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ATP-dependent RNA helicase p62 (EC 3.6.4.13)

 DDX17_DROME             Reviewed;         719 AA.
P19109; A4V2H1; Q6AWN9; Q8IGL7; Q95TB8; Q9I7P5; Q9VNK4;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 3.
18-JUL-2018, entry version 182.
RecName: Full=ATP-dependent RNA helicase p62;
EC=3.6.4.13;
Name=Rm62; Synonyms=Dmp68, p62; ORFNames=CG10279;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
TISSUE=Embryo;
PubMed=2170937; DOI=10.1093/nar/18.18.5489;
Dorer D.R., Christensen A.C., Johnson D.H.;
"A novel RNA helicase gene tightly linked to the Triplo-lethal locus
of Drosophila.";
Nucleic Acids Res. 18:5489-5494(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND D).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND INTERACTION WITH FMR1.
PubMed=12368261; DOI=10.1101/gad.1022002;
Ishizuka A., Siomi M.C., Siomi H.;
"A Drosophila fragile X protein interacts with components of RNAi and
ribosomal proteins.";
Genes Dev. 16:2497-2508(2002).
[7]
FUNCTION IN ANTIVIRAL DEFENSE, AND DISRUPTION PHENOTYPE.
PubMed=25126784; DOI=10.1016/j.cell.2014.06.023;
Moy R.H., Cole B.S., Yasunaga A., Gold B., Shankarling G., Varble A.,
Molleston J.M., tenOever B.R., Lynch K.W., Cherry S.;
"Stem-loop recognition by DDX17 facilitates miRNA processing and
antiviral defense.";
Cell 158:764-777(2014).
-!- FUNCTION: As an RNA helicase, unwinds RNA and alters RNA
structures through ATP binding and hydrolysis. Involved in
multiple cellular processes, including pre-mRNA splicing,
alternative splicing, rRNA processing and miRNA processing, as
well as transcription regulation (By similarity)
(PubMed:12368261). Plays a role in innate immunity. Specifically
restricts bunyavirus infection, including Rift Valley fever virus
(RVFV) or La Crosse virus (LACV), but not vesicular stomatitis
virus (VSV), in an interferon- and DROSHA-independent manner
(PubMed:25126784). {ECO:0000250|UniProtKB:Q92841,
ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:25126784}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:Q92841}.
-!- SUBUNIT: Interacts with Fmr1 to form a ribonucleoprotein (RNP)
complex involved in translation regulation, other components of
the complex are mRpL5, mRpL11, AGO2 and Dcr-1.
{ECO:0000269|PubMed:12368261}.
-!- INTERACTION:
Q9NFU0:Fmr1; NbExp=4; IntAct=EBI-200734, EBI-422631;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92841}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92841}. Cytoplasm,
cytosol {ECO:0000250|UniProtKB:Q92841}. Note=In the course of
bunyavirus infection, relocalizes from the nucleus to the cytosol
where it binds viral RNA to antagonize replication.
{ECO:0000250|UniProtKB:Q92841}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=A;
IsoId=P19109-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=C; Synonyms=B, F;
IsoId=P19109-2; Sequence=VSP_007413, VSP_007415;
Note=No experimental confirmation available.;
Name=D;
IsoId=P19109-3; Sequence=VSP_007414;
Name=E;
IsoId=P19109-4; Sequence=VSP_007413, VSP_007416;
Note=No experimental confirmation available.;
-!- DISRUPTION PHENOTYPE: No phenotype under normal conditions. Upon
infection with Rift Valley fever virus (RVFV) or La Crosse virus
(LACV), knockdown flies exhibit increased mortality. No phenotype
upon infection with other viruses, including vesicular stomatitis
virus (VSV), Sindbis virus (SINV), nor Drosophila C virus (DCV).
{ECO:0000269|PubMed:25126784}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X52846; CAA37037.1; -; mRNA.
EMBL; AE014297; AAF51926.2; -; Genomic_DNA.
EMBL; AE014297; AAF51927.2; -; Genomic_DNA.
EMBL; AE014297; AAG22212.1; -; Genomic_DNA.
EMBL; AE014297; AAG22213.2; -; Genomic_DNA.
EMBL; AE014297; AAN14331.1; -; Genomic_DNA.
EMBL; AE014297; AAN14332.1; -; Genomic_DNA.
