FMR1_DROME
ID FMR1_DROME Reviewed; 684 AA.
AC Q9NFU0; A4V2M8; Q8INM7; Q8T0M0; Q8WQ60; Q95P21; Q9GSG3; Q9TVY4; Q9VH27;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Fragile X messenger ribonucleoprotein 1 homolog {ECO:0000250|UniProtKB:Q06787};
DE AltName: Full=dFMR1 {ECO:0000303|PubMed:11046149};
GN Name=Fmr1 {ECO:0000312|EMBL:AAF14639.1};
GN Synonyms=FXR {ECO:0000312|EMBL:CAB66340.1}; ORFNames=CG6203;
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] {ECO:0000305, ECO:0000312|EMBL:AAG22045.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), SUBUNIT, RNA-BINDING, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ILE-244 AND ILE-307.
RC TISSUE=Ovary {ECO:0000269|PubMed:11046149};
RX PubMed=11046149; DOI=10.1128/mcb.20.22.8536-8547.2000;
RA Wan L., Dockendorff T.C., Jongens T.A., Dreyfuss G.;
RT "Characterization of dFMR1, a Drosophila melanogaster homolog of the
RT fragile X mental retardation protein.";
RL Mol. Cell. Biol. 20:8536-8547(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB66340.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND C), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Berkeley {ECO:0000269|PubMed:11733059};
RC TISSUE=Embryo {ECO:0000269|PubMed:11733059};
RX PubMed=11733059; DOI=10.1016/s0092-8674(01)00589-x;
RA Zhang Y.Q., Bailey A.M., Matthies H.J.G., Renden R.B., Smith M.A.,
RA Speese S.D., Rubin G.M., Broadie K.S.;
RT "Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to
RT control synaptic structure and function.";
RL Cell 107:591-603(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAD19444.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
RC STRAIN=Berkeley {ECO:0000269|Ref.3};
RC TISSUE=Embryo {ECO:0000269|Ref.3}, Ovary {ECO:0000269|Ref.3}, and
RC Testis {ECO:0000312|EMBL:CAC88757.2};
RA Zhang Y.Q., Broadie K.S.;
RT "Modeling human fragile X syndrome in flies.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAF54493.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAF54493.2}
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 [6] {ECO:0000305, ECO:0000312|EMBL:CAD19444.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 105-684 (ISOFORMS C/E).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39327.2}; TISSUE=Embryo, and Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH AGO2; DCR-1; RM62; RPL5 AND RPL11, AND
RP ASSOCIATION WITH POLYRIBOSOME.
RX PubMed=12368261; DOI=10.1101/gad.1022002;
RA Ishizuka A., Siomi M.C., Siomi H.;
RT "A Drosophila fragile X protein interacts with components of RNAi and
RT ribosomal proteins.";
RL Genes Dev. 16:2497-2508(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH VIG; AGO2 AND TUDOR-SN.
RX PubMed=14508492; DOI=10.1038/nature01956;
RA Caudy A.A., Ketting R.F., Hammond S.M., Denli A.M., Bathoorn A.M.,
RA Tops B.B., Silva J.M., Myers M.M., Hannon G.J., Plasterk R.H.;
RT "A micrococcal nuclease homologue in RNAi effector complexes.";
RL Nature 425:411-414(2003).
RN [9]
RP INTERACTION WITH SRA-1.
RX PubMed=12818175; DOI=10.1016/s0896-6273(03)00354-4;
RA Schenck A., Bardoni B., Langmann C., Harden N., Mandel J.-L.,
RA Giangrande A.;
RT "CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the
RT Rac1 GTPase pathway to the fragile X protein.";
RL Neuron 38:887-898(2003).
RN [10] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15183715; DOI=10.1016/j.ydbio.2004.02.010;
RA Zhang Y.Q., Matthies H.J.G., Mancuso J., Andrews H.K., Woodruff E. III,
RA Friedman D., Broadie K.S.;
RT "The Drosophila fragile X-related gene regulates axoneme differentiation
RT during spermatogenesis.";
RL Dev. Biol. 270:290-307(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH PIWI AND VAS.
RX PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
RA Megosh H.B., Cox D.N., Campbell C., Lin H.;
RT "The role of PIWI and the miRNA machinery in Drosophila germline
RT determination.";
RL Curr. Biol. 16:1884-1894(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-408; SER-409;
RP SER-413; SER-532; SER-533; SER-539 AND SER-541, 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).
RN [13]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TRAL AND ME31B, AND SUBCELLULAR
RP LOCATION.
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH YTHDF.
