CUP_DROME
ID CUP_DROME Reviewed; 1117 AA.
AC Q9VMA3; O02432;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein cup;
DE AltName: Full=Oskar ribonucleoprotein complex 147 kDa subunit;
GN Name=cup; Synonyms=fs(2)cup; ORFNames=CG11181;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=9118812; DOI=10.1242/dev.124.7.1419;
RA Keyes L.N., Spradling A.C.;
RT "The Drosophila gene fs(2)cup interacts with otu to define a cytoplasmic
RT pathway required for the structure and function of germ-line chromosomes.";
RL Development 124:1419-1431(1997).
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.
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].
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 INTERACTION WITH NOS.
RX PubMed=11060247; DOI=10.1242/dev.127.23.5225;
RA Verrotti A.C., Wharton R.P.;
RT "Nanos interacts with cup in the female germline of Drosophila.";
RL Development 127:5225-5232(2000).
RN [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH BTZ AND EIF-4E.
RX PubMed=14691132; DOI=10.1083/jcb.200309088;
RA Wilhelm J.E., Hilton M., Amos Q., Henzel W.J.;
RT "Cup is an eIF4E binding protein required for both the translational
RT repression of oskar and the recruitment of Barentsz.";
RL J. Cell Biol. 163:1197-1204(2003).
RN [8]
RP FUNCTION, INTERACTION WITH ARET AND EIF-4E, AND MUTAGENESIS OF TYR-327 AND
RP 332-LEU-MET-333.
RX PubMed=14723848; DOI=10.1016/s1534-5807(03)00400-3;
RA Nakamura A., Sato K., Hanyu-Nakamura K.;
RT "Drosophila Cup is an eIF4E binding protein that associates with Bruno and
RT regulates oskar mRNA translation in oogenesis.";
RL Dev. Cell 6:69-78(2004).
RN [9]
RP FUNCTION, INTERACTION WITH SMG AND EIF-4E, AND MUTAGENESIS OF TYR-327;
RP LEU-364 AND LEU-368.
RX PubMed=14685270; DOI=10.1038/sj.emboj.7600026;
RA Nelson M.R., Leidal A.M., Smibert C.A.;
RT "Drosophila Cup is an eIF4E-binding protein that functions in Smaug-
RT mediated translational repression.";
RL EMBO J. 23:150-159(2004).
RN [10]
RP FUNCTION, INTERACTION WITH EIF-4E, AND SUBCELLULAR LOCATION.
RX PubMed=15465908; DOI=10.1073/pnas.0406451101;
RA Zappavigna V., Piccioni F., Villaescusa J.C., Verrotti A.C.;
RT "Cup is a nucleocytoplasmic shuttling protein that interacts with the
RT eukaryotic translation initiation factor 4E to modulate Drosophila ovary
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14800-14805(2004).
RN [11]
RP SUBCELLULAR 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 [12]
RP FUNCTION, INTERACTION WITH NUP154, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17277377; DOI=10.1534/genetics.106.062844;
RA Grimaldi M.R., Cozzolino L., Malva C., Graziani F., Gigliotti S.;
RT "nup154 genetically interacts with cup and plays a cell-type-specific
RT function during Drosophila melanogaster egg-chamber development.";
RL Genetics 175:1751-1759(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-270; SER-347;
RP SER-350; THR-503; SER-509; SER-513; SER-520; SER-523 AND SER-524, 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 [14]
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 [15]
RP FUNCTION, AND INTERACTION WITH EIF-4E; ME31B AND TRAL.
RX PubMed=21937713; DOI=10.1101/gad.17136311;
RA Igreja C., Izaurralde E.;
RT "CUP promotes deadenylation and inhibits decapping of mRNA targets.";
RL Genes Dev. 25:1955-1967(2011).
RN [16]
RP FUNCTION, INTERACTION WITH ORB, AND DISRUPTION PHENOTYPE.
RX PubMed=22164257; DOI=10.1371/journal.pone.0028261;
RA Wong L.C., Schedl P.;
RT "Cup blocks the precocious activation of the orb autoregulatory loop.";
RL PLoS ONE 6:E28261-E28261(2011).
