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
RT differentiation and nuage/germinal granule formation in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15894-15899(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-1172.
RC TISSUE=Ovary, and Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-1172.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH MAEL.
RX PubMed=16787967; DOI=10.1093/hmg/ddl158;
RA Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A.,
RA Cooke H.J.;
RT "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed
RT chromatin and microRNA pathway?";
RL Hum. Mol. Genet. 15:2324-2334(2006).
RN [7]
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-1019 AND GLU-1023.
RX PubMed=17141210; DOI=10.1016/j.ydbio.2006.10.046;
RA Hosokawa M., Shoji M., Kitamura K., Tanaka T., Noce T., Chuma S.,
RA Nakatsuji N.;
RT "Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
RT composition, intracellular localization, and function in male germ cells in
RT mice.";
RL Dev. Biol. 301:38-52(2007).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PIWIL2.
RX PubMed=19345100; DOI=10.1016/j.cub.2009.02.061;
RA Wang J., Saxe J.P., Tanaka T., Chuma S., Lin H.;
RT "Mili interacts with tudor domain-containing protein 1 in regulating
RT spermatogenesis.";
RL Curr. Biol. 19:640-644(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP PIWIL1; PIWIL2 AND PIWIL4.
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PIWIL2, AND DISRUPTION
RP PHENOTYPE.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=20439430; DOI=10.1101/gad.1902110;
RA Kuramochi-Miyagawa S., Watanabe T., Gotoh K., Takamatsu K., Chuma S.,
RA Kojima-Kita K., Shiromoto Y., Asada N., Toyoda A., Fujiyama A., Totoki Y.,
RA Shibata T., Kimura T., Nakatsuji N., Noce T., Sasaki H., Nakano T.;
RT "MVH in piRNA processing and gene silencing of retrotransposons.";
RL Genes Dev. 24:887-892(2010).
RN [13]
RP INTERACTION WITH TDRD12.
RX PubMed=24067652; DOI=10.1073/pnas.1316316110;
RA Pandey R.R., Tokuzawa Y., Yang Z., Hayashi E., Ichisaka T., Kajita S.,
RA Asano Y., Kunieda T., Sachidanandam R., Chuma S., Yamanaka S., Pillai R.S.;
RT "Tudor domain containing 12 (TDRD12) is essential for secondary PIWI
RT interacting RNA biogenesis in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:16492-16497(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 692-892 ALONE AND IN COMPLEX WITH
RP METHYLATED PEPTIDE, TUDOR DOMAINS, MUTAGENESIS OF ASN-325; TYR-774 AND
RP ASN-796, SUBUNIT, AND INTERACTION WITH PIWIL2.
RX PubMed=22996915; DOI=10.1261/rna.034181.112;
RA Mathioudakis N., Palencia A., Kadlec J., Round A., Tripsianes K.,
RA Sattler M., Pillai R.S., Cusack S.;
RT "The multiple Tudor domain-containing protein TDRD1 is a molecular scaffold
RT for mouse Piwi proteins and piRNA biogenesis factors.";
RL RNA 18:2056-2072(2012).
CC -!- FUNCTION: Plays a central role during spermatogenesis by participating
CC in the repression transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Acts via
CC the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and governs the methylation and subsequent
CC repression of transposons. Required for the localization of Piwi
CC proteins to the meiotic nuage. Involved in the piRNA metabolic process
CC by ensuring the entry of correct transcripts into the normal piRNA pool
CC and limiting the entry of cellular transcripts into the piRNA pathway.
CC May act by allowing the recruitment of piRNA biogenesis or loading
CC factors that ensure the correct entry of transcripts and piRNAs into
CC Piwi proteins. {ECO:0000269|PubMed:17038506,
CC ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}.
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC TDRD7 and DDX4. Interacts with MAEL. Interacts with PIWIL1, PIWIL2 and
CC PIWIL4 (when methylated on arginine residues). Interacts with TDRD12.
CC {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:17141210,
CC ECO:0000269|PubMed:19345100, ECO:0000269|PubMed:19465913,
CC ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:22996915,
CC ECO:0000269|PubMed:24067652}.
CC -!- INTERACTION:
CC Q99MV1; Q8CDG1: Piwil2; NbExp=6; IntAct=EBI-8573364, EBI-8573412;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14550528,
CC ECO:0000269|PubMed:17038506, ECO:0000269|PubMed:17141210,
CC ECO:0000269|PubMed:19345100, ECO:0000269|PubMed:19465913,
CC ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20439430}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis (PubMed:20439430). DDX4 is required for meiotic nuage
CC localization. Also present in chromatoid body.
CC {ECO:0000269|PubMed:20439430}.
CC -!- TISSUE SPECIFICITY: Testis and ovary specific. Present in germ-line
CC cells and is most abundant in fetal prospermatogonia and postnatal
CC primary spermatocytes (at protein level).
