DDX6_DROME
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 03-AUG-2022, entry version 195.
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC 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., 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 [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., 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 [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., 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 [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 localization in
RT Drosophila oocytes.";
RL J. Cell Biol. 148:427-440(2000).
RN [6]
RP FUNCTION, INTERACTION WITH YPS AND EXU, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11546740; DOI=10.1242/dev.128.17.3233;
RA Nakamura A., Amikura R., Hanyu K., Kobayashi S.;
RT "Me31B silences translation of oocyte-localizing RNAs through the formation
RT 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 a
RT 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, AND
RP 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 associate
RT 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 body and
RT 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 AND
RP 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 components
RT 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 Regulates
RT Expression of a CaMKII Reporter mRNA in Dendrites of Drosophila Olfactory
RT Projection Neurons.";
RL Front. Neural Circuits 4:121-121(2010).
RN [15]
RP FUNCTION, INTERACTION WITH AGO3; PAPI AND TRAL, AND SUBCELLULAR 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 TRAL in
RT 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, AND
RP 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 during
RT 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 germ
RT granules.";
RL FEBS Lett. 591:3536-3547(2017).
RN [19]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ATX2; TYF AND PABP, INTERACTION
RP 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 Pacemaker
RT Neurons.";
RL Mol. Cell 66:129-140(2017).
RN [20]
RP FUNCTION, AND INTERACTION WITH GYF.
RX PubMed=31114929; DOI=10.1093/nar/gkz429;
RA Ruscica V., Bawankar P., Peter D., Helms S., Igreja C., Izaurralde E.;
RT "Direct role for the Drosophila GIGYF protein in 4EHP-mediated mRNA
RT repression.";
RL Nucleic Acids Res. 47:7035-7048(2019).
RN [21] {ECO:0007744|PDB:6S8R}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 264-431, INTERACTION WITH GYF;
RP 4E-T; PATR-1 AND EDC3, AND MUTAGENESIS OF CYS-285; LEU-289; LEU-310 AND
RP LYS-314.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a core component of a
CC variety of ribonucleoprotein complexes (RNPs) that play critical roles
CC in translational repression and mRNA decapping during embryogenesis,
CC oogenesis, neurogenesis and neurotransmission (PubMed:11546740,
CC PubMed:16256742, PubMed:17178403, PubMed:18590813, PubMed:21267420,
CC PubMed:21447556, PubMed:28875934, PubMed:28388438, PubMed:17982591,
CC PubMed:31114929). Recruits core components and translational repressors
CC to some RNP complexes, and mediates RNP aggregation into processing
CC granules such as P-bodies (PubMed:28875934, PubMed:11546740,
CC PubMed:16256742, PubMed:17178403, PubMed:21267420, PubMed:21447556,
CC PubMed:17982591). As part of a RNP complex containing tral, eIF4E1,
CC cup, and pAbp, involved in RNP-mediated translational repression of
CC maternal mRNAs during oogenesis and embryogenesis (PubMed:28875934). As
CC part of a RNP complex containing tral and the RNA localization factors
CC exu and yps, mediates translational silencing of mRNAs such as
CC osk/oskar and bcd/bicoid during their transport to the oocyte in order
CC to prevent their translation until they reach their positional
CC destinations (PubMed:11546740). In neurons and possibly imaginal disks,
CC involved in miRNA-mediated translational repression, possibly in
CC association with components of the piRNA transposon silencing pathway
CC (PubMed:21447556, PubMed:17178403, PubMed:21267420, PubMed:17982591,
CC PubMed:21081899). Involved in RNA localization and protein trafficking
CC in the oocyte (PubMed:11546740, PubMed:16256742). As part of an ER-
CC associated RNP containing tral, cup and yps, required for tral-
CC dependent ER exit site formation and consequently efficient trafficking
CC of proteins such as grk and yl through the secretory pathway
CC (PubMed:16256742). Component of neuron RNPs that mediate transport and
CC translation of neuronal RNAs, including translation repression of
CC synaptic transcripts in preparation for their dendritic targeting
CC (PubMed:17178403, PubMed:21267420, PubMed:28388438). As part of the
CC Atx2-Not1 repressor complex promotes Not1-dependent post-
CC transcriptional gene silencing in adult circadian pacemaker neurons in
CC order to sustain high-amplitude circadian rhythms and Pdf cycling in a
CC per-independent manner (PubMed:28388438). Promotes the interaction
CC between Atx2 and Not1 within the Atx2-Not1 RNP complex
CC (PubMed:28388438). Recruited to the 4EHP-GYF2 complex by Gyf, where it
CC plays a role in 4EHP-GYF2 mediated translational repression and mRNA
CC decay (PubMed:31114929). {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, ECO:0000269|PubMed:31114929}.
