DDX4_RAT
ID DDX4_RAT Reviewed; 713 AA.
AC Q64060;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX4;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q61496};
DE AltName: Full=DEAD box protein 4;
DE AltName: Full=Vasa homolog;
DE Short=rVLG;
GN Name=Ddx4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=7857296; DOI=10.1006/bbrc.1995.1202;
RA Komiya T., Tanigawa Y.;
RT "Cloning of a gene of the DEAD box protein family which is specifically
RT expressed in germ cells in rats.";
RL Biochem. Biophys. Res. Commun. 207:405-410(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to
CC repress transposable elements and preventing their mobilization, which
CC is essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC governs the methylation and subsequent repression of transposons.
CC Involved in the secondary piRNAs metabolic process, the production of
CC piRNAs in fetal male germ cells through a ping-pong amplification
CC cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase
CC activity enables utilization of one of the slice cleavage fragments
CC generated by PIWIL2 and processing these pre-piRNAs into piRNAs.
CC {ECO:0000250|UniProtKB:Q61496}.
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:0000250|UniProtKB:Q61496};
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC TDRD7 and DDX4. Interacts with RANBP9. Interacts with RANBP10.
CC Interacts with PIWIL2 and MAEL. Interacts with ARNTL/BMAL1 and CLOCK.
CC Interacts with Tex19.1 and, probably, Tex19.2.
CC {ECO:0000250|UniProtKB:Q61496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q61496}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}.
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. {ECO:0000250|UniProtKB:Q61496}.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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DR EMBL; S75275; AAB33364.1; -; mRNA.
DR PIR; JC2534; JC2534.
DR RefSeq; NP_001071115.1; NM_001077647.1.
DR AlphaFoldDB; Q64060; -.
DR SMR; Q64060; -.
DR STRING; 10116.ENSRNOP00000013035; -.
DR iPTMnet; Q64060; -.
DR PhosphoSitePlus; Q64060; -.
DR jPOST; Q64060; -.
DR PaxDb; Q64060; -.
DR PRIDE; Q64060; -.
DR GeneID; 310090; -.
DR KEGG; rno:310090; -.
DR CTD; 54514; -.
DR RGD; 1308793; Ddx4.
DR eggNOG; KOG0335; Eukaryota.
DR InParanoid; Q64060; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; Q64060; -.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR PRO; PR:Q64060; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0033391; C:chromatoid body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW Hydrolase; Meiosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..713
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000054981"
FT DOMAIN 304..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 515..660
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 23..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..232
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250|UniProtKB:Q9NQI0"
FT REGION 689..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..301
FT /note="Q motif"
FT MOTIF 431..434
FT /note="DEAD box"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
SQ SEQUENCE 713 AA; 77955 MW; A31A4542EF7237F6 CRC64;
MGDEDWEAEI LKPHVSSYVP VFEKDKYSSG ANGDTFNRTS ASSSEMEDGP SGRDHFMRSG
FSSGRNLGNR DIGESSKRET TSTTGGFGRG KGFGNRGFLN NKFEEGDSSG FWKESTNDCE
DTQTRSRGFS KRGGYPDGND SEASGPFRRG GRDSEYDQDQ GSQRGGGLFG SRKPAASDSG
SGDTFQSRSG NARGAYKGLN EEVVTGSGKN SWKSEAEGGE SSDIQGPKVT YIPPPPPEDE
DSIFAHYQTG INFDKYDTIL VEVSGHDAPP AILTFEEANL CQTLNNNIAK AGYTKLTPVQ
KYSIPIVLAG RDLMACAQTG SGKTAAFLLP ILAHMMRDGI TASRFKELQE PECIIVAPTR
ELINQIYLEA RKFSFGTCVR AVVIYGGTQF GHSIRQIVQG CNILCATPGR LMDIIGKEKI
GLKQVKYLVL DEADRMLDMG FGPEMKKLIS CPGMPSKEQR QTLLFSATFP EEIQRLAGEF
LKSNYLFVAV GQVGGACRDV QQSILQVGPV FKKRKLVEIL RNIGDERPMV FVETKKKADF
IATFLCQEKI STTSIHGDRE QREREQALGD FRCGKCPVLV ATSVAARGLD IENVQHVINF
NLPSTIDEYV HRIGRTGRCG NTGRAISFFD TESDNHLAQP LVKVLSDAQQ DVPAWLEEIA
FSSYAPPSFS NSTRGAVFAS FDTRKNFQGK NTLNTAGISS AQAPNPVDDE SWD