CC {ECO:0000269|PubMed:14550528}.
CC -!- DOMAIN: Tudor domains 2 and 3 have higher affinity for arginine-
CC methylated peptides, tudor domain 1 is a poor binder due to an impaired
CC aromatic cage.
CC -!- DISRUPTION PHENOTYPE: Male sterility because of postnatal spermatogenic
CC defects due to demethylation and subsequent derepression of
CC transposable elements. Piwi-associated small RNA profiles are altered,
CC piRNPs accepting the entry of abundant cellular transcripts into the
CC piRNA pathway and accumulating piRNAs with a profile that is
CC drastically different from wild-type. Piwi proteins are delocalized
CC from the nucleus to the cytoplasm. {ECO:0000269|PubMed:17038506,
CC ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}.
CC -!- SIMILARITY: Belongs to the TDRD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI29955.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI29956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK31970.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD27578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB067571; BAC02433.1; -; mRNA.
DR EMBL; AB183526; BAD27575.1; -; mRNA.
DR EMBL; AB183527; BAD27576.1; -; mRNA.
DR EMBL; AB183528; BAD27577.1; -; mRNA.
DR EMBL; AB183529; BAD27578.1; ALT_INIT; mRNA.
DR EMBL; AK029806; BAC26625.1; -; mRNA.
DR EMBL; AF285591; AAK31970.1; ALT_INIT; mRNA.
DR EMBL; BC129954; AAI29955.1; ALT_INIT; mRNA.
DR EMBL; BC129955; AAI29956.1; ALT_INIT; mRNA.
DR CCDS; CCDS29922.1; -.
DR RefSeq; NP_001002238.1; NM_001002238.2.
DR RefSeq; NP_001002240.1; NM_001002240.2.
DR RefSeq; NP_001002241.1; NM_001002241.2.
DR RefSeq; NP_113564.2; NM_031387.3.
DR PDB; 4B9W; X-ray; 2.10 A; A/B=692-892.
DR PDB; 4B9X; X-ray; 2.80 A; A=692-917.
DR PDBsum; 4B9W; -.
DR PDBsum; 4B9X; -.
DR AlphaFoldDB; Q99MV1; -.
DR SMR; Q99MV1; -.
DR BioGRID; 219947; 6.
DR CORUM; Q99MV1; -.
DR DIP; DIP-48523N; -.
DR IntAct; Q99MV1; 3.
DR MINT; Q99MV1; -.
DR STRING; 10090.ENSMUSP00000107231; -.
DR iPTMnet; Q99MV1; -.
DR PhosphoSitePlus; Q99MV1; -.
DR MaxQB; Q99MV1; -.
DR PaxDb; Q99MV1; -.
DR PeptideAtlas; Q99MV1; -.
DR PRIDE; Q99MV1; -.
DR ProteomicsDB; 262743; -.
DR Antibodypedia; 31923; 137 antibodies from 24 providers.
DR DNASU; 83561; -.
DR Ensembl; ENSMUST00000078723; ENSMUSP00000077785; ENSMUSG00000025081.
DR Ensembl; ENSMUST00000111604; ENSMUSP00000107231; ENSMUSG00000025081.
DR Ensembl; ENSMUST00000111606; ENSMUSP00000107233; ENSMUSG00000025081.
DR Ensembl; ENSMUST00000121249; ENSMUSP00000112786; ENSMUSG00000025081.
DR GeneID; 83561; -.
DR KEGG; mmu:83561; -.
DR UCSC; uc008hzi.1; mouse.
DR CTD; 56165; -.
DR MGI; MGI:1933218; Tdrd1.
DR VEuPathDB; HostDB:ENSMUSG00000025081; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00940000158754; -.
DR HOGENOM; CLU_010832_0_0_1; -.
DR InParanoid; Q99MV1; -.
DR OMA; EYCSAQK; -.
DR OrthoDB; 703199at2759; -.
DR PhylomeDB; Q99MV1; -.
DR BioGRID-ORCS; 83561; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Tdrd1; mouse.
DR PRO; PR:Q99MV1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99MV1; protein.
DR Bgee; ENSMUSG00000025081; Expressed in animal zygote and 42 other tissues.
DR Genevisible; Q99MV1; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0071546; C:pi-body; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR CDD; cd04508; TUDOR; 4.
DR Gene3D; 2.40.50.90; -; 4.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00567; TUDOR; 4.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00333; TUDOR; 4.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Differentiation; Meiosis;
KW Metal-binding; Reference proteome; Repeat; RNA-mediated gene silencing;
KW Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..1172
FT /note="Tudor domain-containing protein 1"
FT /id="PRO_0000183162"
FT DOMAIN 307..367
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 536..595
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 756..815
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 982..1040
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT ZN_FING 163..199
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MUTAGEN 325
FT /note="N->Y: Strongly enhanced binding to symmetric
FT dimethylarginines."
