DDX17_DROME
ID DDX17_DROME Reviewed; 719 AA.
AC P19109; A4V2H1; Q6AWN9; Q8IGL7; Q95TB8; Q9I7P5; Q9VNK4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=ATP-dependent RNA helicase p62;
DE EC=3.6.4.13;
GN Name=Rm62; Synonyms=Dmp68, p62; ORFNames=CG10279;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
RC TISSUE=Embryo;
RX PubMed=2170937; DOI=10.1093/nar/18.18.5489;
RA Dorer D.R., Christensen A.C., Johnson D.H.;
RT "A novel RNA helicase gene tightly linked to the Triplo-lethal locus of
RT Drosophila.";
RL Nucleic Acids Res. 18:5489-5494(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND D).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INTERACTION WITH FMR1.
RX PubMed=12368261; DOI=10.1101/gad.1022002;
RA Ishizuka A., Siomi M.C., Siomi H.;
RT "A Drosophila fragile X protein interacts with components of RNAi and
RT ribosomal proteins.";
RL Genes Dev. 16:2497-2508(2002).
RN [7]
RP FUNCTION IN ANTIVIRAL DEFENSE, AND DISRUPTION PHENOTYPE.
RX PubMed=25126784; DOI=10.1016/j.cell.2014.06.023;
RA Moy R.H., Cole B.S., Yasunaga A., Gold B., Shankarling G., Varble A.,
RA Molleston J.M., tenOever B.R., Lynch K.W., Cherry S.;
RT "Stem-loop recognition by DDX17 facilitates miRNA processing and antiviral
RT defense.";
RL Cell 158:764-777(2014).
CC -!- FUNCTION: As an RNA helicase, unwinds RNA and alters RNA structures
CC through ATP binding and hydrolysis. Involved in multiple cellular
CC processes, including pre-mRNA splicing, alternative splicing, rRNA
CC processing and miRNA processing, as well as transcription regulation
CC (By similarity) (PubMed:12368261). Plays a role in innate immunity.
CC Specifically restricts bunyavirus infection, including Rift Valley
CC fever virus (RVFV) or La Crosse virus (LACV), but not vesicular
CC stomatitis virus (VSV), in an interferon- and DROSHA-independent manner
CC (PubMed:25126784). {ECO:0000250|UniProtKB:Q92841,
CC ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:25126784}.
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:Q92841};
CC -!- SUBUNIT: Interacts with Fmr1 to form the RNA-induced silencing complex
CC (RISC), a ribonucleoprotein (RNP) complex involved in translation
CC regulation, other components of the complex are RpL5, RpL11, AGO2 and
CC Dcr-1. {ECO:0000269|PubMed:12368261}.
CC -!- INTERACTION:
CC P19109; Q9NFU0: Fmr1; NbExp=4; IntAct=EBI-200734, EBI-422631;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92841}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q92841}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q92841}. Note=In the course of bunyavirus
CC infection, relocalizes from the nucleus to the cytosol where it binds
CC viral RNA to antagonize replication. {ECO:0000250|UniProtKB:Q92841}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=P19109-1; Sequence=Displayed;
CC Name=C; Synonyms=B, F;
CC IsoId=P19109-2; Sequence=VSP_007413, VSP_007415;
CC Name=D;
CC IsoId=P19109-3; Sequence=VSP_007414;
CC Name=E;
CC IsoId=P19109-4; Sequence=VSP_007413, VSP_007416;
CC -!- DISRUPTION PHENOTYPE: No phenotype under normal conditions. Upon
CC infection with Rift Valley fever virus (RVFV) or La Crosse virus
CC (LACV), knockdown flies exhibit increased mortality. No phenotype upon
CC infection with other viruses, including vesicular stomatitis virus
CC (VSV), Sindbis virus (SINV), nor Drosophila C virus (DCV).
CC {ECO:0000269|PubMed:25126784}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; X52846; CAA37037.1; -; mRNA.
DR EMBL; AE014297; AAF51926.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF51927.2; -; Genomic_DNA.
DR EMBL; AE014297; AAG22212.1; -; Genomic_DNA.
DR EMBL; AE014297; AAG22213.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN14331.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14332.1; -; Genomic_DNA.
DR EMBL; BT001716; AAN71471.1; -; mRNA.
DR EMBL; BT011476; AAR99134.1; -; mRNA.
DR EMBL; BT015209; AAT94438.1; -; mRNA.
DR PIR; S11485; S11485.
DR RefSeq; NP_001163528.1; NM_001170057.1. [P19109-3]
DR RefSeq; NP_001189182.1; NM_001202253.2. [P19109-4]
DR RefSeq; NP_524243.2; NM_079519.2. [P19109-1]
DR RefSeq; NP_731031.1; NM_169118.1. [P19109-3]
DR RefSeq; NP_731032.1; NM_169119.3. [P19109-4]
DR RefSeq; NP_731033.1; NM_169120.1. [P19109-2]
DR RefSeq; NP_731034.1; NM_169121.2. [P19109-2]
DR RefSeq; NP_731035.2; NM_169122.1. [P19109-2]
DR AlphaFoldDB; P19109; -.