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 granules (P-
CC body, nuage, sponge body or polar granules) and P-body-like neuronal
CC RNPs (PubMed:11546740, PubMed:16256742, PubMed:18765641,
CC PubMed:18590813, PubMed:19285948, PubMed:28388438). Consequently it
CC interacts with a wide variety of proteins, some of which appear to be
CC common interactive partners in almost all RNPs types i.e. cup and tral,
CC whereas other interactions are specific to a germ granule/RNP
CC (PubMed:28945271). Core functional components in me31B-containing RNPs
CC include RNA 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 RNPs
CC (PubMed:17178403, PubMed:28945271). In the P-body RNPs, interacts with
CC at least the translation repressor proteins tral, cup and Edc3, and the
CC mRNA localization factor yps (PubMed:16256742, PubMed:18765641,
CC PubMed:18590813, PubMed:19285948). Interaction with tral or Edc3 is
CC required for translation repression and possibly RNA decapping; binding
CC to tral and Edc3 is mutually exclusive (PubMed:18765641,
CC PubMed:19285948). In the nuage and germ plasm polar granule RNPs,
CC interacts with at least tral, cup, and additional proteins required for
CC assembly and function of the germ granules such as tud, vas and aub
CC (PubMed:18765641, PubMed:18590813, PubMed:19285948, PubMed:28945271).
CC Interacts (when dimethylated on Arg residues) with tud; interaction is
CC RNA-independent (PubMed:28945271). Component of the osk RNP complex,
CC which is composed of at least me31B, exu, yps, aret/bruno, cup, and the
CC mRNA of osk (PubMed:10662770). Component of the nos RNP complex, which
CC is composed of at least smg, cup, tral, me31B, the CCR4-NOT complex
CC members Rga/NOT2 and Caf1-55, 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 least
CC me31B, eIF4E1, cup, tral and pAbp; this interaction is required for the
CC translational silencing of maternal mRNAs during the maternal-to-
CC zygotic transition (PubMed:28875934). In the sponge body, forms a RNP
CC containing at least me31B, exu, yps and the mRNA of osk; interactions
CC with exu and yps are RNA dependent (PubMed:11546740). Component of a
CC neuronal RNP, at least composed of me31B, tral and Fmr1
CC (PubMed:17178403). Component of the Atx2-Not1 repressor complex,
CC composed of at least me31B, Atx2, tyf and pAbp (PubMed:28388438).
CC Interacts (via the C-terminus) with Atx2, tyf, pAbp and Lsm12a
CC (PubMed:28388438). Interacts (via RecA-like domain 2) with 4EHP-GYF2
CC complex member Gyf (via the me31B binding motif) (PubMed:31114929,
CC PubMed:31439631). Interacts with 4E-T, Edc3 and Patr-1
CC (PubMed:31439631). {ECO:0000269|PubMed:10662770,
CC ECO:0000269|PubMed:11546740, ECO:0000269|PubMed:16256742,
CC ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:18590813,
CC ECO:0000269|PubMed:18765641, ECO:0000269|PubMed:19285948,
CC ECO:0000269|PubMed:21081899, ECO:0000269|PubMed:21447556,
CC ECO:0000269|PubMed:28388438, ECO:0000269|PubMed:28875934,
CC ECO:0000269|PubMed:28945271, ECO:0000269|PubMed:31114929}.
CC -!- INTERACTION:
CC P23128; 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}. Cytoplasm,
CC Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:11546740,
CC ECO:0000269|PubMed:16256742, ECO:0000269|PubMed:17178403,
CC ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:21267420,
CC ECO:0000269|PubMed:21447556, ECO:0000269|PubMed:28945271}. Cytoplasm,
CC P-body {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 nurse
CC cells, sponge bodies of nurse cells and early egg chambers in oocytes,
CC as well as polar granules in the germ plasm at the posterior pole of
CC mid-late stage oocytes and in early embryos (PubMed:11546740,
CC PubMed:18590813, PubMed:21447556, PubMed:28945271, PubMed:21267420).
