DDX41_DROME
ID DDX41_DROME Reviewed; 619 AA.
AC Q9V3C0; Q9U6D0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=ATP-dependent RNA helicase abstrakt;
DE Short=DEAD box protein abstrakt;
DE EC=3.6.4.13;
GN Name=abs; ORFNames=CG14637;
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].
RX PubMed=10704843; DOI=10.1016/s0925-4773(99)00298-1;
RA Schmucker D., Vorbrueggen G., Yeghiayan P., Fan H.Q., Jaeckle H., Gaul U.;
RT "The Drosophila gene abstrakt, required for visual system development,
RT encodes a putative RNA helicase of the DEAD box protein family.";
RL Mech. Dev. 91:189-196(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 14B AND 33B.
RX PubMed=10607561; DOI=10.1016/s0960-9822(00)80082-2;
RA Irion U., Leptin M.;
RT "Developmental and cell biological functions of the Drosophila DEAD-box
RT protein abstrakt.";
RL Curr. Biol. 9:1373-1381(1999).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-14; SER-56;
RP SER-57; SER-58 AND SER-66, 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. Is essential for the directed and
CC fasciculated early outgrowth of the bolwig nerves, as well as for its
CC navigation at later stages. Is required during post-transcriptional
CC gene expression. Plays a role during morphogenetic process, apoptosis
CC and the establishment of cell polarity.
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: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX41 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF212866; AAF19985.1; -; mRNA.
DR EMBL; AF187729; AAF04040.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF52165.1; -; Genomic_DNA.
DR EMBL; AY051752; AAK93176.1; -; mRNA.
DR RefSeq; NP_524220.1; NM_079496.4.
DR AlphaFoldDB; Q9V3C0; -.
DR SMR; Q9V3C0; -.
DR BioGRID; 65752; 17.
DR DIP; DIP-21861N; -.
DR IntAct; Q9V3C0; 5.
DR STRING; 7227.FBpp0078606; -.
DR iPTMnet; Q9V3C0; -.
DR PaxDb; Q9V3C0; -.
DR PRIDE; Q9V3C0; -.
DR DNASU; 40530; -.
DR EnsemblMetazoa; FBtr0078967; FBpp0078606; FBgn0015331.
DR GeneID; 40530; -.
DR KEGG; dme:Dmel_CG14637; -.
DR UCSC; CG14637-RA; d. melanogaster.
DR CTD; 40530; -.
DR FlyBase; FBgn0015331; abs.
DR VEuPathDB; VectorBase:FBgn0015331; -.
DR eggNOG; KOG0341; Eukaryota.
DR GeneTree; ENSGT00940000156333; -.
DR HOGENOM; CLU_003041_16_5_1; -.
DR InParanoid; Q9V3C0; -.
DR OMA; DMLDKKM; -.
DR OrthoDB; 447398at2759; -.
DR PhylomeDB; Q9V3C0; -.
DR Reactome; R-DME-1834941; STING mediated induction of host immune responses.
DR SignaLink; Q9V3C0; -.
DR BioGRID-ORCS; 40530; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40530; -.
DR PRO; PR:Q9V3C0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015331; Expressed in testis and 13 other tissues.
DR Genevisible; Q9V3C0; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal 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:0004386; F:helicase activity; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd17951; DEADc_DDX41; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044113; DEADc_DDX41.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
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 SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..619
FT /note="ATP-dependent RNA helicase abstrakt"
FT /id="PRO_0000054974"
FT DOMAIN 208..392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 403..563
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 577..594
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..205
FT /note="Q motif"
FT MOTIF 340..343
FT /note="DEAD box"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 241
FT /note="E -> K (in allele 14B; temperature sensitive)"
FT VARIANT 431
FT /note="V -> M (in allele 33B; temperature sensitive)"
FT CONFLICT 5
FT /note="K -> Q (in Ref. 2; AAF04040)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..30
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 69488 MW; F148D277A1FD0BEC CRC64;
MAHVKRYRRS SKSSEEGDLD NEDYVPYVPV KERKKQHMIK LGRIVQLVSE TAQPKSSSEN
ENEDDSQGAH DVETWGRKYN ISLLDQHTEL KKIAEAKKLS AVEKQLREEE KIMESIAQQK
ALMGVAELAK GIQYEQPIKT AWKPPRYIRE MSEEEREAVR HELRILVEGE TPSPPIRSFR
EMKFPKGILN GLAAKGIKNP TPIQVQGLPT VLAGRDLIGI AFTGSGKTLV FVLPVIMFAL
EQEYSLPFER NEGPYGLIIC PSRELAKQTH EIIQHYSKHL QACGMPEIRS CLAMGGLPVS
EALDVISRGV HIVVATPGRL MDMLDKKILT LDMCRYLCMD EADRMIDMGF EEDVRTIFSF
FKGQRQTLLF SATMPKKIQN FARSALVKPV TINVGRAGAA SMNVTQQVEY VKQEAKVVYL
LDCLQKTAPP VLIFAEKKQD VDCIHEYLLL KGVEAVAIHG GKDQEERSRA VDAYRVGKKD
VLVATDVASK GLDFPNVQHV INYDMPDDIE NYVHRIGRTG RSNTKGLATT LINKTTEQSV
LLDLKHLLIE GKQEVPDFLD ELAPETEHQH LDLGDSHGCT YCGGLGHRIT ECPKLEAVQN
KQASNIGRRD YLSNTAADY