RN [17]
RP FUNCTION, INTERACTION WITH OSK; VAS AND CCR4-NOT COMPLEX, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22454519; DOI=10.1242/jcs.095208;
RA Ottone C., Gigliotti S., Giangrande A., Graziani F.,
RA Verrotti di Pianella A.;
RT "The translational repressor Cup is required for germ cell development in
RT Drosophila.";
RL J. Cell Sci. 125:3114-3123(2012).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=24335285; DOI=10.1093/nar/gkt1265;
RA Kamenska A., Lu W.T., Kubacka D., Broomhead H., Minshall N., Bushell M.,
RA Standart N.;
RT "Human 4E-T represses translation of bound mRNAs and enhances microRNA-
RT mediated silencing.";
RL Nucleic Acids Res. 42:3298-3313(2014).
RN [19]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH EIF4E1; ME31B; 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 during
RT the Drosophila maternal-to-zygotic transition.";
RL Elife 6:0-0(2017).
RN [20] {ECO:0007744|PDB:4AXG}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 296-425 IN COMPLEX WITH EIF4E1,
RP AND INTERACTION WITH EIF4E1.
RX PubMed=22832024; DOI=10.1261/rna.033639.112;
RA Kinkelin K., Veith K., Grunwald M., Bono F.;
RT "Crystal structure of a minimal eIF4E-Cup complex reveals a general
RT mechanism of eIF4E regulation in translational repression.";
RL RNA 18:1624-1634(2012).
CC -!- FUNCTION: Adapter protein that plays a central role in localization of
CC transcripts in the oocyte and in young embryos (PubMed:9118812).
CC Maintains RNA targets in a repressed state by promoting their
CC deadenylation and protects deadenylated mRNAs from further degradation
CC (PubMed:21937713). Binds to and recruits eIF-4E to the 3'-UTR of some
CC mRNA targets which prevents interaction between eIF4E1 and eIF4G
CC (PubMed:14685270, PubMed:15465908, PubMed:21081899). This may
CC contribute to translational repression but does not appear to be
CC necessary for it to occur (PubMed:21081899). Can promote translational
CC repression independently of deadenylation and eIF4E1 binding
CC (PubMed:21937713). Required for correct localization of eIF4E1 in the
CC developing oocyte (PubMed:15465908). Required for translational
CC repression of oskar (osk) mRNA (PubMed:14691132, PubMed:14723848). Also
CC required for the translational repression of nanos (nos) mRNA
CC (PubMed:21081899). Promotes the accumulation of the germ plasm
CC components osk, vas and stau at the posterior pole of the oocyte and is
CC required for germ cell development (PubMed:22454519, PubMed:17277377).
CC Represses orb positive autoregulatory activity which prevents premature
CC activation of orb and ensures its accumulation specifically in the
CC developing oocyte (PubMed:22164257). In 0-1 hour embryos, forms a
CC complex with me31B, cup, tral and pAbp which binds to various mRNAs
CC including maternal mRNAs, and down-regulates their expression during
CC the maternal-to-zygotic transition (PubMed:28875934).
CC {ECO:0000269|PubMed:14685270, ECO:0000269|PubMed:14691132,
CC ECO:0000269|PubMed:14723848, ECO:0000269|PubMed:15465908,
CC ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:21081899,
CC ECO:0000269|PubMed:21937713, ECO:0000269|PubMed:22164257,
CC ECO:0000269|PubMed:22454519, ECO:0000269|PubMed:28875934,
CC ECO:0000269|PubMed:9118812}.
CC -!- SUBUNIT: Component of the osk RNP complex, which is composed of at
CC least exu, yps, aret/bruno, cup, and the mRNA of osk (PubMed:10662770).
