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Database: UniProt
Entry: P23128
LinkDB: P23128
Original site: P23128 
ID   DDX6_DROME              Reviewed;         459 AA.
AC   P23128; Q8IPC9; Q961D2; Q9VL17;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 3.
DT   13-NOV-2019, entry version 182.
DE   RecName: Full=ATP-dependent RNA helicase me31b;
DE            EC=3.6.4.13;
DE   AltName: Full=Maternal expression at 31B;
GN   Name=me31B; ORFNames=CG4916;
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] (ISOFORM A), AND DEVELOPMENTAL STAGE.
RX   PubMed=1900936; DOI=10.1073/pnas.88.6.2113;
RA   de Valoir T., Tucker M.A., Belikoff E.J., Camp L.A., Bolduc C.,
RA   Beckingham K.;
RT   "A second maternally expressed Drosophila gene encodes a putative RNA
RT   helicase of the 'DEAD box' family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2113-2117(1991).
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.,
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   [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.,
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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   [5]
RP   IDENTIFICATION IN THE OSK RNP COMPLEX.
RX   PubMed=10662770; DOI=10.1083/jcb.148.3.427;
RA   Wilhelm J.E., Mansfield J., Hom-Booher N., Wang S., Turck C.W.,
RA   Hazelrigg T., Vale R.D.;
RT   "Isolation of a ribonucleoprotein complex involved in mRNA
RT   localization in Drosophila oocytes.";
RL   J. Cell Biol. 148:427-440(2000).
RN   [6]
RP   FUNCTION, INTERACTION WITH YPS AND EXU, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=11546740;
RA   Nakamura A., Amikura R., Hanyu K., Kobayashi S.;
RT   "Me31B silences translation of oocyte-localizing RNAs through the
RT   formation of cytoplasmic RNP complex during Drosophila oogenesis.";
RL   Development 128:3233-3242(2001).
RN   [7]
RP   FUNCTION, INTERACTION WITH TRAL, AND SUBCELLULAR LOCATION.
RX   PubMed=16256742; DOI=10.1016/j.devcel.2005.09.015;
RA   Wilhelm J.E., Buszczak M., Sayles S.;
RT   "Efficient protein trafficking requires trailer hitch, a component of
RT   a ribonucleoprotein complex localized to the ER in Drosophila.";
RL   Dev. Cell 9:675-685(2005).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH TRAL AND FMR1, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17178403; DOI=10.1016/j.neuron.2006.10.028;
RA   Barbee S.A., Estes P.S., Cziko A.M., Hillebrand J., Luedeman R.A.,
RA   Coller J.M., Johnson N., Howlett I.C., Geng C., Ueda R., Brand A.H.,
RA   Newbury S.F., Wilhelm J.E., Levine R.B., Nakamura A., Parker R.,
RA   Ramaswami M.;
RT   "Staufen- and FMRP-containing neuronal RNPs are structurally and
RT   functionally related to somatic P bodies.";
RL   Neuron 52:997-1009(2006).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17982591; DOI=10.1100/tsw.2007.206;
RA   Hillebrand J., Barbee S.A., Ramaswami M.;
RT   "P-body components, microRNA regulation, and synaptic plasticity.";
RL   ScientificWorldJournal 7:178-190(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-29 AND SER-450,
RP   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).
RN   [11]
RP   INTERACTION WITH EDC3 AND TRAL.
RX   PubMed=18765641; DOI=10.1128/mcb.00759-08;
RA   Tritschler F., Eulalio A., Helms S., Schmidt S., Coles M.,
RA   Weichenrieder O., Izaurralde E., Truffault V.;
RT   "Similar modes of interaction enable Trailer Hitch and EDC3 to
RT   associate with DCP1 and Me31B in distinct protein complexes.";
RL   Mol. Cell. Biol. 28:6695-6708(2008).
RN   [12]
RP   FUNCTION, INTERACTION WITH TUD AND VAS, AND SUBCELLULAR LOCATION.
RX   PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
RA   Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
RT   "Isolation of new polar granule components in Drosophila reveals P
RT   body and ER associated proteins.";
RL   Mech. Dev. 125:865-873(2008).
RN   [13]
RP   INTERACTION WITH EDC3, AND MUTAGENESIS OF GLN-281; HIS-284; THR-288
RP   AND LYS-292.
