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Database: UniProt
Entry: Q9V3C0
LinkDB: Q9V3C0
Original site: Q9V3C0 
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   16-OCT-2019, entry version 172.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   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-
RT   box 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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;
RP   SER-56; SER-57; SER-58 AND SER-66, AND IDENTIFICATION BY MASS
RP   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
CC       directed and fasciculated early outgrowth of the bolwig nerves, as
CC       well as for its navigation at later stages. Is required during
CC       post-transcriptional gene expression. Plays a role during
CC       morphogenetic process, apoptosis and the establishment of cell
CC       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
CC       subfamily. {ECO:0000305}.
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   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   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   eggNOG; KOG0341; Eukaryota.
DR   eggNOG; ENOG410XQQC; LUCA.
DR   GeneTree; ENSGT00940000156333; -.
DR   InParanoid; Q9V3C0; -.
DR   KO; K13116; -.
DR   OMA; HIMVATP; -.
DR   OrthoDB; 447398at2759; -.
DR   PhylomeDB; Q9V3C0; -.
DR   Reactome; R-DME-1834941; STING mediated induction of host immune responses.
DR   GenomeRNAi; 40530; -.
DR   PRO; PR:Q9V3C0; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0015331; Expressed in 30 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila).
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:0004386; F:helicase activity; ISS:FlyBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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   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; Complete proteome; Helicase; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Zinc; Zinc-finger.
FT   CHAIN         1    619       ATP-dependent RNA helicase abstrakt.
FT                                /FTId=PRO_0000054974.
FT   DOMAIN      208    392       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      403    563       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     221    228       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   ZN_FING     577    594       CCHC-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00047}.
FT   MOTIF       177    205       Q motif.
FT   MOTIF       340    343       DEAD box.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      56     56       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      57     57       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      58     58       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      66     66       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VARIANT     241    241       E -> K (in allele 14B; temperature
FT                                sensitive).
FT   VARIANT     431    431       V -> M (in allele 33B; temperature
FT                                sensitive).
FT   CONFLICT      5      5       K -> Q (in Ref. 2; AAF04040).
FT                                {ECO:0000305}.
FT   CONFLICT     26     30       Missing (in Ref. 2). {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
//
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