CC Interacts with the decapping activators me31B and tral
CC (PubMed:21937713). Component of the nos RNP complex, which is composed
CC of at least smg, cup, tral, me31B, the CCR4-NOT complex members
CC Rga/NOT2 and Caf1, and the mRNA of nos (PubMed:21081899). Interacts
CC with btz (PubMed:14691132, PubMed:14723848). Recruited to the 3'-UTR of
CC nos and osk mRNAs by smg and btz, respectively (PubMed:14685270,
CC PubMed:14691132). Forms a ribonucleoprotein complex (RNP) containing at
CC least me31B, eIF4E1, cup, tral and pAbp; this interaction is required
CC for the translational silencing of maternal mRNAs during the maternal-
CC to-zygotic transition (PubMed:28875934). No interaction was detected
CC with pAbp in 1-5 hour embryos (PubMed:28875934). Interacts with osk and
CC vas (PubMed:22454519). Interacts with Pop2, twin/CCR4, Rga, Not3 and
CC Not1 which are all core components of the CCR4-NOT deadenylase complex;
CC interaction with the complex is required for cup deadenylation activity
CC (PubMed:21937713). Interacts with nos (PubMed:11060247). Interacts with
CC smg (PubMed:14685270). Interacts (via YXXXXLphi motifs) with eIF4E1;
CC the interaction promotes retention of cup in the cytoplasm
CC (PubMed:14723848, PubMed:14685270, PubMed:15465908, PubMed:21937713,
CC PubMed:22832024). Interacts with orb; the interaction represses the orb
CC positive autoregulatory loop (PubMed:22164257). Interacts with Nup154
CC (PubMed:17277377). {ECO:0000269|PubMed:10662770,
CC ECO:0000269|PubMed:11060247, ECO:0000269|PubMed:14685270,
CC ECO:0000269|PubMed:14691132, ECO:0000269|PubMed:14723848,
CC ECO:0000269|PubMed:15465908, ECO:0000269|PubMed:17277377,
CC ECO:0000269|PubMed:21081899, ECO:0000269|PubMed:21937713,
CC ECO:0000269|PubMed:22164257, ECO:0000269|PubMed:22454519,
CC ECO:0000269|PubMed:22832024, ECO:0000269|PubMed:28875934}.
CC -!- INTERACTION:
CC Q9VMA3; P48598: eIF4E1; NbExp=6; IntAct=EBI-95398, EBI-198574;
CC Q9VMA3; P23128: me31B; NbExp=3; IntAct=EBI-95398, EBI-300281;
CC Q9VMA3; Q23972: smg; NbExp=4; IntAct=EBI-95398, EBI-108638;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465908,
CC ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:24335285,
CC ECO:0000269|PubMed:9118812}. Nucleus {ECO:0000269|PubMed:15465908,
CC ECO:0000269|PubMed:24335285}. Cytoplasm, Cytoplasmic ribonucleoprotein
CC granule {ECO:0000269|PubMed:17178403}. Note=Retained in the cytoplasm
CC by interaction with eIF4E1. Located throughout the cytoplasm of all
CC germline cells and is excluded from the nucleus of nurse cells, oocytes
CC and follicular cells (PubMed:15465908). During oogenesis, accumulates
CC in the cytoplasm at the posterior end of the forming oocyte
CC (PubMed:15465908). Component of the germ plasm in developing oocytes
CC (PubMed:22454519). Does not localizes in processing bodies (P-bodies)
CC (PubMed:24335285). {ECO:0000269|PubMed:15465908,
CC ECO:0000269|PubMed:22454519, ECO:0000269|PubMed:24335285}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in ovaries and in 0-2 hours
CC old embryos. Weakly expressed in testis. Expressed in young embryos
CC through stage 9, then it decreases throughout the rest of
CC embryogenesis. In ovaries, it is expressed in germ cells throughout
CC pre-vitellogenic development, but is not expressed in the somatic
CC follicle cells. In germarial cysts, the protein (and not the
CC transcripts) is transported selectively into the oocyte.
CC {ECO:0000269|PubMed:9118812}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the egg chamber and more specifically
CC in nurse cells (at protein level) (PubMed:17277377). Expressed during
CC the first 2 hours of embryogenesis but is absent in 2-5 hour embryos
CC (at protein level) (PubMed:28875934). Expressed both maternally and
CC zygotically (PubMed:9118812). Expressed throughout embryogenesis
CC (PubMed:22454519). In stage 2, uniformly distributed throughout the
CC whole embryo (PubMed:22454519). During blastoderm formation,
CC concentrated at the posterior pole to become incorporated into newly
CC formed germ cells (PubMed:22454519). Subsequently accumulates
CC specifically in the pole cells at stage 10, when they migrate through
CC the posterior midgut primordium, and during stage 14, when the germ
CC cells reach their final destination (PubMed:22454519).
