GenomeNet

Database: UniProt
Entry: Q14BI7
LinkDB: Q14BI7
Original site: Q14BI7 
ID   TDRD9_MOUSE             Reviewed;        1383 AA.
AC   Q14BI7; B1Q3J8; Q14AW6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 3.
DT   16-OCT-2019, entry version 110.
DE   RecName: Full=ATP-dependent RNA helicase TDRD9 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000305|PubMed:28633017};
DE   AltName: Full=Tudor domain-containing protein 9 {ECO:0000305};
GN   Name=Tdrd9 {ECO:0000312|MGI:MGI:1921941};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Shoji M., Tanaka T., Kitamura K., Hosokawa M., Kato Y., Kondoh G.,
RA   Okawa K., Sasaki H., Chuma S., Nakatsuji N.;
RT   "Regulation of retroelement expression and genome dna methylation
RT   through conserved TDRD9/SPN-E function in the germline.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH PIWIL4.
RX   PubMed=20059948; DOI=10.1016/j.devcel.2009.10.012;
RA   Shoji M., Tanaka T., Hosokawa M., Reuter M., Stark A., Kato Y.,
RA   Kondoh G., Okawa K., Chujo T., Suzuki T., Hata K., Martin S.L.,
RA   Noce T., Kuramochi-Miyagawa S., Nakano T., Sasaki H., Pillai R.S.,
RA   Nakatsuji N., Chuma S.;
RT   "The TDRD9-MIWI2 complex is essential for piRNA-mediated
RT   retrotransposon silencing in the mouse male germline.";
RL   Dev. Cell 17:775-787(2009).
RN   [5]
RP   INTERACTION WITH PIWIL1 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
RT   arginine methylation in specifying interaction with Tudor family
RT   members.";
RL   Genes Dev. 23:1749-1762(2009).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20011505; DOI=10.1371/journal.pgen.1000764;
RA   Aravin A.A., van der Heijden G.W., Castaneda J., Vagin V.V.,
RA   Hannon G.J., Bortvin A.;
RT   "Cytoplasmic compartmentalization of the fetal piRNA pathway in
RT   mice.";
RL   PLoS Genet. 5:E1000764-E1000764(2009).
RN   [7]
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   GLU-257.
RX   PubMed=28633017; DOI=10.1016/j.devcel.2017.05.021;
RA   Wenda J.M., Homolka D., Yang Z., Spinelli P., Sachidanandam R.,
RA   Pandey R.R., Pillai R.S.;
RT   "Distinct roles of RNA helicases MVH and TDRD9 in PIWI slicing-
RT   triggered mammalian piRNA biogenesis and function.";
RL   Dev. Cell 41:623-637(2017).
CC   -!- FUNCTION: ATP-binding RNA helicase which plays a central role
CC       during spermatogenesis by repressing transposable elements and
CC       preventing their mobilization, which is essential for the germline
CC       integrity (PubMed:20059948, PubMed:28633017). Acts via the piRNA
CC       metabolic process, which mediates the repression of transposable
CC       elements during meiosis by forming complexes composed of piRNAs
CC       and Piwi proteins and governs the methylation and subsequent
CC       repression of transposons (PubMed:20059948, PubMed:28633017). Acts
CC       downstream of piRNA biogenesis: exclusively required for
CC       transposon silencing in the nucleus, suggesting that it acts as a
CC       nuclear effector in the nucleus together with PIWIL4
CC       (PubMed:28633017). {ECO:0000269|PubMed:20059948,
CC       ECO:0000269|PubMed:28633017}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000305|PubMed:28633017};
CC   -!- SUBUNIT: Interacts with piRNA-associated proteins PIWIL1 and
CC       PIWIL4. {ECO:0000269|PubMed:19584108,
CC       ECO:0000269|PubMed:20059948}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20011505,
CC       ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}. Nucleus
CC       {ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}.
