TDR12_BOMMO
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 03-AUG-2022, entry version 70.
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; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC 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., 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 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 in
RT 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 cytosolic
RT 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 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. {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 (PubMed:24067652).
CC Component of the PET complex, at least composed of EXD1, SIWI, TDRD12
CC and piRNAs (PubMed:26669262). {ECO:0000269|PubMed:24067652,
CC 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. Note=At 36
CC hours after oviposition, detected in the nucleus and the cytosol where
CC it is associated with chromosomes and to the surface of the nuclear
CC membrane (PubMed:17098166). Component of the meiotic nuage, also named
CC P granule, a germ-cell-specific organelle required to repress
CC transposon activity during meiosis (PubMed:24067652).
CC {ECO:0000269|PubMed:17098166, ECO:0000269|PubMed:24067652}.
CC -!- TISSUE SPECIFICITY: Expressed in the yolk cells. Not detected in yolk
CC granules. {ECO:0000269|PubMed:17098166}.
CC -!- DEVELOPMENTAL STAGE: Detected in non-diapause eggs through all stages
CC of development. Detected only from 0-12 hours after oviposition in
CC diapause eggs. Also expressed in diapause eggs following artificial
CC diapause termination. {ECO:0000269|PubMed:17098166}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE93115.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB252573; BAE93115.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001037005.1; NM_001043540.1.
DR AlphaFoldDB; Q1XG89; -.
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 HOGENOM; CLU_238314_0_0_1; -.
DR InParanoid; Q1XG89; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
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; Cytoplasm; Developmental protein; Differentiation;
KW Helicase; Hydrolase; Meiosis; Membrane; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1759
FT /note="Putative ATP-dependent RNA helicase TDRD12"
FT /id="PRO_0000407281"
FT DOMAIN 74..153
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 611..789
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 823..980
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1335..1394
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1618..1704
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 480..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 624..631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 270
FT /note="S -> A (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="K -> E (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="K -> N (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="D -> N (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="D -> G (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 664..666
FT /note="SKS -> IKI (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="P -> L (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="N -> S (in Ref. 3; BAE93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 1534
FT /note="A -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1545..1546
FT /note="EY -> DN (in Ref. 1; no nucleotide entry)"
FT /evidence="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