FT /evidence="ECO:0000269|PubMed:22996915"
FT MUTAGEN 774
FT /note="Y->N: Strongly reduced binding to symmetric
FT dimethylarginines."
FT /evidence="ECO:0000269|PubMed:22996915"
FT MUTAGEN 796
FT /note="N->A: Significantly reduced binding to symmetric
FT dimethylarginines."
FT /evidence="ECO:0000269|PubMed:22996915"
FT MUTAGEN 1019
FT /note="Y->N: Abolishes localization to meiotic nuage; when
FT associated with K-1023."
FT /evidence="ECO:0000269|PubMed:17141210"
FT MUTAGEN 1023
FT /note="E->K: Abolishes localization to meiotic nuage; when
FT associated with N-1019."
FT /evidence="ECO:0000269|PubMed:17141210"
FT CONFLICT 903
FT /note="A -> G (in Ref. 3; BAC26625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1128
FT /note="I -> T (in Ref. 5; AAI29956/AAI29955)"
FT /evidence="ECO:0000305"
FT STRAND 709..719
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 722..727
FT /evidence="ECO:0007829|PDB:4B9W"
FT HELIX 732..748
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 762..766
FT /evidence="ECO:0007829|PDB:4B9W"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 773..781
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 787..791
FT /evidence="ECO:0007829|PDB:4B9W"
FT TURN 792..794
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:4B9W"
FT HELIX 802..804
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:4B9W"
FT HELIX 810..813
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 820..828
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:4B9W"
FT HELIX 836..846
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 851..859
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 862..869
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 871..874
FT /evidence="ECO:0007829|PDB:4B9W"
FT HELIX 878..884
FT /evidence="ECO:0007829|PDB:4B9W"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:4B9W"
SQ SEQUENCE 1172 AA; 129696 MW; EF42786CAD71933D CRC64;
MMPRNNLEAS TCKMAEPFNF EKKESKPPPQ DPLRSPVAQH NHPTFRLKSP ENGNTKNNFL
LCEQNKQYLA SQEDSSVVSS NPAVVNGEVG GSKGDRKPPP TGNPVSPLSL GNSSPPNQVK
TKPSSNVTPE KSKKSHKLFE NALSVNNPAL FNSLGPPLRS TTCHRCGLFG SLRCSQCKQT
YYCSTACQRR DWSSHSTICR PVQQSLNKLE DNKSPFETKA IEVKSEVDCP PGVTKEITAG
AERVMFSDLR SLQLKKTMEI KGTVTEFKHP SNFYIQLYSS EVLENMNQLS TSLKETYANV
VPEDGYLPVK GEVCVAKYTV DQTWNRAIVQ AVDVLQRKAH VLYIDYGNEE MIPIDSVHPL
SRGLDLFPPS AIKCCVSGVI PTAGEWSEGC VAAVKALLFE QFCSVKVMDI LEEEVLTCAV
DLVLQSSGKQ LDHVLVEMGY GVKPGEQSST EQSVDHSALE DVGRVTVESK IVTDRNALIP
KVLTLNVGDE FCGVVAHIQT PEDFFCQQLQ SGHKLAELQE SLSEYCGHVI PRSDFYPTIG
DVCCAQFSED DQWYRASVLA YASEESVLVG YVDYGNFEIL SLKRLCPIIP KLLDLPMQAL
NCVLAGVKPS LGIWTPEAVC VMKEMVQNRM VTVRVVGMLG TRALVELIDK SVAPHVSASK
ALIDSGFAIK EKDVADKGSS MHTASVPLAI EGPAEALEWT WVEFTVDETV DVVVCMMYSP
GEFYCHFLKD DALEKLDDLN QSLADYCAQK PPNGFKAEIG RPCCAFFSGD GNWYRALVKE
ILPSGNVKVH FVDYGNVEEV TTDQLQAILP QFLLLPFQGM QCWLVDIQPP NKHWTKEATA
RFQACVVGLK LQARVVEITA NGVGVELTDL STPYPKIISD VLIREQLVLR CGSPQDSLMS
RPANQHKQID SHRVQASPSA EQWKTMELPV NKTIAANVLE IISPALFYAI PSEMSENQEK
LCVLAAELLE HCNAQKGQPA YRPRTGDACC AKYTNDDFWY RAIVLETSES DVKVLYADYG
NIETLPLSRV QPIPASHLEL PFQIIRCSLE GPMELNGSCS QLVMELLRNA MLNQSVVLSV
KAISKNVHAV SVEKCSENGM INIAENLVMC GLAENLTSKR KSASTKEIPH SRDCCCTELQ
KQIEKHEQIL LFLLNNPTNQ SKFTEMKKLL RS