CC       Note=Component of the nuage, also named P granule, a germ-cell-
CC       specific organelle required to repress transposon activity during
CC       meiosis. Specifically localizes to piP-bodies, a subset of the
CC       nuage which contains secondary piRNAs. PIWIL2 is required for its
CC       localization to piP-bodies. {ECO:0000269|PubMed:20059948}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q14BI7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14BI7-2; Sequence=VSP_033554;
CC       Name=3;
CC         IsoId=Q14BI7-3; Sequence=VSP_033553, VSP_033555;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in reproductive
CC       organs. Detected in mitotic spermatogonia, meiotic spermatocytes
CC       (predominantly at the pachytene stage), haploid spermatids in the
CC       testis, and in growing oocytes in the ovary (at protein level).
CC       {ECO:0000269|PubMed:20059948}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable but show male sterility with
CC       chromosome synapsis failure. In fetal testes, LINE-1 (L1)
CC       transposable elements derepression and an aberrant piRNA profile
CC       in prospermatogonia, followed by cognate DNA demethylation are
CC       observed. {ECO:0000269|PubMed:20059948}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
DR   EMBL; AB362563; BAG15992.1; -; mRNA.
DR   EMBL; AC112520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115831; AAI15832.1; -; mRNA.
DR   EMBL; BC116656; AAI16657.1; -; mRNA.
DR   CCDS; CCDS49184.1; -. [Q14BI7-1]
DR   RefSeq; NP_083332.1; NM_029056.1. [Q14BI7-1]
DR   RefSeq; XP_006516384.1; XM_006516321.3. [Q14BI7-2]
DR   SMR; Q14BI7; -.
DR   BioGrid; 216946; 1.
DR   IntAct; Q14BI7; 1.
DR   STRING; 10090.ENSMUSP00000078022; -.
DR   iPTMnet; Q14BI7; -.
DR   PhosphoSitePlus; Q14BI7; -.
DR   PaxDb; Q14BI7; -.
DR   PRIDE; Q14BI7; -.
DR   Ensembl; ENSMUST00000079009; ENSMUSP00000078022; ENSMUSG00000054003. [Q14BI7-1]
DR   GeneID; 74691; -.
DR   KEGG; mmu:74691; -.
DR   UCSC; uc007pei.1; mouse. [Q14BI7-1]
DR   UCSC; uc007pej.1; mouse. [Q14BI7-3]
DR   CTD; 122402; -.
DR   MGI; MGI:1921941; Tdrd9.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   GeneTree; ENSGT00940000157035; -.
DR   HOGENOM; HOG000047965; -.
DR   InParanoid; Q14BI7; -.
DR   KO; K18408; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; Q14BI7; -.
DR   TreeFam; TF324869; -.
DR   ChiTaRS; Tdrd9; mouse.
DR   PRO; PR:Q14BI7; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000054003; Expressed in 40 organ(s), highest expression level in female gonad.
DR   ExpressionAtlas; Q14BI7; baseline and differential.
DR   Genevisible; Q14BI7; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0071547; C:piP-body; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IMP:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0009566; P:fertilization; IMP:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR   GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   Gene3D; 2.40.50.90; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW   Developmental protein; Differentiation; Helicase; Hydrolase; Meiosis;
KW   Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN         1   1383       ATP-dependent RNA helicase TDRD9.
FT                                /FTId=PRO_0000333814.
FT   DOMAIN      144    310       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      378    545       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      945   1005       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   NP_BIND     157    164       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       256    259       DEAH box. {ECO:0000269|PubMed:28633017}.
FT   VAR_SEQ       1    772       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_033553.
FT   VAR_SEQ       1    401       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_033554.
FT   VAR_SEQ     773    813       PKTTVVLKHIPPYGFLYYKQLQSLFRQCGQVKSIVFDGAKA
FT                                -> MDIGTKCTSQVAAGVTAWHLWRRSGPGRLADSEESCGV
FT                                PRA (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_033555.