RX   PubMed=19285948; DOI=10.1016/j.molcel.2009.02.014;
RA   Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E.,
RA   Weichenrieder O.;
RT   "Structural basis for the mutually exclusive anchoring of P body
RT   components EDC3 and Tral to the DEAD box protein DDX6/Me31B.";
RL   Mol. Cell 33:661-668(2009).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=21267420; DOI=10.3389/fncir.2010.00121;
RA   Hillebrand J., Pan K., Kokaram A., Barbee S., Parker R., Ramaswami M.;
RT   "The Me31B DEAD-Box Helicase Localizes to Postsynaptic Foci and
RT   Regulates Expression of a CaMKII Reporter mRNA in Dendrites of
RT   Drosophila Olfactory Projection Neurons.";
RL   Front. Neural Circuits 4:121-121(2010).
RN   [15]
RP   FUNCTION, INTERACTION WITH AGO3; PAPI AND TRAL, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=21447556; DOI=10.1242/dev.059287;
RA   Liu L., Qi H., Wang J., Lin H.;
RT   "PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and
RT   TRAL in the nuage to silence transposition.";
RL   Development 138:1863-1873(2011).
RN   [16]
RP   FUNCTION, AND IDENTIFICATION IN THE NOS RNP COMPLEX.
RX   PubMed=21081899; DOI=10.1038/emboj.2010.283;
RA   Jeske M., Moritz B., Anders A., Wahle E.;
RT   "Smaug assembles an ATP-dependent stable complex repressing nanos mRNA
RT   translation at multiple levels.";
RL   EMBO J. 30:90-103(2011).
RN   [17]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH EIF4E1; CUP; TRAL AND PABP,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=28875934; DOI=10.7554/elife.27891;
RA   Wang M., Ly M., Lugowski A., Laver J.D., Lipshitz H.D., Smibert C.A.,
RA   Rissland O.S.;
RT   "ME31B globally represses maternal mRNAs by two distinct mechanisms
RT   during the Drosophila maternal-to-zygotic transition.";
RL   Elife 6:0-0(2017).
RN   [18]
RP   INTERACTION WITH TUD AND AUB, SUBCELLULAR LOCATION, AND METHYLATION.
RX   PubMed=28945271; DOI=10.1002/1873-3468.12854;
RA   DeHaan H., McCambridge A., Armstrong B., Cruse C., Solanki D.,
RA   Trinidad J.C., Arkov A.L., Gao M.;
RT   "An in vivo proteomic analysis of the Me31B interactome in Drosophila
RT   germ granules.";
RL   FEBS Lett. 591:3536-3547(2017).
RN   [19]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH ATX2; TYF AND PABP,
RP   INTERACTION WITH TYF; PABP; ATX2 AND LSM12A, AND DISRUPTION PHENOTYPE.
RX   PubMed=28388438; DOI=10.1016/j.molcel.2017.03.004;
RA   Lee J., Yoo E., Lee H., Park K., Hur J.H., Lim C.;
RT   "LSM12 and ME31B/DDX6 Define Distinct Modes of Posttranscriptional
RT   Regulation by ATAXIN-2 Protein Complex in Drosophila Circadian
RT   Pacemaker Neurons.";
RL   Mol. Cell 66:129-140(2017).
CC   -!- FUNCTION: ATP-dependent RNA helicase which is a core component of
CC       a variety of ribonucleoprotein complexes (RNPs) that play critical
CC       roles in translational repression and mRNA decapping during
CC       embryogenesis, oogenesis, neurogenesis and neurotransmission
CC       (PubMed:11546740, PubMed:16256742, PubMed:17178403,
CC       PubMed:18590813, PubMed:21267420, PubMed:21447556,
CC       PubMed:28875934, PubMed:28388438, PubMed:17982591). Recruits core
CC       components and translational repressors to some RNP complexes, and
CC       mediates RNP aggregation into processing granules such as P-bodies
CC       (PubMed:28875934, PubMed:11546740, PubMed:16256742,
CC       PubMed:17178403, PubMed:21267420, PubMed:21447556,
CC       PubMed:17982591). As part of a RNP complex containing tral,
CC       eIF4E1, cup, and pAbp, involved in RNP-mediated translational
CC       repression of maternal mRNAs during oogenesis and embryogenesis
CC       (PubMed:28875934). As part of a RNP complex containing tral and
CC       the RNA localization factors exu and yps, mediates translational
CC       silencing of mRNAs such as osk/oskar and bcd/bicoid during their
CC       transport to the oocyte in order to prevent their translation
CC       until they reach their positional destinations (PubMed:11546740).