RX PubMed=33428246; DOI=10.15252/embj.2020104975;
RA Worpenberg L., Paolantoni C., Longhi S., Mulorz M.M., Lence T.,
RA Wessels H.H., Dassi E., Aiello G., Sutandy F.X.R., Scheibe M.,
RA Edupuganti R.R., Busch A., Moeckel M.M., Vermeulen M., Butter F.,
RA Koenig J., Notarangelo M., Ohler U., Dieterich C., Quattrone A.,
RA Soldano A., Roignant J.Y.;
RT "Ythdf is a N6-methyladenosine reader that modulates Fmr1 target mRNA
RT selection and restricts axonal growth in Drosophila.";
RL EMBO J. 40:e104975-e104975(2021).
CC -!- FUNCTION: Polyribosome-associated RNA-binding protein that plays a role
CC in neuronal development and synaptic plasticity through the regulation
CC of protein synthesis of mRNAs (PubMed:11046149, PubMed:11733059,
CC PubMed:12368261, PubMed:17178403). Plays a role as a negative
CC translational regulator of specific mRNAs (PubMed:11733059,
CC PubMed:17178403). Represses translation of the microtubule-associated
CC protein futsch mRNA to regulate microtubule-dependent synaptic growth
CC and function (PubMed:11733059). Localizes to specific N6-
CC methyladenosine (m6A)-containing RNAs as part of a complex with the m6A
CC reader Ythdf and thereby regulates axonal growth in the mushroom bodies
CC and neuromuscular junctions (PubMed:33428246). May also be involved in
CC microRNA (miRNA)-mediated translational suppression as part of the RNA-
CC induced silencing complex (RISC) (PubMed:12368261, PubMed:14508492).
CC Required for stability of the central pair of microtubules in the
CC spermatid axoneme (PubMed:15183715). Regulates photoreceptor structure
CC and neuromuscular junction (NMJ) neurotransmission in the eye
CC (PubMed:11733059, PubMed:17178403). During embryogenesis, involved in
CC germline fate determination (PubMed:16949822).
CC {ECO:0000269|PubMed:11046149, ECO:0000269|PubMed:11733059,
CC ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:14508492,
CC ECO:0000269|PubMed:15183715, ECO:0000269|PubMed:16949822,
CC ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:33428246}.
CC -!- SUBUNIT: Homodimer (PubMed:11046149). Interacts with AGO2, Dcr-1, Rm62,
CC vig, RpL5 and RpL11; these interactions form the RNA-induced silencing
CC complex (RISC), a messenger ribonucleoprotein particle (RNP) complex
CC involved in translation regulation (PubMed:12368261, PubMed:14508492).
CC As part of the RISC complex, interacts with Tudor-SN (PubMed:14508492).
CC Component of a neuronal RNP at least composed of Fmr1, tral and me31B
CC (PubMed:17178403). Interacts with piwi and vas; these interactions
CC occur in the polar granules (PubMed:16949822). Interacts with Sra-1
CC (PubMed:12818175). Associates with polyribosome (PubMed:12368261).
CC Interacts with Ythdf; the interaction is RNA independent
CC (PubMed:33428246). {ECO:0000269|PubMed:11046149,
CC ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:12818175,
CC ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:16949822,
CC ECO:0000269|PubMed:17178403, ECO:0000269|PubMed:33428246}.
CC -!- INTERACTION:
CC Q9NFU0; Q9VUQ5: AGO2; NbExp=4; IntAct=EBI-422631, EBI-442476;
CC Q9NFU0; Q9NFU0: Fmr1; NbExp=2; IntAct=EBI-422631, EBI-422631;
CC Q9NFU0; P19109: Rm62; NbExp=4; IntAct=EBI-422631, EBI-200734;
CC Q9NFU0; P46222: RpL11; NbExp=5; IntAct=EBI-422631, EBI-183104;
CC Q9NFU0; Q9NIU2: RpL5; NbExp=5; IntAct=EBI-422631, EBI-605695;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11046149,
CC ECO:0000269|PubMed:17178403}. Perikaryon {ECO:0000269|PubMed:11733059}.
CC Cell projection, neuron projection {ECO:0000269|PubMed:11733059}.
CC Synapse {ECO:0000269|PubMed:11733059}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic
CC ribonucleoprotein granule {ECO:0000269|PubMed:17178403}. Note=Localizes
CC in the neuronal soma and cell processes, and in pre- and postsynaptic
CC neurons, as well as in postsynaptic muscles.
