GenomeNet

Database: UniProt
Entry: Q1XG89
LinkDB: Q1XG89
Original site: Q1XG89 
ID   TDR12_BOMMO             Reviewed;        1759 AA.
AC   Q1XG89; H9JJS3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   16-OCT-2019, entry version 60.
DE   RecName: Full=Putative ATP-dependent RNA helicase TDRD12;
DE            EC=3.6.4.13;
DE   AltName: Full=RNA helicase-like protein {ECO:0000312|EMBL:BAE93115.1};
DE   AltName: Full=Tudor domain-containing protein 12;
DE            Short=BmTdrd12;
GN   Name=TDRD12; Synonyms=RHL;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Bombycoidea; Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   SIWI.
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.,
RA   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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T;
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx
RT   mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAE93115.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 264-1170, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=p50T; TISSUE=Egg {ECO:0000269|PubMed:17098166};
RX   PubMed=17098166; DOI=10.1016/j.ibmb.2006.09.002;
RA   Sawada H., Yamahama Y., Yamamoto T., Mase K., Ogawa H., Iino T.;
RT   "A novel RNA helicase-like protein during early embryonic development
RT   in silkworm Bombyx mori: molecular characterization and intracellular
RT   localization.";
RL   Insect Biochem. Mol. Biol. 36:911-920(2006).
RN   [4]
RP   FUNCTION, AND IDENTIFICATION IN THE PET COMPLEX.
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
RT   cytosolic targets of the mouse piRNA pathway.";
RL   Mol. Cell 61:138-152(2016).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase required during
CC       spermatogenesis to repress transposable elements and preventing
CC       their mobilization, which is essential for the germline integrity.
CC       Acts via the piRNA metabolic process, which mediates the
CC       repression of transposable elements during meiosis by forming
CC       complexes composed of piRNAs and Piwi proteins and governs the
CC       methylation and subsequent repression of transposons.
CC       {ECO:0000305|PubMed:26669262}.
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   -!- SUBUNIT: Interacts (via Tudor domain 2) with Siwi
CC       (PubMed:24067652). Component of the PET complex, at least composed
CC       of EXD1, SIWI, TDRD12 and piRNAs (PubMed:26669262).
CC       {ECO:0000269|PubMed:24067652, ECO:0000269|PubMed:26669262}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:17098166}.
CC       Cytoplasm, cytosol {ECO:0000269|PubMed:17098166}. Nucleus membrane
CC       {ECO:0000269|PubMed:17098166}; Peripheral membrane protein.
CC       Note=At 36 hours after oviposition, detected in the nucleus and
CC       the cytosol where it is associated with chromosomes and to the
CC       surface of the nuclear membrane (PubMed:17098166). Component of
CC       the meiotic nuage, also named P granule, a germ-cell-specific
CC       organelle required to repress transposon activity during meiosis
CC       (PubMed:24067652). {ECO:0000269|PubMed:17098166,
CC       ECO:0000269|PubMed:24067652}.
CC   -!- TISSUE SPECIFICITY: Expressed in the yolk cells. Not detected in
CC       yolk granules. {ECO:0000269|PubMed:17098166}.
CC   -!- DEVELOPMENTAL STAGE: Detected in non-diapause eggs through all
CC       stages of development. Detected only from 0-12 hours after
CC       oviposition in diapause eggs. Also expressed in diapause eggs
CC       following artificial diapause termination.
CC       {ECO:0000269|PubMed:17098166}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE93115.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AB252573; BAE93115.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001037005.1; NM_001043540.1.
DR   SMR; Q1XG89; -.
DR   STRING; 7091.BGIBMGA009774-TA; -.
DR   PRIDE; Q1XG89; -.
DR   GeneID; 692554; -.
DR   KEGG; bmor:692554; -.
DR   CTD; 91646; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   eggNOG; KOG2279; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; Q1XG89; -.
DR   KO; K18409; -.
DR   OrthoDB; 66196at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR   GO; GO:1990923; C:PET complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51203; CS; 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   ATP-binding; Chromosome; Complete proteome; Cytoplasm;
KW   Developmental protein; Differentiation; Helicase; Hydrolase; Meiosis;
KW   Membrane; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW   RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN         1   1759       Putative ATP-dependent RNA helicase
FT                                TDRD12.
FT                                /FTId=PRO_0000407281.
FT   DOMAIN       74    153       Tudor 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   DOMAIN      611    789       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      823    980       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1335   1394       Tudor 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   DOMAIN     1618   1704       CS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00547}.
FT   NP_BIND     624    631       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   CONFLICT    270    270       S -> A (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    297    297       K -> E (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT    331    331       K -> N (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT    395    395       D -> N (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT    493    493       D -> G (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT    664    666       SKS -> IKI (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT    784    784       P -> L (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT    857    857       N -> S (in Ref. 3; BAE93115).