CC       In neurons and possibly imaginal disks, involved in miRNA-mediated
CC       translational repression, possibly in association with components
CC       of the piRNA transposon silencing pathway (PubMed:21447556,
CC       PubMed:17178403, PubMed:21267420, PubMed:17982591,
CC       PubMed:21081899). Involved in RNA localization and protein
CC       trafficking in the oocyte (PubMed:11546740, PubMed:16256742). As
CC       part of an ER-associated RNP containing tral, cup and yps,
CC       required for tral-dependent ER exit site formation and
CC       consequently efficient trafficking of proteins such as grk and yl
CC       through the secretory pathway (PubMed:16256742). Component of
CC       neuron RNPs that mediate transport and translation of neuronal
CC       RNAs, including translation repression of synaptic transcripts in
CC       preparation for their dendritic targeting (PubMed:17178403,
CC       PubMed:21267420, PubMed:28388438). As part of the Atx2-Not1
CC       repressor complex promotes Not1-dependent post-transcriptional
CC       gene silencing in adult circadian pacemaker neurons in order to
CC       sustain high-amplitude circadian rhythms and Pdf cycling in a per-
CC       independent manner (PubMed:28388438). Promotes the interaction
CC       between Atx2 and Not1 within the Atx2-Not1 RNP complex
CC       (PubMed:28388438). {ECO:0000269|PubMed:11546740,
CC       ECO:0000269|PubMed:16256742, ECO:0000269|PubMed:17178403,
CC       ECO:0000269|PubMed:17982591, ECO:0000269|PubMed:18590813,
CC       ECO:0000269|PubMed:21081899, ECO:0000269|PubMed:21267420,
CC       ECO:0000269|PubMed:21447556, ECO:0000269|PubMed:28388438,
CC       ECO:0000269|PubMed:28875934}.
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: Conserved component of different types of multiprotein
CC       ribonucleoprotein complexes (RNPs) that form distinct germ
CC       granules (P-body, nuage, sponge body or polar granules) and P-
CC       body-like neuronal RNPs (PubMed:11546740, PubMed:16256742,
CC       PubMed:18765641, PubMed:18590813, PubMed:19285948,
CC       PubMed:28388438). Consequently it interacts with a wide variety of
CC       proteins, some of which appear to be common interactive partners
CC       in almost all RNPs types i.e. cup and tral, whereas other
CC       interactions are specific to a germ granule/RNP (PubMed:28945271).
CC       Core functional components in me31B-containing RNPs include RNA
CC       regulatory proteins (such as translational repressor, RNA-
CC       decapping and exonuclease proteins), RNA localization proteins and
CC       additional proteins depending on the biological context of the
CC       RNPs (PubMed:17178403, PubMed:28945271). In the P-body RNPs,
CC       interacts with at least the translation repressor proteins tral,
CC       cup and Edc3, and the mRNA localization factor yps
CC       (PubMed:16256742, PubMed:18765641, PubMed:18590813,
CC       PubMed:19285948). Interaction with tral or Edc3 is required for
CC       translation repression and possibly RNA decapping; binding to tral
CC       and Edc3 is mutually exclusive (PubMed:18765641, PubMed:19285948).
CC       In the nuage and germ plasm polar granule RNPs, interacts with at
CC       least tral, cup, and additional proteins required for assembly and
CC       function of the germ granules such as tud, vas and aub
CC       (PubMed:18765641, PubMed:18590813, PubMed:19285948,
CC       PubMed:28945271). Interacts (when dimethylated on Arg residues)
CC       with tud; interaction is RNA-independent (PubMed:28945271).
CC       Component of the osk RNP complex, which is composed of at least
CC       me31B, exu, yps, aret/bruno, cup, and the mRNA of osk
CC       (PubMed:10662770). Component of the nos RNP complex, which is
CC       composed of at least smg, cup, tral, me31B, the CCR4-NOT complex
CC       members Rga/NOT2 and Caf1, and the mRNA of nos (PubMed:21081899).
