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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
 
 
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