DX39B_DROME
ID DX39B_DROME Reviewed; 424 AA.
AC Q27268; Q540X0; Q9VMQ1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATP-dependent RNA helicase WM6;
DE Short=DEAD box protein UAP56;
DE Short=Dmrnahel;
DE EC=3.6.4.13;
DE AltName: Full=HEL/UAP56;
GN Name=Hel25E; Synonyms=Dbp25F, hel, WM6; ORFNames=CG7269;
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].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=7808417; DOI=10.1007/bf00282229;
RA Warbrick E., Glover D.;
RT "A Drosophila gene encoding a DEAD box RNA helicase can suppress loss of
RT wee1/mik1 function in Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 245:654-657(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9215899; DOI=10.1093/genetics/146.3.951;
RA Eberl D.F., Lorenz L.J., Melnick M.B., Sood V., Lasko P., Perrimon N.;
RT "A new enhancer of position-effect variegation in Drosophila melanogaster
RT encodes a putative RNA helicase that binds chromosomes and is regulated by
RT the cell cycle.";
RL Genetics 146:951-963(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE EXON JUNCTION
RP COMPLEX.
RX PubMed=11696332; DOI=10.1016/s0960-9822(01)00532-2;
RA Gatfield D., Le Hir H., Schmitt C., Braun I.C., Koecher T., Wilm M.,
RA Izaurralde E.;
RT "The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in
RT Drosophila.";
RL Curr. Biol. 11:1716-1721(2001).
RN [7]
RP FUNCTION.
RX PubMed=12743041; DOI=10.1093/emboj/cdg233;
RA Herold A., Teixeira L., Izaurralde E.;
RT "Genome-wide analysis of nuclear mRNA export pathways in Drosophila.";
RL EMBO J. 22:2472-2483(2003).
CC -!- FUNCTION: Required for mRNA export out of the nucleus. Probable RNA
CC helicase that may regulate entry into mitosis by down-regulating the
CC expression of other genes whose activity may be rate-limiting for entry
CC into mitosis during embryogenesis. Binds to salivary gland chromosomes
CC and modifies position effect variegation. Promotes an open chromatin
CC structure that favors transcription during development by regulating
CC the spread of heterochromatin. {ECO:0000269|PubMed:11696332,
CC ECO:0000269|PubMed:12743041, ECO:0000269|PubMed:9215899}.
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 -!- SUBUNIT: Component of the spliceosome (Probable). Interacts with the
CC exon junction complex. {ECO:0000269|PubMed:11696332, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11696332,
CC ECO:0000269|PubMed:9215899}. Note=Locates to nuclei of embryos and
CC ovaries, but disappears in mitotic domains of embryos as chromosomes
CC condense.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9215899}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; X79802; CAA56197.1; -; mRNA.
DR EMBL; L06018; AAB65835.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52261.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10544.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10545.1; -; Genomic_DNA.
DR EMBL; AY118921; AAM50781.1; -; mRNA.
DR PIR; S51601; S51601.
DR RefSeq; NP_723089.1; NM_164646.3.
DR RefSeq; NP_723090.1; NM_164647.1.
DR RefSeq; NP_723091.1; NM_164648.2.
DR AlphaFoldDB; Q27268; -.
DR SMR; Q27268; -.
DR BioGRID; 59949; 54.
DR DIP; DIP-20199N; -.
DR IntAct; Q27268; 4.
DR STRING; 7227.FBpp0078754; -.
DR PaxDb; Q27268; -.
DR PRIDE; Q27268; -.
DR DNASU; 33781; -.
DR EnsemblMetazoa; FBtr0079123; FBpp0078754; FBgn0014189.
DR EnsemblMetazoa; FBtr0079124; FBpp0078755; FBgn0014189.
DR EnsemblMetazoa; FBtr0079125; FBpp0078756; FBgn0014189.
DR GeneID; 33781; -.
DR KEGG; dme:Dmel_CG7269; -.
DR CTD; 33781; -.
DR FlyBase; FBgn0014189; Hel25E.
DR VEuPathDB; VectorBase:FBgn0014189; -.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00940000154912; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q27268; -.
DR OMA; IKPICRK; -.
DR PhylomeDB; Q27268; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR SignaLink; Q27268; -.
DR BioGRID-ORCS; 33781; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33781; -.
DR PRO; PR:Q27268; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0014189; Expressed in secondary oocyte and 30 other tissues.
DR ExpressionAtlas; Q27268; baseline and differential.
DR Genevisible; Q27268; DM.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
DR GO; GO:0000346; C:transcription export complex; ISS:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; 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; 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; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..424
FT /note="ATP-dependent RNA helicase WM6"
FT /id="PRO_0000055080"
FT DOMAIN 72..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 258..419
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..69
FT /note="Q motif"
FT MOTIF 193..196
FT /note="DECD box"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 424 AA; 48652 MW; CE132476090E1AFE CRC64;
MADNDDLLDY EDEEQTETTA VENQEAPKKD VKGTYVSIHS SGFRDFLLKP EILRAIVDCG
FEHPSEVQHE CIPQAVLGMD ILCQAKSGMG KTAVFVLATL QQLEPSDNNT CHVLVMCHTR
ELAFQISKEY ERFSKYMPTV KVAVFFGGMA IQKDEETLKS GTPHIVVGTP GRILALIRNK
KLNLKLLKHF VLDECDKMLE QLDMRRDVQE IFRSTPHGKQ VMMFSATLSK DIRPVCKKFM
QDPMEVYVDD EAKLTLHGLQ QHYVNLKENE KNKKLFELLD VLEFNQVVIF VKSVQRCVAL
SQLLTEQNFP AIGIHRGMTQ EERLNRYQQF KDFQKRILVA TNLFGRGMDI ERVNIVFNYD
MPEDSDTYLH RVARAGRFGT KGLAITFVSD ENDAKILNEV QDRFDVNISE LPEEIDLSTY
IEGR