CC       Interacts with tral and piRNA pathway components papi and AGO3;
CC       promotes interaction between nuage RNPs and the piRNA-mediated
CC       transposon silencing (PubMed:21447556). Forms a RNP containing at
CC       least me31B, eIF4E1, cup, tral and pAbp; this interaction is
CC       required for the translational silencing of maternal mRNAs during
CC       the maternal-to-zygotic transition (PubMed:28875934). In the
CC       sponge body, forms a RNP containing at least me31B, exu, yps and
CC       the mRNA of osk; interactions with exu and yps are RNA dependent
CC       (PubMed:11546740). Component of a neuronal RNP, at least composed
CC       of me31B, tral and Fmr1 (PubMed:17178403). Component of the Atx2-
CC       Not1 repressor complex, composed of at least me31B, Atx2, tyf and
CC       pAbp (PubMed:28388438). Interacts (via the C-terminus) with Atx2,
CC       tyf, pAbp and Lsm12a (PubMed:28388438).
CC       {ECO:0000269|PubMed:10662770, ECO:0000269|PubMed:11546740,
CC       ECO:0000269|PubMed:16256742, ECO:0000269|PubMed:17178403,
CC       ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:18765641,
CC       ECO:0000269|PubMed:19285948, ECO:0000269|PubMed:21081899,
CC       ECO:0000269|PubMed:21447556, ECO:0000269|PubMed:28388438,
CC       ECO:0000269|PubMed:28875934, ECO:0000269|PubMed:28945271}.
CC   -!- INTERACTION:
CC       Q9VMA3:cup; NbExp=3; IntAct=EBI-300281, EBI-95398;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11546740,
CC       ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:28945271}.
CC       Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC       {ECO:0000269|PubMed:11546740, ECO:0000269|PubMed:16256742,
CC       ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:18590813,
CC       ECO:0000269|PubMed:21267420, ECO:0000269|PubMed:21447556,
CC       ECO:0000269|PubMed:28945271}. Cytoplasm, P-body
CC       {ECO:0000269|PubMed:17982591, ECO:0000269|PubMed:21447556,
CC       ECO:0000269|PubMed:28945271}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16256742}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:21267420}. Note=Component of a variety of germ
CC       granule ribonucleoprotein complexes (RNPs) including the nuage of
CC       nurse cells, sponge bodies of nurse cells and early egg chambers
CC       in oocytes, as well as polar granules in the germ plasm at the
CC       posterior pole of mid-late stage oocytes and in early embryos
CC       (PubMed:11546740, PubMed:18590813, PubMed:21447556,
CC       PubMed:28945271, PubMed:21267420). Component of an RNP that
CC       localizes to discrete subdomains of the ER cytoplasmic surface
CC       (PubMed:21267420, PubMed:16256742). Also present in cytoplasmic
CC       granules in the cell bodies and neuropil area of the antennal
CC       lobes (PubMed:21267420). In the olfactory sensory and projection
CC       neurons, granules appear to predominately localize to postsynaptic
CC       dendrites (PubMed:21267420). {ECO:0000269|PubMed:11546740,
CC       ECO:0000269|PubMed:16256742, ECO:0000269|PubMed:18590813,
CC       ECO:0000269|PubMed:21267420, ECO:0000269|PubMed:21447556,
CC       ECO:0000269|PubMed:28945271}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P23128-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P23128-2; Sequence=VSP_019286;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout the brain
CC       (at protein level) (PubMed:21267420, PubMed:17178403). Expressed
CC       in the olfactory system including the antennal lobes, projection
CC       neurons, local interneurons, mushroom-body Kenyon cells and glial
CC       cells (at protein level) (PubMed:21267420).
CC       {ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:21267420}.
CC   -!- DEVELOPMENTAL STAGE: First detected at low levels in the germarium
CC       region 2B where it is concentrated in the pro-oocytes (at protein
CC       level) (PubMed:11546740). Remains concentrated in the oocyte until
CC       mid-oogenesis (at protein level) (PubMed:11546740). In early egg
CC       chambers detected in nurse cells and oocytes, and later
CC       accumulates at the posterior pole of stage 10 oocytes (at protein
CC       level) (PubMed:11546740). Expression decreases during the first 5
CC       hours of embryogenesis; expression levels are high during the
CC       first 2 hours of embryogenesis then sharply decrease at 2-3 hours
CC       and remains low (at protein level) (PubMed:28875934). Ubiquitously
CC       expressed in cleavage embryos but is not detected at the cellular
CC       blastoderm stage (at protein level) (PubMed:11546740). Expressed
CC       both maternally and zygotically (PubMed:1900936).
CC       {ECO:0000269|PubMed:11546740, ECO:0000269|PubMed:1900936,
CC       ECO:0000269|PubMed:28875934}.
