DDX4_BOVIN
ID DDX4_BOVIN Reviewed; 729 AA.
AC Q5W5U4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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;
GN Name=DDX4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Bartholomew R.A., Parks J.E.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF541971; AAQ11373.1; -; mRNA.
DR RefSeq; NP_001007820.1; NM_001007819.1.
DR AlphaFoldDB; Q5W5U4; -.
DR SMR; Q5W5U4; -.
DR STRING; 9913.ENSBTAP00000011682; -.
DR PaxDb; Q5W5U4; -.
DR PRIDE; Q5W5U4; -.
DR GeneID; 493725; -.
DR KEGG; bta:493725; -.
DR CTD; 54514; -.
DR eggNOG; KOG0335; Eukaryota.
DR InParanoid; Q5W5U4; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0033391; C:chromatoid body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
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:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
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:0007283; P:spermatogenesis; ISS:UniProtKB.
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 2: Evidence at transcript 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..729
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000244562"
FT DOMAIN 321..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 532..677
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 22..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250|UniProtKB:Q9NQI0"
FT REGION 706..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..318
FT /note="Q motif"
FT MOTIF 448..451
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 78..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64060"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
SQ SEQUENCE 729 AA; 79443 MW; 2E0B9A147EAC0734 CRC64;
MGDEDWEAEI IKPHISSYVP VFEKDRYSSG ANGDTFNRTP ASSSEMGDGS SRRDHFMRSG
FASGRSLGNR DPGESNKREN TSTVGGFGVG KSFGNRGFSN NKFEEGDSSG FWRESSIDCE
DNQTRNRGFS KRGGYQDGND SEALGSSRRG GRGSFRGCRG GFGRGSPNSD YEQDEGTQRS
GGIFGSRRSA LSGAGNGDTF QSRSGGGSGR GGYKGLNEEV ITGSGKNSWK SEAEGGESGD
TQGPKVTYIP PPPPEDEDSI FAHYQTGINF DKYDTILVEV SGHDPPPAIL TFEEANLCQT
LNNNIAKAGY TKLTPVQKYS IPIIQGGRDL MACAQTGSGK TAAFLLPILA HMMRDGITAS
RFKELQEPEC IIVAPTRELI NQIYLEARKF SFGTCVRAVV IYGGTQLGHS IRQIVQGCNI
LCATPGRLMD VIGKEKIGLR QVKYLVLDEA DRMLDMGFGP EMKKLISCPG MPSKEQRQTL
MFSATFPEEI QRLAGEFLKS NYLFVAVGQV GGACRDVQQT ILQVGQYSKR EKLVEILRNI
GDERTMVFVE TKKKADFIAT FLCQEKISTT SIHGDREQRE REQALGDFRC GKCPVLVATS
VAARGLDIEN VQHVINFDLP STIDEYVHRI GRTGRCGNTG RAISFFDLES DSQLAQPLVK
VLSDAQQDVP AWLEEIAFST YGPGFSGNAR GNVFASVDTR KNYPGKSSLN TAGFSSTQAP
NPVDDESWD