CC Component of an RNP that localizes to discrete subdomains of the ER
CC cytoplasmic surface (PubMed:21267420, PubMed:16256742). Also present in
CC cytoplasmic granules in the cell bodies and neuropil area of the
CC antennal lobes (PubMed:21267420). In the olfactory sensory and
CC projection neurons, granules appear to predominately localize to
CC postsynaptic 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 -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout the brain (at
CC protein level) (PubMed:21267420, PubMed:17178403). Expressed in the
CC olfactory system including the antennal lobes, projection neurons,
CC local interneurons, mushroom-body Kenyon cells and glial cells (at
CC protein level) (PubMed:21267420). {ECO:0000269|PubMed:17178403,
CC 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 mid-
CC oogenesis (at protein level) (PubMed:11546740). In early egg chambers
CC detected in nurse cells and oocytes, and later accumulates at the
CC posterior pole of stage 10 oocytes (at protein level)
CC (PubMed:11546740). Expression decreases during the first 5 hours of
CC embryogenesis; expression levels are high during the first 2 hours of
CC embryogenesis then sharply decrease at 2-3 hours and remains low (at
CC protein level) (PubMed:28875934). Ubiquitously expressed in cleavage
CC embryos but is not detected at the cellular blastoderm stage (at
CC protein level) (PubMed:11546740). Expressed both maternally and
CC zygotically (PubMed:1900936). {ECO:0000269|PubMed:11546740,
CC ECO:0000269|PubMed:1900936, 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 loss
CC of Pdf circadian daily oscillations which is consistent with their
CC behavioral arrhythmicity (PubMed:28388438). However, there is no effect
CC on the daily oscillations of pir and tim proteins in Pdf neurons
CC (PubMed:28388438). Double knockdown with Atx2 enhances the behavioral
CC arrhythmicity (PubMed:28388438). RNAi-mediated knockdown in the dorsal-
CC most class IV neurons frequently results in defects in terminal
CC dendrite morphology and dendritic tiling (PubMed:17178403). RNAi-
CC mediated knockdown in adult projection neurons increases levels of the
CC translational reporter protein CaMKII in the antennal lobe
CC (PubMed:21267420). RNAi-mediated knockdown in the anterior/posterior
CC boundary of the wing imaginal disk causes loss of DCP1- and pcm-
CC expressing P-bodies (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}.
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; 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 AlphaFoldDB; P23128; -.
DR SMR; P23128; -.
DR BioGRID; 60455; 44.
DR IntAct; P23128; 16.
DR MINT; P23128; -.
DR STRING; 7227.FBpp0079565; -.
DR iPTMnet; P23128; -.
DR PaxDb; P23128; -.
DR PRIDE; P23128; -.
DR ABCD; P23128; 6 sequenced antibodies.
DR DNASU; 34364; -.
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 VEuPathDB; VectorBase:FBgn0004419; -.
DR eggNOG; KOG0326; Eukaryota.
DR GeneTree; ENSGT00940000170366; -.
DR InParanoid; P23128; -.
DR OMA; TYEDRHT; -.
DR PhylomeDB; P23128; -.
DR Reactome; R-DME-430039; mRNA decay by 5' to 3' exoribonuclease.
DR SignaLink; P23128; -.
DR BioGRID-ORCS; 34364; 1 hit in 1 CRISPR screen.
DR ChiTaRS; me31B; fly.
DR GenomeRNAi; 34364; -.
DR PRO; PR:P23128; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004419; Expressed in egg cell and 31 other tissues.
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; IDA:CACAO.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IGI:FlyBase.
DR GO; GO:0046959; P:habituation; IMP:FlyBase.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IMP:UniProtKB.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IGI:FlyBase.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0033962; P:P-body assembly; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IGI:FlyBase.
DR GO; GO:0060148; P:positive regulation of post-transcriptional 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 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; 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 Cytoplasm; Endoplasmic reticulum; Helicase; Hydrolase; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Translation regulation.
FT CHAIN 1..459
FT /note="ATP-dependent RNA helicase me31b"
FT /id="PRO_0000054982"
FT DOMAIN 89..259
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 269..429
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..267
FT /note="RecA-like domain 1"
FT /evidence="ECO:0000303|PubMed:31439631"
FT REGION 264..431
FT /note="Gyf binding"
FT /evidence="ECO:0000269|PubMed:31439631"
FT REGION 432..459
FT /note="RecA-like domain 2"
FT /evidence="ECO:0000269|PubMed:31439631"
FT MOTIF 58..86
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 207..210
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_019286"
FT MUTAGEN 281
FT /note="Q->A: Abolishes interaction with Edc3; when
FT associated with A-284; A-288 and A-292."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 284
FT /note="H->A: Abolishes interaction with Edc3; when
FT associated with A-281; A-288 and A-292."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 285
FT /note="C->A: In CL-AA; reduced interaction with Gyf and
FT Patr-1 but has no effect on interaction with 4E-T; when
FT associated with A-289."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 288
FT /note="T->A: Abolishes interaction with Edc3; when
FT associated with A-281; A-284 and A-292."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 289
FT /note="L->A: In CL-AA; reduced interaction with Gyf and
FT Patr-1 but has no effect on interaction with 4E-T; when
FT associated with A-285."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 292
FT /note="K->A: Abolishes interaction with Edc3; when
FT associated with A-281; A-284 and A-288."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 310
FT /note="L->A: In LK-AA; reduced interaction with Gyf, Patr-1
FT and 4E-T; when associated with A-314."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 314
FT /note="K->A: In LK-AA; reduced interaction with Gyf, Patr-1
FT and 4E-T; when associated with A-310."
FT /evidence="ECO:0000269|PubMed:31439631"
FT CONFLICT 39..45
FT /note="KLPPKDN -> NCRQRTT (in Ref. 1; AAA28603)"
FT /evidence="ECO:0000305"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:6S8R"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:6S8R"
FT HELIX 427..429
FT /evidence="ECO:0007829|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