CC   -!- PTM: Symmetrically dimethylated on arginine residues.
CC       {ECO:0000269|PubMed:28945271}.
CC   -!- DISRUPTION PHENOTYPE: Larvae lethal at the second- or third-instar
CC       stage (PubMed:11546740). RNAi-mediated knockdown in adult pigment
CC       dispersing factor (Pdf)-expressing clock neurons results in poor
CC       circadian locomotor rhythms under constant dark (DD) conditions
CC       (PubMed:28388438). The axonal terminus of s-LNv neurons display a
CC       loss of Pdf circadian daily oscillations which is consistent with
CC       their behavioral arrhythmicity (PubMed:28388438). However, there
CC       is no effect on the daily oscillations of pir and tim proteins in
CC       Pdf neurons (PubMed:28388438). Double knockdown with Atx2 enhances
CC       the behavioral arrhythmicity (PubMed:28388438). RNAi-mediated
CC       knockdown in the dorsal-most class IV neurons frequently results
CC       in defects in terminal dendrite morphology and dendritic tiling
CC       (PubMed:17178403). RNAi-mediated knockdown in adult projection
CC       neurons increases levels of the translational reporter protein
CC       CaMKII in the antennal lobe (PubMed:21267420). RNAi-mediated
CC       knockdown in the anterior/posterior boundary of the wing imaginal
CC       disk causes loss of DCP1- and pcm-expressing P-bodies
CC       (PubMed:17982591). {ECO:0000269|PubMed:11546740,
CC       ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:17982591,
CC       ECO:0000269|PubMed:21267420, ECO:0000269|PubMed:28388438}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
DR   EMBL; M59926; AAA28603.1; -; mRNA.
DR   EMBL; AE014134; AAF52881.2; -; Genomic_DNA.
DR   EMBL; AE014134; AAN10728.1; -; Genomic_DNA.
DR   EMBL; AY051663; AAK93087.1; -; mRNA.
DR   PIR; A39157; A39157.
DR   RefSeq; NP_523533.2; NM_078809.4. [P23128-1]
DR   RefSeq; NP_723539.1; NM_164898.2. [P23128-2]
DR   PDB; 6S8R; X-ray; 2.41 A; A=264-431.
DR   PDBsum; 6S8R; -.
DR   SMR; P23128; -.
DR   BioGrid; 60455; 35.
DR   IntAct; P23128; 14.
DR   MINT; P23128; -.
DR   STRING; 7227.FBpp0079565; -.
DR   iPTMnet; P23128; -.
DR   PaxDb; P23128; -.
DR   PRIDE; P23128; -.
DR   EnsemblMetazoa; FBtr0079975; FBpp0079565; FBgn0004419. [P23128-1]
DR   EnsemblMetazoa; FBtr0079976; FBpp0079566; FBgn0004419. [P23128-2]
DR   GeneID; 34364; -.
DR   KEGG; dme:Dmel_CG4916; -.
DR   CTD; 34364; -.
DR   FlyBase; FBgn0004419; me31B.
DR   eggNOG; KOG0326; Eukaryota.
DR   eggNOG; ENOG410XRAZ; LUCA.
DR   GeneTree; ENSGT00940000170366; -.
DR   InParanoid; P23128; -.
DR   KO; K12614; -.
DR   OMA; DWNLMSS; -.
DR   PhylomeDB; P23128; -.
DR   Reactome; R-DME-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   ChiTaRS; me31B; fly.
DR   GenomeRNAi; 34364; -.
DR   PRO; PR:P23128; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0004419; Expressed in 33 organ(s), highest expression level in egg chamber.
DR   Genevisible; P23128; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR   GO; GO:0043186; C:P granule; IDA:FlyBase.
DR   GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR   GO; GO:0071683; C:sensory dendrite; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; IMP:FlyBase.
DR   GO; GO:0035195; P:gene silencing by miRNA; IGI:FlyBase.
DR   GO; GO:0046959; P:habituation; IMP:FlyBase.
DR   GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IMP:UniProtKB.
DR   GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:UniProtKB.
DR   GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR   GO; GO:0007279; P:pole cell formation; IGI:FlyBase.
DR   GO; GO:1905618; P:positive regulation of miRNA mediated inhibition of translation; IDA:UniProtKB.
DR   GO; GO:0060148; P:positive regulation of posttranscriptional gene silencing; IMP:UniProtKB.