FT   MUTAGEN     257    257       E->Q: In Tdrd9(KI); heterozygous and
FT                                homozygous knockin male mice are
FT                                infertile due to derepression of
FT                                transposable elements. PiRNA biogenesis
FT                                in not affected but piRNAs fail to
FT                                accumulate in the nucleus.
FT                                {ECO:0000269|PubMed:28633017}.
SQ   SEQUENCE   1383 AA;  155980 MW;  55946F4F639B5777 CRC64;
     MLRKLTVDQI NDWFTIGKTV TNVELLGLPP AFPAEAPREE VQRSEEVPNE DPTAQAQVPV
     KATAPARPAS TSGRSLSQRS SEMEYINKYR QLEEQELDIY GQDQPPSGPG LRSPLAKLSN
     VACIPETTYK YPDLPINRCK EEVISLIESN SVVIIHGATG SGKSTQLPQY VLDHYTQRSA
     FCNIVVTQPR KIGASSIARW ISKERSWTLG GLVGYQVGLE KIATEDTRLI YMTTGVLLQK
     IVSAKSLMEF THIFIDEVHE RTEEMDFLLL VVRKLLRTNS RFVKVVLMSA TINCKQFADY
     FAVPVQNKMN PAYVFEVEGK PHAIEEYYLN DLGHIYHSGL PYRLEEPVIT KDVYEVAVSL
     IQMFDDLDMK ESGNKTWSGA QFVSERSSVL VFLPGLGEIN YMHELLTNMI HKRLQVYPLH
     SSVTLEEQNN VFLSPVPGYR KIILSTNIAE SSVTVPDVKY VIDFCLTRTL VCDEDTNYQS
     LRLSWASKTS CDQRKGRAGR VSKGYCYRLI PRDFWDSAIP DHVVPEMLRC PLGSTILKVK
     LLDMGEPRAL LATALSPPSL SDIERTILLL KEVGALAVSG QREDENPHDG ELTFLGRVLA
     QLPVSQQLGK LVVLGHVFGC LDECLIIAAA LSLKNFFTMP FRQHLDGYRN KVHFSGSSRS
     DCLALVEAFR AWQACRQRGE LRRPKDELDW GRLNYIQIKR IREVAELYEE LKNRISQFNM
     FVGPHHPVLD QEYPYKQRFI LQVVLAGAFY PNYFTFGQPD EEMAVRELAG KDPKTTVVLK
     HIPPYGFLYY KQLQSLFRQC GQVKSIVFDG AKAFVEFSRN PTERFKTLPA VNLAVKMSQL
     KVSLELSVHA AEEIEGKVQG GSVSKLRNTR VNVDFQKQTV DPMQVSFNTL DRPRTVADLL
     LTIDVTEVVE VGHFWGYRID ERNAELLKQL TAEINRLELV PLPIHPHPDL VCLAPFTDYN
     KESYFRAQIL YVSGNSAEVF FVDYGNRSHV DLDLLREIPC QFLELPFQAL EFKICKMRPS
     AKSLICGEHW SGGAHGRFAA LVGGCPLLVK VFSIVHSVLH VDVYRYSGAQ DAVNVRDVLI
     REGYAELAEE SYESKQSYEV LKGFFAKSVD TMPDGSVSSP LKDDEKHLLR ILLESFASNR
     LGAPNCKAVL HGPFNPYELK CHSLTRISKF RCVWIEKESI NSVVISDSPA DLHQRMLVAA
     SLSVNETGST MLLRETSLMP HIPGLPALLS MLFAPVMELR VDREGKCYTG VLCGLGWNSA
     TEAPILPEHD IELAFDVRLN VEDIVEINIL RAAINKLVCD GPNGSKYLGP ERIAQLQENA
     RQKLLGLFCR LKPREKITPQ WHEKPYEWNQ VDPRLIMEQA EPEGSPGKST SLYQLHTPVV
     LSP
//
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