CC {ECO:0000269|PubMed:22454519, ECO:0000269|PubMed:28875934}.
CC -!- DOMAIN: The YXXXXLphi motifs mediate interaction with eIF4E1.
CC {ECO:0000269|PubMed:14685270, ECO:0000269|PubMed:14723848}.
CC -!- DISRUPTION PHENOTYPE: Mislocalization and precocious expression of orb
CC in the ovary, accumulation of high levels of orb in nurse cells,
CC elongation of orb poly-A tails, hyperphosphorylation of orb and reduced
CC osk mRNA levels (PubMed:22164257). Reduced number of germ cells
CC (PubMed:22454519). {ECO:0000269|PubMed:22164257,
CC ECO:0000269|PubMed:22454519}.
CC -!- SIMILARITY: Belongs to the 4E-T/EIF4E-T family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64427.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL39852.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF004917; AAB64427.1; ALT_INIT; mRNA.
DR EMBL; AE014134; AAF52418.3; -; Genomic_DNA.
DR EMBL; AY069707; AAL39852.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285687.1; NM_001298758.1.
DR RefSeq; NP_523493.3; NM_078769.3.
DR PDB; 4AXG; X-ray; 2.80 A; C/D=296-425.
DR PDBsum; 4AXG; -.
DR AlphaFoldDB; Q9VMA3; -.
DR SMR; Q9VMA3; -.
DR BioGRID; 60088; 64.
DR ComplexPortal; CPX-3177; eIF4E-cup complex.
DR DIP; DIP-17920N; -.
DR ELM; Q9VMA3; -.
DR IntAct; Q9VMA3; 10.
DR MINT; Q9VMA3; -.
DR STRING; 7227.FBpp0288761; -.
DR iPTMnet; Q9VMA3; -.
DR PaxDb; Q9VMA3; -.
DR PRIDE; Q9VMA3; -.
DR EnsemblMetazoa; FBtr0290322; FBpp0288761; FBgn0000392.
DR EnsemblMetazoa; FBtr0346452; FBpp0312102; FBgn0000392.
DR GeneID; 33934; -.
DR KEGG; dme:Dmel_CG11181; -.
DR UCSC; CG11181-RB; d. melanogaster.
DR CTD; 33934; -.
DR FlyBase; FBgn0000392; cup.
DR VEuPathDB; VectorBase:FBgn0000392; -.
DR eggNOG; ENOG502SXKW; Eukaryota.
DR HOGENOM; CLU_278765_0_0_1; -.
DR InParanoid; Q9VMA3; -.
DR OMA; MGMSNNR; -.
DR PhylomeDB; Q9VMA3; -.
DR SignaLink; Q9VMA3; -.
DR BioGRID-ORCS; 33934; 0 hits in 1 CRISPR screen.
DR ChiTaRS; cup; fly.
DR GenomeRNAi; 33934; -.
DR PRO; PR:Q9VMA3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000392; Expressed in ovary and 13 other tissues.
DR Genevisible; Q9VMA3; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0045182; F:translation regulator activity; IDA:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IGI:UniProtKB.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IDA:UniProtKB.
DR GO; GO:1905536; P:negative regulation of eukaryotic translation initiation factor 4F complex assembly; IDA:FlyBase.
DR GO; GO:0007319; P:negative regulation of oskar mRNA translation; IDA:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IMP:FlyBase.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:FlyBase.
DR GO; GO:0030715; P:oocyte growth in germarium-derived egg chamber; IGI:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007297; P:ovarian follicle cell migration; HMP:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR DisProt; DP01494; -.
DR IDEAL; IID50295; -.
DR InterPro; IPR018862; eIF4E-T.
DR PANTHER; PTHR12269; PTHR12269; 2.
DR Pfam; PF10477; EIF4E-T; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Oogenesis; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1117
FT /note="Protein cup"
FT /id="PRO_0000079561"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 327..333
FT /note="YXXXXLphi motif 1"
FT /evidence="ECO:0000269|PubMed:14685270,
FT ECO:0000269|PubMed:14723848"
FT MOTIF 363..369
FT /note="YXXXXLphi motif 2"
FT /evidence="ECO:0000269|PubMed:14685270"
FT COMPBIAS 51..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 327
FT /note="Y->A: Strong reduction in interaction with eIF4E1.