CC {ECO:0000269|PubMed:11733059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A {ECO:0000269|PubMed:11733059};
CC IsoId=Q9NFU0-1; Sequence=Displayed;
CC Name=B {ECO:0000269|Ref.3};
CC IsoId=Q9NFU0-4; Sequence=VSP_050785, VSP_050786, VSP_050787;
CC Name=C {ECO:0000269|PubMed:11733059}; Synonyms=D
CC {ECO:0000303|PubMed:10731132};
CC IsoId=Q9NFU0-2; Sequence=VSP_050784;
CC Name=E {ECO:0000303|PubMed:10731132};
CC IsoId=Q9NFU0-3; Sequence=VSP_050783, VSP_050784;
CC -!- TISSUE SPECIFICITY: Highly expressed in testes in the early stages of
CC spermatogenesis before spermatid individualization (at protein level)
CC (PubMed:15183715). {ECO:0000269|PubMed:15183715}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the embryonic development
CC (PubMed:11046149). Expressed both maternally and zygotically in embryos
CC (PubMed:11046149). Until early gastrulation, expression is uniformly
CC distributed in the embryo (PubMed:11046149). At mid-gastrulation (stage
CC 11), expressed everywhere with discernible concentration in the
CC mesoderm (PubMed:11046149). After gastrulation (stage 14), expressed in
CC the mesoderm, ventral nerve cord, and brain (PubMed:11046149). At stage
CC 16, elevated expression is also seen in the muscle (PubMed:11046149).
CC Highly expressed in nervous system throughout later development (at
CC protein level) (PubMed:11046149, PubMed:11733059).
CC {ECO:0000269|PubMed:11046149, ECO:0000269|PubMed:11733059}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
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DR EMBL; AF305881; AAG22045.1; -; mRNA.
DR EMBL; AF205596; AAF14639.1; -; mRNA.
DR EMBL; AF205597; AAF14640.1; -; Genomic_DNA.
DR EMBL; AJ271221; CAB66340.1; -; mRNA.
DR EMBL; AJ413217; CAC88757.2; -; mRNA.
DR EMBL; AJ422082; CAD19443.1; -; mRNA.
DR EMBL; AJ422083; CAD19444.1; -; mRNA.
DR EMBL; AE014297; AAF54493.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13451.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13452.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13453.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13454.1; -; Genomic_DNA.
DR EMBL; AY069182; AAL39327.2; -; mRNA.
DR EMBL; BT031124; ABX00746.1; -; mRNA.
DR RefSeq; NP_001303443.1; NM_001316514.1. [Q9NFU0-2]
DR RefSeq; NP_001303444.1; NM_001316515.1. [Q9NFU0-2]
DR RefSeq; NP_611645.1; NM_137801.4. [Q9NFU0-1]
DR RefSeq; NP_731443.1; NM_169324.2. [Q9NFU0-2]
DR RefSeq; NP_731444.1; NM_169325.3. [Q9NFU0-2]
DR RefSeq; NP_731445.1; NM_169326.3. [Q9NFU0-3]
DR RefSeq; NP_731446.1; NM_169327.2. [Q9NFU0-4]
DR AlphaFoldDB; Q9NFU0; -.
DR SMR; Q9NFU0; -.
DR BioGRID; 63147; 124.
DR IntAct; Q9NFU0; 22.
DR MINT; Q9NFU0; -.
DR STRING; 7227.FBpp0300445; -.
DR iPTMnet; Q9NFU0; -.
DR PaxDb; Q9NFU0; -.
DR PRIDE; Q9NFU0; -.
DR DNASU; 37528; -.
DR EnsemblMetazoa; FBtr0082196; FBpp0081674; FBgn0028734. [Q9NFU0-4]
DR EnsemblMetazoa; FBtr0082197; FBpp0081675; FBgn0028734. [Q9NFU0-1]
DR EnsemblMetazoa; FBtr0082198; FBpp0081676; FBgn0028734. [Q9NFU0-2]
DR EnsemblMetazoa; FBtr0082199; FBpp0081677; FBgn0028734. [Q9NFU0-2]
DR EnsemblMetazoa; FBtr0082200; FBpp0081678; FBgn0028734. [Q9NFU0-3]
DR EnsemblMetazoa; FBtr0347104; FBpp0312465; FBgn0028734. [Q9NFU0-2]
DR EnsemblMetazoa; FBtr0347105; FBpp0312466; FBgn0028734. [Q9NFU0-2]
DR GeneID; 37528; -.
DR KEGG; dme:Dmel_CG6203; -.
DR UCSC; CG6203-RD; d. melanogaster.
DR CTD; 2332; -.
DR FlyBase; FBgn0028734; Fmr1.
DR VEuPathDB; VectorBase:FBgn0028734; -.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR GeneTree; ENSGT00950000183189; -.
DR InParanoid; Q9NFU0; -.
DR OMA; DQQQRGY; -.
DR PhylomeDB; Q9NFU0; -.
DR SignaLink; Q9NFU0; -.
DR BioGRID-ORCS; 37528; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Fmr1; fly.
DR GenomeRNAi; 37528; -.
DR PRO; PR:Q9NFU0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0028734; Expressed in wing disc and 34 other tissues.
DR ExpressionAtlas; Q9NFU0; baseline and differential.
