MGN_DROME
ID MGN_DROME Reviewed; 147 AA.
AC P49028; Q9W2L3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein mago nashi;
GN Name=mago {ECO:0000312|FlyBase:FBgn0002736};
GN Synonyms=mgn {ECO:0000312|FlyBase:FBgn0002736}; ORFNames=CG9401;
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 [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF GLY-19 AND ILE-91.
RX PubMed=8026338; DOI=10.1242/dev.120.5.1303;
RA Newmark P.A., Boswell R.E.;
RT "The mago nashi locus encodes an essential product required for germ plasm
RT assembly in Drosophila.";
RL Development 120:1303-1313(1994).
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 FUNCTION.
RX PubMed=9272960; DOI=10.1242/dev.124.16.3197;
RA Newmark P.A., Mohr S.E., Gong L., Boswell R.E.;
RT "Mago nashi mediates the posterior follicle cell-to-oocyte signal to
RT organize axis formation in Drosophila.";
RL Development 124:3197-3207(1997).
RN [6]
RP FUNCTION.
RX PubMed=9210377; DOI=10.1016/s0960-9822(06)00218-1;
RA Micklem D.R., Dasgupta R., Elliott H., Gergely F., Davidson C., Brand A.,
RA Gonzalez-Reyes A., St Johnston D.;
RT "The mago nashi gene is required for the polarisation of the oocyte and the
RT formation of perpendicular axes in Drosophila.";
RL Curr. Biol. 7:468-478(1997).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE EJC COMPLEX, INTERACTION WITH EIF4AIII,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14973490; DOI=10.1038/nature02351;
RA Palacios I.M., Gatfield D., St Johnston D., Izaurralde E.;
RT "An eIF4AIII-containing complex required for mRNA localization and
RT nonsense-mediated mRNA decay.";
RL Nature 427:753-757(2004).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLU-21.
RX PubMed=20946982; DOI=10.1016/j.cell.2010.09.036;
RA Roignant J.Y., Treisman J.E.;
RT "Exon junction complex subunits are required to splice Drosophila MAP
RT kinase, a large heterochromatic gene.";
RL Cell 143:238-250(2010).
RN [9]
RP FUNCTION.
RX PubMed=20946983; DOI=10.1016/j.cell.2010.09.014;
RA Ashton-Beaucage D., Udell C.M., Lavoie H., Baril C., Lefrancois M.,
RA Chagnon P., Gendron P., Caron-Lizotte O., Bonneil E., Thibault P.,
RA Therrien M.;
RT "The exon junction complex controls the splicing of MAPK and other long
RT intron-containing transcripts in Drosophila.";
RL Cell 143:251-262(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH PYM.
RX PubMed=24967911; DOI=10.1371/journal.pgen.1004455;
RA Ghosh S., Obrdlik A., Marchand V., Ephrussi A.;
RT "The EJC binding and dissociating activity of PYM is regulated in
RT Drosophila.";
RL PLoS Genet. 10:E1004455-E1004455(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH TSU.
RX PubMed=12704080; DOI=10.1101/gad.260403;
RA Shi H., Xu R.-M.;
RT "Crystal structure of the Drosophila Mago nashi-Y14 complex.";
RL Genes Dev. 17:971-976(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH TSU, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12730685; DOI=10.1038/nsb926;
RA Fribourg S., Gatfield D., Izaurralde E., Conti E.;
RT "A novel mode of RBD-protein recognition in the Y14-Mago complex.";
RL Nat. Struct. Biol. 10:433-439(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH TSU AND PYM.
RX PubMed=14968132; DOI=10.1038/sj.embor.7400091;
RA Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.;
RT "Molecular insights into the interaction of PYM with the Mago-Y14 core of
RT the exon junction complex.";
RL EMBO Rep. 5:304-310(2004).
CC -!- FUNCTION: Core component of the splicing-dependent multiprotein exon
CC junction complex (EJC) deposited at splice junctions on mRNAs
CC (PubMed:14973490, PubMed:24967911). Involved in exon definition of
CC genes containing long introns, including the rolled/MAPK gene
CC (PubMed:20946982, PubMed:20946983). The mago-tsu heterodimer interacts
CC with the EJC key regulator Pym leading to EJC disassembly in the
CC cytoplasm (PubMed:24967911). Has a role in oskar mRNA localization to
CC the posterior pole of the developing oocyte, and may also be involved
CC in polarization of the oocyte microtubule cytoskeleton (PubMed:8026338,
CC PubMed:9272960). {ECO:0000269|PubMed:12730685,
CC ECO:0000269|PubMed:24967911, ECO:0000269|PubMed:8026338,
CC ECO:0000269|PubMed:9210377, ECO:0000269|PubMed:9272960}.