FT Strong reduction in interaction with eIF4E1; when
FT associated with A-332 and A-348. Complete loss of
FT interaction with eIF4E1; when associated with A-364 and A-
FT 368."
FT /evidence="ECO:0000269|PubMed:14685270,
FT ECO:0000269|PubMed:14723848"
FT MUTAGEN 332..333
FT /note="LM->AA: Reduction in interaction with eIF4E1. Strong
FT reduction in interaction with eIF4E1; when associated with
FT A-327."
FT /evidence="ECO:0000269|PubMed:14723848"
FT MUTAGEN 364
FT /note="L->A: Mild reduction in interaction with eIF4E1.
FT Complete loss of interaction with eIF4E1; when associated
FT with A-327 and A-368."
FT /evidence="ECO:0000269|PubMed:14685270"
FT MUTAGEN 368
FT /note="L->A: Mild reduction in interaction with eIF4E1.
FT Complete loss of interaction with eIF4E1; when associated
FT with A-327 and A-364."
FT /evidence="ECO:0000269|PubMed:14685270"
FT CONFLICT 836
FT /note="H -> Q (in Ref. 1; AAB64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="N -> K (in Ref. 1; AAB64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="K -> Q (in Ref. 1; AAB64427)"
FT /evidence="ECO:0000305"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:4AXG"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:4AXG"
SQ SEQUENCE 1117 AA; 125672 MW; 91274997F199EFD3 CRC64;
MQMAEAEQEN GAGALKIATN AGATDRPAHQ QLPLPVEDQQ DEVLTPAEKG KFEYPPPPPP
PTPVQAPLAT KATALNASQE HDDDEANSEK WEDPCAPPPP PPLPTSAFLA TGLGYLKLPA
FKLKDALEKA ITKLEANKRT LKASPESSRS IKNKNVVALE MLPRRSNPET IGDGSMLAST
STAVMLQTKK PAVIVEMERR CKIINLLAKQ NQILESISGE AIPMHGPSKH LHEDEGLTLQ
VLSARASTPY TQPSSMLSCT AVSCDLEHDS PRKQVASKEA VPEQQSSQVQ QKRPPSTGIH
KPGSLRAPKA VRPTTAPVVS SKPVKSYTRS RLMDIRNGMF NALMHRSKES FVMPRIATCD
DIELEGRLRR MNIWRTSDGT RFRTRSTTAN LNMNNNNNNE CMPAFFKNKN KPNLISDESI
IQSQPPQPQT EFQDPAIVNQ RRIGSGRLNH SKWGYNDEDY HSYHNGKSQH MEEVNSKNSK
NMTVLQFFDN GEISSQPQRR PNTPVMGMSI NRSENDTLHS NESSEDLSRA NENYVKRVMS
GFLVVSKPKS RDVEDRHHRR YRNQNEEPEW FSCGPTSRLD TIELCGFDED EEKMLKEGNK
NHGLGETERE TSKQKMDHKY KWTHAEPMGR SKYMPKHDTN NNHNVENMNN VMATEHQQQK
EEKRPGSGRS FQFDKFNQSQ QNYESSSYVN HQQPPQTQPQ QMQQQSNTNT NNSKFMSFFA
NEGNSSSSSL NEFFKQAINQ GHGNNPEQPK SLGHIGQMPS VDQLEAKWRR NSLNNVGETA
NKQTDNFQKL IGSLSSAKPQ SQAVGYDAIS NFIMQQQQYQ QQQQKQHLII QQQQQHTAFL
ASLQLKAILG RADTQLLLLR LTKGEISKHG LLVQLANPRL TDMDREAITA VLQFTNTQQQ
QQQHKQQLDM LSSTVIASQL QNLHNLAIVQ QTLAARQQPQ HNPQTQAPHQ LSQEDLQAHA
NVIMRNAVMK RKIEEQTSKL INGGAKHQAQ QQYLNRGQQR QARPDANSNA LLHALISGGG
NNHASGYPMN GQPQKHHSNL RFGDNQNFQS FESNQPHFAT QYKQQYQQSQ QQHPHQQPQQ
LNSLHQNNAG AVNSFNKAQM QAQSAISMLP NSGDEFH