EMBL; BT001716; AAN71471.1; -; mRNA.
EMBL; BT011476; AAR99134.1; -; mRNA.
EMBL; BT015209; AAT94438.1; -; mRNA.
PIR; S11485; S11485.
RefSeq; NP_001163528.1; NM_001170057.1. [P19109-3]
RefSeq; NP_001189182.1; NM_001202253.2. [P19109-4]
RefSeq; NP_524243.2; NM_079519.2. [P19109-1]
RefSeq; NP_731031.1; NM_169118.1. [P19109-3]
RefSeq; NP_731032.1; NM_169119.3. [P19109-4]
RefSeq; NP_731033.1; NM_169120.1. [P19109-2]
RefSeq; NP_731034.1; NM_169121.2. [P19109-2]
RefSeq; NP_731035.2; NM_169122.1. [P19109-2]
UniGene; Dm.1520; -.
ProteinModelPortal; P19109; -.
SMR; P19109; -.
BioGrid; 65943; 42.
DIP; DIP-17867N; -.
IntAct; P19109; 52.
MINT; P19109; -.
STRING; 7227.FBpp0078301; -.
PaxDb; P19109; -.
PRIDE; P19109; -.
EnsemblMetazoa; FBtr0078649; FBpp0078298; FBgn0003261. [P19109-2]
EnsemblMetazoa; FBtr0078650; FBpp0078299; FBgn0003261. [P19109-3]
EnsemblMetazoa; FBtr0078651; FBpp0078300; FBgn0003261. [P19109-2]
EnsemblMetazoa; FBtr0078652; FBpp0078301; FBgn0003261. [P19109-1]
EnsemblMetazoa; FBtr0078653; FBpp0078302; FBgn0003261. [P19109-4]
EnsemblMetazoa; FBtr0078654; FBpp0078303; FBgn0003261. [P19109-2]
EnsemblMetazoa; FBtr0301947; FBpp0291159; FBgn0003261. [P19109-3]
EnsemblMetazoa; FBtr0302597; FBpp0291753; FBgn0003261. [P19109-4]
GeneID; 40739; -.
KEGG; dme:Dmel_CG10279; -.
UCSC; CG10279-RC; d. melanogaster.
CTD; 40739; -.
FlyBase; FBgn0003261; Rm62.
eggNOG; KOG0331; Eukaryota.
eggNOG; COG0513; LUCA.
GeneTree; ENSGT00920000149008; -.
InParanoid; P19109; -.
KO; K12823; -.
OrthoDB; EOG091G033A; -.
PhylomeDB; P19109; -.
Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
Reactome; R-DME-9018519; Estrogen-dependent gene expression.
ChiTaRS; Rm62; fly.
GenomeRNAi; 40739; -.
PRO; PR:P19109; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0003261; -.
ExpressionAtlas; P19109; baseline and differential.
Genevisible; P19109; DM.
GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
GO; GO:0050688; P:regulation of defense response to virus; IMP:FlyBase.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0016246; P:RNA interference; IMP:FlyBase.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
Alternative splicing; Antiviral defense; ATP-binding;
Complete proteome; Cytoplasm; Helicase; Hydrolase; Immunity;
mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
Reference proteome; RNA-binding; RNA-mediated gene silencing;
Translation regulation.
CHAIN 1 719 ATP-dependent RNA helicase p62.
/FTId=PRO_0000055007.
DOMAIN 312 487 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 519 664 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 325 332 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 281 309 Q motif.
MOTIF 435 438 DEAD box.
COMPBIAS 153 225 Gly-rich.
COMPBIAS 671 713 Gly-rich.
VAR_SEQ 1 144 Missing (in isoform D).
{ECO:0000303|PubMed:2170937,
ECO:0000303|Ref.5}.
/FTId=VSP_007414.
VAR_SEQ 1 141 Missing (in isoform C and isoform E).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_007413.
VAR_SEQ 142 145 EGVM -> MRAK (in isoform E).
{ECO:0000305}.
/FTId=VSP_007416.
VAR_SEQ 142 144 EGV -> MMM (in isoform C).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_007415.
CONFLICT 195 195 R -> A (in Ref. 1; CAA37037).
{ECO:0000305}.
CONFLICT 675 675 R -> P (in Ref. 1; CAA37037).
{ECO:0000305}.
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


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