ID DDX4_MACFA Reviewed; 725 AA.
AC Q4R5S7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 84.
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;
GN Name=DDX4; ORFNames=QtsA-21246;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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 BMAL1 and CLOCK.
CC Interacts with Tex19.1 and, probably, Tex19.2. Interacts with RBM46.
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; AB169466; BAE01548.1; -; mRNA.
DR RefSeq; NP_001270270.1; NM_001283341.1.
DR AlphaFoldDB; Q4R5S7; -.
DR SMR; Q4R5S7; -.
DR STRING; 9541.ENSMFAP00000042985; -.
DR eggNOG; KOG0335; Eukaryota.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000233100; Unplaced.
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:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA processing; ISS:UniProtKB.
DR GO; GO:0141006; P:piRNA-mediated retrotransposon silencing by heterochromatin formation; ISS:UniProtKB.
DR GO; GO:0141007; P:siRNA-mediated retrotransposon silencing by heterochromatin formation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd18052; DEADc_DDX4; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF143; ATP-DEPENDENT RNA HELICASE DDX4-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..725
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000054978"
FT DOMAIN 320..503
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 531..676
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..248
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250|UniProtKB:Q9NQI0"
FT REGION 702..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 289..317
FT /note="Q motif"
FT MOTIF 447..450
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 77..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64060"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
SQ SEQUENCE 725 AA; 79168 MW; 5780C6A6BB44C17D CRC64;
MGDEDWEAEI NPHMSSYVPI FEKDRYSSGE NGDNFNRTPT SSSEMDDGPS RRDHFMKSGF
ASGRNFGNRD AGESNKRDNT STMGGFGVGK SFGNRGFSNS KFEDGDSSGF WRESSNDCED
NPTRNRGFSK RGGYRDGNNS EASGPSRRGG RSSFRGCRGG FGLGSPNNDL DPDECMQRTG
GLFGSRRPAL SGTGNGDTSQ SRSGSGSERG GYKGLNEEVI TGSGKNSWKS EAEGGESSDT
QGPKVTYIPP PPPEDEDSIF AHYQTGISFD KYDTILVEVS GHDAPPAILT FEEANLCQTL
NNNIAKAGYT KLTPVQKYSI PIILAGRDLM ACAQTGSGKT AAFLLPILAH MMHDGITASC
FKELQEPECI IVAPTRELVN QIYLEARKFS FGTCVRAVVI YGGTQLGHSI RQIVQGCNIL
CATPGRLMDI IGKEKIGLKQ IKYLVLDEAD RMLDMGFGPE MKKLISCPGM PSKEQRQTLM
FSATFPEEIQ RLAAEFLKSN YLFVAVGQVG GACRDVQQTV LQVGQFSKRE KLVEILRNIG
DERTMVFVET KKKADFIATF LCQEKISTTS IHGDREQRER EQALGDFRCG KCPVLVATSV
AARGLDIENV QHVINFDLPS TIDEYVHRIG RTGRCGNTGR AISFFDLESD NHLAQPLVKV
LTDAQQDVPA WLEEIAFSTY IPGFSGSTRG NVFASVDTRK GKSSLNTAGF SSSQAPNPVD
DESWD
//