DR SMR; P19109; -.
DR BioGRID; 65943; 46.
DR DIP; DIP-17867N; -.
DR IntAct; P19109; 36.
DR MINT; P19109; -.
DR STRING; 7227.FBpp0078301; -.
DR PaxDb; P19109; -.
DR PRIDE; P19109; -.
DR DNASU; 40739; -.
DR EnsemblMetazoa; FBtr0078649; FBpp0078298; FBgn0003261. [P19109-2]
DR EnsemblMetazoa; FBtr0078650; FBpp0078299; FBgn0003261. [P19109-3]
DR EnsemblMetazoa; FBtr0078651; FBpp0078300; FBgn0003261. [P19109-2]
DR EnsemblMetazoa; FBtr0078652; FBpp0078301; FBgn0003261. [P19109-1]
DR EnsemblMetazoa; FBtr0078653; FBpp0078302; FBgn0003261. [P19109-4]
DR EnsemblMetazoa; FBtr0078654; FBpp0078303; FBgn0003261. [P19109-2]
DR EnsemblMetazoa; FBtr0301947; FBpp0291159; FBgn0003261. [P19109-3]
DR EnsemblMetazoa; FBtr0302597; FBpp0291753; FBgn0003261. [P19109-4]
DR GeneID; 40739; -.
DR KEGG; dme:Dmel_CG10279; -.
DR UCSC; CG10279-RC; d. melanogaster.
DR CTD; 40739; -.
DR FlyBase; FBgn0003261; Rm62.
DR VEuPathDB; VectorBase:FBgn0003261; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000170749; -.
DR HOGENOM; CLU_003041_16_7_1; -.
DR InParanoid; P19109; -.
DR PhylomeDB; P19109; -.
DR BRENDA; 3.6.4.13; 1994.
DR SignaLink; P19109; -.
DR BioGRID-ORCS; 40739; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Rm62; fly.
DR GenomeRNAi; 40739; -.
DR PRO; PR:P19109; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003261; Expressed in egg cell and 23 other tissues.
DR ExpressionAtlas; P19109; baseline and differential.
DR Genevisible; P19109; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
DR GO; GO:0050688; P:regulation of defense response to virus; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 Alternative splicing; Antiviral defense; ATP-binding; Cytoplasm; Helicase;
KW Hydrolase; Immunity; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..719
FT /note="ATP-dependent RNA helicase p62"
FT /id="PRO_0000055007"
FT DOMAIN 312..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 519..664
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 94..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 281..309
FT /note="Q motif"
FT MOTIF 435..438
FT /note="DEAD box"
FT COMPBIAS 102..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 325..332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:2170937, ECO:0000303|Ref.5"
FT /id="VSP_007414"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform C and isoform E)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007413"
FT VAR_SEQ 142..145
FT /note="EGVM -> MRAK (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_007416"
FT VAR_SEQ 142..144
FT /note="EGV -> MMM (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007415"
FT CONFLICT 195
FT /note="R -> A (in Ref. 1; CAA37037)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="R -> P (in Ref. 1; CAA37037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 719 AA; 78548 MW; A70A071A920B24FC CRC64;
MLKLVQYIAP RVGGATPRPT ACGWGNLLLI SPRSGASSEK CITQRRHFLF SSASSSGTFA
SSSSLCTEQR QQFHGSRRNR ETILFPSTYS SLQAQSQRAF RDSSKPDSDD YVDSIPKAEQ
RTRTRKSLFN DPDERTEEIK IEGVMAPHDR DFGHSGRGGR GGDRGGDDRR GGGGGGNRFG
GGGGGGDYHG IRNGRVEKRR DDRGGGNRFG GGGGFGDRRG GGGGGSQDLP MRPVDFSNLA
PFKKNFYQEH PNVANRSPYE VQRYREEQEI TVRGQVPNPI QDFSEVHLPD YVMKEIRRQG
YKAPTAIQAQ GWPIAMSGSN FVGIAKTGSG KTLGYILPAI VHINNQQPLQ RGDGPIALVL
APTRELAQQI QQVATEFGSS SYVRNTCVFG GAPKGGQMRD LQRGCEIVIA TPGRLIDFLS
AGSTNLKRCT YLVLDEADRM LDMGFEPQIR KIVSQIRPDR QTLMWSATWP KEVKQLAEDF
LGNYIQINIG SLELSANHNI RQVVDVCDEF SKEEKLKTLL SDIYDTSESP GKIIIFVETK
RRVDNLVRFI RSFGVRCGAI HGDKSQSERD FVLREFRSGK SNILVATDVA ARGLDVDGIK
YVINFDYPQN SEDYIHRIGR TGRSNTKGTS FAFFTKNNAK QAKALVDVLR EANQEINPAL
ENLARNSRYD GGGGRSRYGG GGGGGRFGGG GFKKGSLSNG RGFGGGGGGG GEGRHSRFD