FT                                {ECO:0000305}.
FT   CONFLICT   1534   1534       A -> P (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT   1545   1546       EY -> DN (in Ref. 1; no nucleotide
FT                                entry). {ECO:0000305}.
SQ   SEQUENCE   1759 AA;  199878 MW;  DD4636E9819B548B CRC64;
     MASDYYQVEI LHYLNPNLIW VEVLNSPNEI SFEQLGVYGI LPIDASLDVE RPGLKLQRSE
     DWMPATAILM KNIFQNLEQV WFSPTHIDRR SSIFDNNIHK YGELIIKKNG VQLYLSKELV
     KAGLATEDPC QFHQYMSLGK IKTKLSNTET RAVIKNLEEY YRKSSKPKEL WQKSVHQNTS
     IFHAGERLQA LTVKNLERHN NRQNIMLLEN KLKDLEQCKG SDEVSLGRGV CRVPSNKSEM
     VMLTNKRLKN RLELLSKINM KSDATDAVKS TKRNFSGDGQ RKNFENDFES DDESVKKVSI
     ANTINTSDGS ANVVDKLLDE KQIDNVFNNK KQICYTESTR RNPVKKAACI VYGPPSINID
     KLPLKEAPKM TKTVKWTPHV DCDKEASEVS FGDVDSHVKL DVKNLDKFHE IADRIEIEKT
     IPVDVNIHKD LYDSMINNKN ESESKIMETA NLKTEMKNLR KSSILQSKLK QFDKFNVSSN
     SAASESSTKS SMDSSRISDE DDLSSDDEMS EIMETFKLNL ATPKKSEAKH TIDHIEVNNT
     KLNANPFKNL DGSKSVFVDK LTSPVLLVHT KRNNKVQPCS LLRDVPFGTS IHVVLRNMGI
     KHPTRLQTVS WGTILRGLST FLISPPRSGK TMGYLPAVCR LVRDFRKESP DSCGPKCIIV
     CATSKSVSEV ERISKMLLGL EDKVFACYSG MDNLSVTTAL LNGCDLLICT PKSIVRLLQN
     DLSVDLRDLT TFVVDDCERI SDVYSNEVKY VLYEIKNMLK NRVNKELKVQ IVVASRIWCD
     FLEPIVLKAP DSVVCIGAFQ ELILYSKIST TVDFLRPENK IANVLQFIDS VQGPKRTVVV
     CRADNEVKAV ESSLRYNNRV VFACDNTMNI HDLYNLNVVW GDFEDPTLGP ILVCCDSNLV
     HLNVTDASYL IHYSLPALFS TFCKRFSVLN DNYPSIFKNE SRDLKVKVLM DESNVEQLPK
     ILNFLKRCTE NVPKILDEVS EKILNEKDLA KVKDLVPLCD NLLSLGICPD TWNCTERHRI
     FKECDSPADW IPKNGVVTFQ ILYFHSAVMY SARLLSNTVD GETTKYPQTY STLSLKMGMY
     FSKESSRRLH GIPMVGDVCA VSKKQNFFIR CQVVKIISFY KNGNPNYVVI KLIDEEKFEQ
     SRDIYLYHLP DEFKDMKTYV VQVRLANIQP QDKDITFSCL AKNELEKIVE KNEDLFMRGH
     VAMSVGSCIF VDTLEACLDL SSLSETVVRH NFKQELLNAH AVPNPKHLSI LEEMCEKSGL
     IVKAVTNEQV VPKPIPVLPA AQWAHLEDDL SSVYLASVED MDKLFVRLVK FESCMKLLNI
     EINKYVSENT VPLDGSNVGD IVLAKFPDDS MYERARIDHI YSEDKVKCFF VDQGDWRDVS
     TNDLATITEN FITQLPFQAI ECRLIGIRPF GEQWTEFSTN WFSDHCFEDA KGNLKHLYVK
     HFTKEKADCT GGHKYGVALI DTYTNEDIIV NQLLIDLNLA KENVDEIAYL SEIKCNKTVL
     NNDATVDEEE GSLSGVSEPE SNINVPLDKV FLKAPIRSVP LVDSEYETSD SDTWQINRPE
     DFKALFMRTR PESSKIIPMI TANEVQNNAD GETSKDTSTI LEEKGQLPEK VKDDELKLSK
     PKICWSQNKN TVKLKILIAG IEDYKLKIED RAVAFSANHC DVEYGFKLEL YGVVDVNKSR
     HSNKGQYVLV TMTKLMCRNW LALTKEGDSQ KWIVYDVDTI EASSDEEVYR DDTLEVIKNI
     HNTNNGSDSE DDDFLDDVS
//
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