DDX4_XENLA
ID DDX4_XENLA Reviewed; 700 AA.
AC Q91372;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
DE Short=xVLG1;
GN Name=ddx4 {ECO:0000250|UniProtKB:Q64060};
GN Synonyms=vlg1 {ECO:0000312|EMBL:AAC03114.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC03114.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary {ECO:0000269|PubMed:8150200};
RX PubMed=8150200; DOI=10.1006/dbio.1994.1093;
RA Komiya T., Itoh K., Ikenishi K., Furusawa M.;
RT "Isolation and characterization of a novel gene of the DEAD box protein
RT family which is specifically expressed in germ cells of Xenopus laevis.";
RL Dev. Biol. 162:354-363(1994).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RA Ikenishi K., Tanaka T.S., Komiya T.;
RT "Spatio-temporal distribution of the protein of Xenopus vasa homologue
RT (Xenopus vasa-like gene 1, XVLG1) in the embryos.";
RL Dev. Growth Differ. 38:527-535(1996).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=9338598; DOI=10.1046/j.1440-169x.1997.t01-4-00010.x;
RA Ikenishi K., Tanaka T.S.;
RT "Involvement of the protein of Xenopus vasa homolog (Xenopus vasa-like gene
RT 1, XVLG1) in the differentiation of primordial germ cells.";
RL Dev. Growth Differ. 39:625-633(1997).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10830432; DOI=10.1046/j.1440-169x.2000.00493.x;
RA Ikenishi K., Tanaka T.S.;
RT "Spatio-temporal expression of Xenopus vasa homolog, XVLG1, in oocytes and
RT embryos: the presence of XVLG1 RNA in somatic cells as well as germline
RT cells.";
RL Dev. Growth Differ. 42:95-103(2000).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=14706067; DOI=10.1111/j.1440-169x.2003.00708.x;
RA Ikenishi K., Yamakita S.;
RT "A trial for induction of supernumerary primordial germ cells in Xenopus
RT tadpoles by injecting RNA of Xenopus vasa homologue into germline cells of
RT 32-cell embryos.";
RL Dev. Growth Differ. 45:417-426(2003).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase required during
CC spermatogenesis (PubMed:14706067, PubMed:9338598). Required to repress
CC transposable elements and preventing their mobilization, which is
CC 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 cycle
CC (By similarity). {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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8150200}. Nucleus
CC {ECO:0000269|PubMed:8150200}. Note=Localizes to the cytoplasm of
CC somatic cells, primordial germ cells (PGCs) and most adult germline
CC cells, except spermatogonia where it is located in the nucleus
CC (PubMed:8150200). Component of the meiotic nuage, also named P granule,
CC a germ-cell-specific organelle required to repress transposon activity
CC during meiosis (By similarity). {ECO:0000250|UniProtKB:Q61496,
CC ECO:0000269|PubMed:8150200}.
CC -!- TISSUE SPECIFICITY: An mRNA and protein component of germ plasm and
CC primordial germ cells (PGCs). Doesn't appear to localize to the
CC mitochondrial cloud of early oocytes. In contrast to its germ plasm
CC localization, shows weak expression in the animal hemispheres of stage
CC 1-5 embryos. Expressed in spermatogonia, spermatocytes and, to a lower
CC extent, spermatids of the adult testis but not adult sperm. Expressed
CC in oogonia and oocytes of the adult ovary. Somatically expressed in
CC animal cells at the cleavage stages and in ecto- and mesodermal cells
CC from the gastrula stage onwards. Prominent in cells of the entochord
CC and somites from the neurula to the tail-bud stage, and in cells of
CC somites and spinal cord at subsequent stages until stage 46.
CC {ECO:0000269|PubMed:10830432, ECO:0000269|PubMed:8150200,
CC ECO:0000269|Ref.2}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed from stage I to stage III oocytes, with levels decreasing
CC throughout oocyte growth. Expression levels then increase from
CC unfertilized eggs through oocyte maturation.
CC {ECO:0000269|PubMed:10830432, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000250|UniProtKB:Q64060}.
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DR EMBL; AF046043; AAC03114.1; -; mRNA.
DR PIR; I51235; I51235.
DR RefSeq; NP_001081728.1; NM_001088259.1.
DR RefSeq; XP_018089220.1; XM_018233731.1.
DR RefSeq; XP_018089273.1; XM_018233784.1.
DR AlphaFoldDB; Q91372; -.
DR SMR; Q91372; -.
DR PRIDE; Q91372; -.
DR GeneID; 398019; -.
DR KEGG; xla:398019; -.
DR CTD; 398019; -.
DR Xenbase; XB-GENE-1016814; ddx4.L.
DR OMA; DVKQTIY; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398019; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR GO; GO:0045495; C:pole plasm; IDA: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: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:0007281; P:germ cell development; IMP:UniProtKB.
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:0048477; P:oogenesis; IEA:UniProtKB-KW.
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; Nucleus; Oogenesis;
KW Reference proteome; Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..700
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000248853"
FT DOMAIN 305..488
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 513..661
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 MOTIF 274..302
FT /note="Q motif"
FT MOTIF 432..435
FT /note="DEAD box"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT COMPBIAS 14..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 700 AA; 78240 MW; C504ECA38EFB0B7E CRC64;
MEENWDTEIE TEKPTYVPNF STLETENTDN YSAYSNNDIN NQNYDSERSF GNRGGYRSER
SRPSNFNRGS RTERGRGRGF GTNRNDNYSS ERDVFGDDER DQRRGFPGRG GYNGNEDGQK
PNAFRGRGGF RNENEQRRGF GERGGFRSEN GQRNFDNRGD FGNSGEEEDR PRSYGRGGFN
NSDTGGRGRR GGRGGGSQYG GYKGRNEEVG VESGKSQEEG NEKDEKPKKV TYIPPPPPDG
EDNIFRQYQS GINFDKYDEI LVDVTGKDVP PAILTFEEAN LCETLRRNVA RAGYVKLTPV
QKHSIPIIMA GRDLMACAQT GSGKTAAFLL PILSYMMNEG ITASQYLQLQ EPEAIIIAPT
RELINQIYLD ARKFSYGTCV RPVVVYGGIQ PVHAMRDVEK GCNILCATPG RLLDIVSKEK
IGLSKLRYLV LDEADRMLDM GFAPEIEKLM TKPGMPTKEK RQTLMFSATY PEEIRRLASN
YLKSEHLFVV VGLVGGACSD VAQTVLEMRE NGKMEKLLEI LKSSEKERTM IFVNTKKKAD
FIAGYLCQEK FSSTSIHGDR EQYQRESALW DFRTGKCTVI VCTAVAARGL DIENVQHVIN
YDVPKEVDEY VHRIGRTGRC GNTGKATSFF NVQDDHVIAR PLVKILTDAH QEVPAWLEEI
AFGGHGALNS FYAADSMGEQ AGGNAVTTPS FAQEEEASWD
