DDX4_PIG
ID DDX4_PIG Reviewed; 722 AA.
AC Q6GWX0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 AltName: Full=Vasa-like protein;
GN Name=DDX4; Synonyms=VASA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee G.;
RT "Characterization of porcine VASA homolog gene.";
RL Submitted (MAY-2004) 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; AY626785; AAT46129.1; -; mRNA.
DR AlphaFoldDB; Q6GWX0; -.
DR SMR; Q6GWX0; -.
DR STRING; 9823.ENSSSCP00000026827; -.
DR PaxDb; Q6GWX0; -.
DR PeptideAtlas; Q6GWX0; -.
DR PRIDE; Q6GWX0; -.
DR eggNOG; KOG0335; Eukaryota.
DR InParanoid; Q6GWX0; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0033391; C:chromatoid body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
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: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: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: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..722
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000054980"
FT DOMAIN 317..500
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 528..673
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..245
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250|UniProtKB:Q9NQI0"
FT REGION 702..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 286..314
FT /note="Q motif"
FT MOTIF 444..447
FT /note="DEAD box"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64060"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
SQ SEQUENCE 722 AA; 78810 MW; 5C7BC665863604C2 CRC64;
MGDEDWEAEI NPHVSSYVPI FEKDGYSGEN GDKFNRTTAS SSEMDDGPSG RDHFMKSGFT
SGRSYGKRDA GESNKRENTS TTGGFGVGKS FGNRGFSNNR FEDGDSSGFW RESTNDCEDN
TTRNRGFSKR GGSRDGNKSE ASGPFRRGGR GSFRGCRGGF GLGSQNSELD PDQGMQRGGG
LFGSGRPAAS DTGNGDTYQS RSGRGRGGYK GLNEEVVTGS GKNSWKSEAE GGESSDTQGP
KVTYIPPPPP EDEDSIFAHY QTGINFDKYD TILVEVSGHD APPAILTFEE ANLCQTLNNN
IAKAGYTKLT PVQKYSIPII LAGRDLMACA QTGSGKTAAF LLPILAHMMH DGITASRFKE
LQEPECIIVA PTRELVNQIY LEARKFSFGT CVRAVVIYGG TQLGHSIRQI VQGCNILCAT
PGRLMDIIGK EKIGLKQIKY LVLDEADRML DMGFGPEMKK LISCPGMPSK EQRQTLMFSA
TFPEEIQRLA AEFLKSNYLF VAVGQVGGAC RDVQQADLQV GQYSKREKLL EILRNIGDER
TMVFVETKKK ADFIATFLCQ EKISTTSIHG DREQREREQA LGDFRFGKCP VLVATSVAAR
GLDIENVQHV INFDLPSTID EYVHRIGRTG RCGNTGRAIS FFDLESDNHL AQPLVKVLTD
AQQDVPAWLE EIAFSTYIPG FSGSTRGNVF ASVDTRKGKS TLNTAGFSSS QAPNPVDDES
WD
