DDX3_DROME
ID DDX3_DROME Reviewed; 798 AA.
AC Q9VHP0; Q8SXI8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=ATP-dependent RNA helicase bel;
DE EC=3.6.4.13;
DE AltName: Full=Protein belle;
GN Name=bel {ECO:0000312|EMBL:AAF54262.1}; ORFNames=CG9748;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15572142; DOI=10.1016/j.ydbio.2004.09.009;
RA Johnstone O., Deuring R., Bock R., Linder P., Fuller M.T., Lasko P.;
RT "Belle is a Drosophila DEAD-box protein required for viability and in the
RT germ line.";
RL Dev. Biol. 277:92-101(2005).
RN [2] {ECO:0000312|EMBL:AAF54262.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAF54262.1};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF54262.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAL90351.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL90351.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16531407; DOI=10.1074/jbc.m513868200;
RA Ulvila J., Parikka M., Kleino A., Sormunen R., Ezekowitz R.A., Kocks C.,
RA Ramet M.;
RT "Double-stranded RNA is internalized by scavenger receptor-mediated
RT endocytosis in Drosophila S2 cells.";
RL J. Biol. Chem. 281:14370-14375(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-179; SER-214;
RP SER-219 AND SER-638, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: ATP-dependent RNA helicase that is essential and required for
CC cellular function, larval growth, and for male and female fertility.
CC Also required for RNA interference (RNAi), double-stranded RNA induces
CC potent and specific gene silencing, by acting downstream of dsRNA
CC internalization. RNAi is mediated by the RNA-induced silencing complex
CC (RISC), a sequence-specific, multicomponent nuclease that destroys or
CC silences messenger RNAs homologous to the silencing trigger.
CC {ECO:0000269|PubMed:15572142, ECO:0000269|PubMed:16531407}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15572142}. Note=In
CC nurse cells, follicle cells, and within the oocyte. Vas and bel
CC colocalize in the perinuclear region of nurse cells.
CC -!- TISSUE SPECIFICITY: Vas and bel colocalize in nuage (perinuclear,
CC electron-dense granules in germline cells) and at the oocyte posterior
CC during oogenesis. {ECO:0000269|PubMed:15572142}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, highest
CC expression in second larval instar and adult females.
CC {ECO:0000269|PubMed:15572142}.
CC -!- DISRUPTION PHENOTYPE: Flies are recessive lethal with a larval growth
CC defect phenotype. Hypomorphic bel mutants are male-sterile due to
CC defects in spermatogenesis and female sterile as oogenesis usually
CC arrests around stages 8-9 and egg chambers completely degenerate.
CC {ECO:0000269|PubMed:15572142}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000255}.
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DR EMBL; AE014297; AAF54262.1; -; Genomic_DNA.
DR EMBL; AY089613; AAL90351.1; -; mRNA.
DR RefSeq; NP_536783.1; NM_080522.4.
DR AlphaFoldDB; Q9VHP0; -.
DR SMR; Q9VHP0; -.
DR BioGRID; 69908; 26.
DR IntAct; Q9VHP0; 26.
DR STRING; 7227.FBpp0081374; -.
DR iPTMnet; Q9VHP0; -.
DR PaxDb; Q9VHP0; -.
DR PRIDE; Q9VHP0; -.
DR ABCD; Q9VHP0; 2 sequenced antibodies.
DR EnsemblMetazoa; FBtr0081888; FBpp0081374; FBgn0263231.
DR GeneID; 45826; -.
DR KEGG; dme:Dmel_CG9748; -.
DR UCSC; CG9748-RA; d. melanogaster.
DR CTD; 100035747; -.
DR FlyBase; FBgn0263231; bel.
DR VEuPathDB; VectorBase:FBgn0263231; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000168275; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q9VHP0; -.
DR OMA; CYRSWVR; -.
DR PhylomeDB; Q9VHP0; -.
DR BRENDA; 3.6.4.13; 1994.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 45826; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 45826; -.
DR PRO; PR:Q9VHP0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0263231; Expressed in seminal fluid secreting gland and 30 other tissues.
DR ExpressionAtlas; Q9VHP0; baseline and differential.
DR Genevisible; Q9VHP0; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0035072; P:ecdysone-mediated induction of salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0002168; P:instar larval development; IMP:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
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; 1.
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; Nucleotide-binding; Oogenesis; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..798
FT /note="ATP-dependent RNA helicase bel"
FT /id="PRO_0000270580"
FT DOMAIN 326..515
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 542..693
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 16..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 295..323
FT /note="Q motif"
FT /evidence="ECO:0000255"
FT MOTIF 459..462
FT /note="DEAD box"
FT /evidence="ECO:0000255"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 315..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 339..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 513
FT /note="I -> T (in Ref. 4; AAL90351)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="G -> S (in Ref. 4; AAL90351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 85081 MW; 516A9C8BEF8F8017 CRC64;
MSNAINQNGT GLEQQVAGLD LNGGSADYSG PITSKTSTNS VTGGVYVPPH LRGGGGNNNA
ADAESQGQGQ GQGQGFDSRS GNPRQETRDP QQSRGGGGEY RRGGGGGGRG FNRQSGDYGY
GSGGGGRRGG GGRFEDNYNG GEFDSRRGGD WNRSGGGGGG GRGFGRGPSY RGGGGGSGSN
LNEQTAEDGQ AQQQQQPRND RWQEPERPAG FDGSEGGQSA GGNRSYNNRG ERGGGGYNSR
WKEGGGSNVD YTKLGARDER LEVELFGVGN TGINFDKYED IPVEATGQNV PPNITSFDDV
QLTEIIRNNV ALARYDKPTP VQKHAIPIII NGRDLMACAQ TGSGKTAAFL VPILNQMYEL
GHVPPPQSTR QYSRRKQYPL GLVLAPTREL ATQIFEEAKK FAYRSRMRPA VLYGGNNTSE
QMRELDRGCH LIVATPGRLE DMITRGKVGL ENIRFLVLDE ADRMLDMGFE PQIRRIVEQL
NMPPTGQRQT LMFSATFPKQ IQELASDFLS NYIFLAVGRV GSTSENITQT ILWVYEPDKR
SYLLDLLSSI RDGPEYTKDS LTLIFVETKK GADSLEEFLY QCNHPVTSIH GDRTQKEREE
ALRCFRSGDC PILVATAVAA RGLDIPHVKH VINFDLPSDV EEYVHRIGRT GRMGNLGVAT
SFFNEKNRNI CSDLLELLIE TKQEIPSFME DMSSDRGHGG AKRAGRGGGG RYGGGFGSRD
YRQSSGGGGG GRSGPPPRSG GSGSGGGGGS YRSNGNSYGG NSGGGGYYGG GAGGGSYGGS
YGGGSASHSS NAPDWWAQ