DR Genevisible; Q9NFU0; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:FlyBase.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0032838; C:plasma membrane bounded cell projection cytoplasm; IDA:FlyBase.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:FlyBase.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0045182; F:translation regulator activity; IMP:CACAO.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IDA:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0050802; P:circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IMP:FlyBase.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0048134; P:germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0007625; P:grooming behavior; IMP:FlyBase.
DR GO; GO:0046959; P:habituation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
DR GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0030517; P:negative regulation of axon extension; IGI:UniProtKB.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IMP:FlyBase.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0051964; P:negative regulation of synapse assembly; IMP:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IDA:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IGI:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:FlyBase.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0048621; P:post-embryonic digestive tract morphogenesis; IMP:FlyBase.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0060998; P:regulation of dendritic spine development; IBA:GO_Central.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IGI:FlyBase.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0090328; P:regulation of olfactory learning; IMP:FlyBase.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; IMP:FlyBase.
DR GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IBA:GO_Central.
DR GO; GO:1990834; P:response to odorant; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0035176; P:social behavior; IMP:FlyBase.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:FlyBase.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR GO; GO:0098883; P:synapse pruning; IMP:FlyBase.
DR GO; GO:0070142; P:synaptic vesicle budding; IMP:FlyBase.
DR GO; GO:0097091; P:synaptic vesicle clustering; IMP:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR022034; FXMRP1_C_core.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR041560; Tudor_FRX1.
DR PANTHER; PTHR10603; PTHR10603; 1.
DR Pfam; PF12235; FXMRP1_C_core; 1.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF17904; KH_9; 1.
DR Pfam; PF18336; Tudor_FRX1; 1.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS51641; AGENET_LIKE; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW RNA-binding; RNA-mediated gene silencing; Sensory transduction; Synapse;
KW Translation regulation; Vision.
FT CHAIN 1..684
FT /note="Fragile X messenger ribonucleoprotein 1 homolog"
FT /id="PRO_0000050109"
FT DOMAIN 1..49
FT /note="Agenet-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT DOMAIN 65..117
FT /note="Agenet-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT DOMAIN 221..282
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 284..353
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 386..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..489
FT /note="RNA-binding RGG-box"
FT COMPBIAS 386..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_050783"
FT VAR_SEQ 321..330
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_050785"
FT VAR_SEQ 321..323
FT /note="Missing (in isoform C and isoform E)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:11046149, ECO:0000303|PubMed:11733059,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.6"
FT /id="VSP_050784"
FT VAR_SEQ 537..539
FT /note="ADS -> DTN (in isoform B)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_050786"
FT VAR_SEQ 540..684
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_050787"
FT MUTAGEN 244
FT /note="I->N: Impairs RNA-binding."
FT /evidence="ECO:0000269|PubMed:11046149"
FT MUTAGEN 307
FT /note="I->N: Impairs RNA-binding."
FT /evidence="ECO:0000269|PubMed:11046149"
FT CONFLICT 343
FT /note="F -> L (in Ref. 1; AAG22045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 76076 MW; 973489A73B97F1FE CRC64;
MEDLLVEVRL DNGAYYKGQV TAVADDGIFV DVDGVPESMK YPFVNVRLPP EETVEVAAPI
FEEGMEVEVF TRTNDRETCG WWVGIIKMRK AEIYAVAYIG FETSYTEICE LGRLRAKNSN
PPITAKTFYQ FTLPVPEELR EEAQKDGIHK EFQRTIDAGV CNYSRDLDAL IVISKFEHTQ
KRASMLKDMH FRNLSQKVML LKRTEEAARQ LETTKLMSRG NYVEEFRVRD DLMGLAIGSH
GSNIQAARTV DGVTNIELEE KSCTFKISGE TEESVQRARA MLEYAEEFFQ VPRELVGKVI
GKNGRIIQEI VDKSGVFRIK VSAIAGDDEQ DQNIPRELAH VPFVFIGTVE SIANAKVLLE
YHLSHLKEVE QLRQEKMEID QQLRAIQESS MGSTQSFPVT RRSERGYSSD IESVRSMRGG
GGGQRGRVRG RGGGGPGGGN GLNQRYHNNR RDEDDYNSRG DHQRDQQRGY NDRGGGDNTG
SYRGGGGGAG GPGNNRRGGI NRRPPRNDQQ NGRDYQHHNH TTEEVRETRE MSSVERADSN
SSYEGSSRRR RRQKNNNGPS NTNGAVANNN NKPQSAQQPQ QQQPPAPGNK AALNAGDASK
QNSGNANAAG GASKPKDASR NGDKQQAGTQ QQQPSQVQQQ QAAQQQQPKP RRNKNRSNNH
TDQPSGQQQL AENVKKEGLV NGTS