DR   GO; GO:0050688; P:regulation of defense response to virus; IMP:FlyBase.
DR   GO; GO:0150011; P:regulation of neuron projection arborization; IMP:UniProtKB.
DR   GO; GO:0090328; P:regulation of olfactory learning; IMP:FlyBase.
DR   GO; GO:0034063; P:stress granule assembly; 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; 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   3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW   Complete proteome; Cytoplasm; Endoplasmic reticulum; Helicase;
KW   Hydrolase; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repressor; RNA-binding; Translation regulation.
FT   CHAIN         1    459       ATP-dependent RNA helicase me31b.
FT                                /FTId=PRO_0000054982.
FT   DOMAIN       89    259       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      269    429       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     102    109       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        58     86       Q motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00552}.
FT   MOTIF       207    210       DEAD box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOD_RES       8      8       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      29     29       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     450    450       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VAR_SEQ       1     31       Missing (in isoform B). {ECO:0000305}.
FT                                /FTId=VSP_019286.
FT   MUTAGEN     281    281       Q->A: Abolishes interaction with Edc3;
FT                                when associated with A-284; A-288 and A-
FT                                292. {ECO:0000269|PubMed:19285948}.
FT   MUTAGEN     284    284       H->A: Abolishes interaction with Edc3;
FT                                when associated with A-281; A-288 and A-
FT                                292. {ECO:0000269|PubMed:19285948}.
FT   MUTAGEN     288    288       T->A: Abolishes interaction with Edc3;
FT                                when associated with A-281; A-284 and A-
FT                                292. {ECO:0000269|PubMed:19285948}.
FT   MUTAGEN     292    292       K->A: Abolishes interaction with Edc3;
FT                                when associated with A-281; A-284 and A-
FT                                288. {ECO:0000269|PubMed:19285948}.
FT   CONFLICT     39     45       KLPPKDN -> NCRQRTT (in Ref. 1; AAA28603).
FT                                {ECO:0000305}.
FT   STRAND      270    276       {ECO:0000244|PDB:6S8R}.
FT   HELIX       279    281       {ECO:0000244|PDB:6S8R}.
FT   HELIX       282    292       {ECO:0000244|PDB:6S8R}.
FT   STRAND      296    301       {ECO:0000244|PDB:6S8R}.
FT   HELIX       305    318       {ECO:0000244|PDB:6S8R}.
FT   STRAND      323    325       {ECO:0000244|PDB:6S8R}.
FT   HELIX       331    343       {ECO:0000244|PDB:6S8R}.
FT   STRAND      345    351       {ECO:0000244|PDB:6S8R}.
FT   STRAND      364    371       {ECO:0000244|PDB:6S8R}.
FT   HELIX       376    383       {ECO:0000244|PDB:6S8R}.
FT   STRAND      385    390       {ECO:0000244|PDB:6S8R}.
FT   STRAND      393    399       {ECO:0000244|PDB:6S8R}.
FT   HELIX       401    403       {ECO:0000244|PDB:6S8R}.
FT   HELIX       404    414       {ECO:0000244|PDB:6S8R}.
FT   HELIX       427    429       {ECO:0000244|PDB:6S8R}.
SQ   SEQUENCE   459 AA;  51945 MW;  B783E8185EF11E86 CRC64;
     MMTEKLNSGH TNLTSKGIIN DLQIAGNTSD DMGWKSKLKL PPKDNRFKTT DVTDTRGNEF
     EEFCLKRELL MGIFEKGWER PSPIQEAAIP IALSGKDVLA RAKNGTGKTG AYCIPVLEQI
     DPTKDYIQAL VMVPTRELAL QTSQICIELA KHLDIRVMVT TGGTILKDDI LRIYQKVQLI
     IATPGRILDL MDKKVADMSH CRILVLDEAD KLLSLDFQGM LDHVILKLPK DPQILLFSAT
     FPLTVKNFME KHLREPYEIN LMEELTLKGV TQYYAFVQER QKVHCLNTLF SKLQINQSII
     FCNSTQRVEL LAKKITELGY CCYYIHAKMA QAHRNRVFHD FRQGLCRNLV CSDLFTRGID
     VQAVNVVINF DFPRMAETYL HRIGRSGRFG HLGIAINLIT YEDRFDLHRI EKELGTEIKP
     IPKVIDPALY VANVGASVGD TCNNSDLNNS ANEEGNVSK
//
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