CC -!- SUBUNIT: Heterodimer with tsu/RBM8A (PubMed:12704080, PubMed:12730685,
CC PubMed:14968132). Part of the mRNA splicing-dependent exon junction
CC complex (EJC) complex; the core complex contains btz/CASC3, eIF4AIII,
CC mago and tsu/RBM8A (PubMed:14973490). Interacts with Pym (via N-
CC terminus); the interaction is direct (PubMed:24967911,
CC PubMed:14968132). Interacts with eIF4AIII (PubMed:14973490).
CC {ECO:0000269|PubMed:12704080, ECO:0000269|PubMed:12730685,
CC ECO:0000269|PubMed:14968132, ECO:0000269|PubMed:24967911}.
CC -!- INTERACTION:
CC P49028; Q9V535: tsu; NbExp=6; IntAct=EBI-159609, EBI-172458;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730685}. Cytoplasm
CC {ECO:0000269|PubMed:12730685}. Note=Part of the EJC assembled on mRNAs
CC in the nucleus and remains part of the complex when mRNA moves into the
CC cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:8026338). Localizes to the posterior pole of the oocyte during
CC stage 9 of oogenesis (PubMed:14973490). {ECO:0000269|PubMed:14973490,
CC ECO:0000269|PubMed:8026338}.
CC -!- MISCELLANEOUS: 'Mago nashi' means 'without grandchildren' in Japanese.
CC -!- SIMILARITY: Belongs to the mago nashi family. {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; U03559; AAC13746.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46677.1; -; Genomic_DNA.
DR EMBL; AY071060; AAL48682.1; -; mRNA.
DR RefSeq; NP_476636.1; NM_057288.4.
DR PDB; 1HL6; X-ray; 2.50 A; B/D=1-147.
DR PDB; 1OO0; X-ray; 1.85 A; A=1-147.
DR PDB; 1RK8; X-ray; 1.90 A; B=1-147.
DR PDB; 2X1G; X-ray; 3.35 A; B/D=1-147.
DR PDBsum; 1HL6; -.
DR PDBsum; 1OO0; -.
DR PDBsum; 1RK8; -.
DR PDBsum; 2X1G; -.
DR AlphaFoldDB; P49028; -.
DR SMR; P49028; -.
DR BioGRID; 63039; 19.
DR ComplexPortal; CPX-3100; mago-y14 exon-exon junction subcomplex.
DR ComplexPortal; CPX-3147; PYM-mago-Y14 complex.
DR ComplexPortal; CPX-3171; cdm-mago-Y14 complex.
DR DIP; DIP-23439N; -.
DR IntAct; P49028; 6.
DR STRING; 7227.FBpp0071497; -.
DR PaxDb; P49028; -.
DR PRIDE; P49028; -.
DR EnsemblMetazoa; FBtr0071569; FBpp0071497; FBgn0002736.
DR GeneID; 37402; -.
DR KEGG; dme:Dmel_CG9401; -.
DR CTD; 37402; -.
DR FlyBase; FBgn0002736; mago.
DR VEuPathDB; VectorBase:FBgn0002736; -.
DR eggNOG; KOG3392; Eukaryota.
DR GeneTree; ENSGT00390000003156; -.
DR HOGENOM; CLU_109497_1_1_1; -.
DR InParanoid; P49028; -.
DR OMA; VSECEIM; -.
DR OrthoDB; 1373136at2759; -.
DR PhylomeDB; P49028; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P49028; -.
DR BioGRID-ORCS; 37402; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P49028; -.
DR GenomeRNAi; 37402; -.
DR PRO; PR:P49028; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0002736; Expressed in wing disc and 50 other tissues.
DR ExpressionAtlas; P49028; baseline and differential.
DR Genevisible; P49028; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0035145; C:exon-exon junction complex; IPI:FlyBase.
DR GO; GO:1990501; C:exon-exon junction subcomplex mago-y14; IPI:ComplexPortal.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0045495; C:pole plasm; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051170; P:import into nucleus; IDA:ComplexPortal.
DR GO; GO:0046594; P:maintenance of pole plasm mRNA location; TAS:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000335; P:negative regulation of transposition, DNA-mediated; IMP:FlyBase.
DR GO; GO:0051168; P:nuclear export; IDA:ComplexPortal.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; TAS:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; TAS:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IDA:ComplexPortal.
DR GO; GO:0008380; P:RNA splicing; IMP:FlyBase.
DR CDD; cd11295; Mago_nashi; 1.
DR Gene3D; 3.30.1560.10; -; 1.
DR InterPro; IPR004023; Mago_nashi.
DR InterPro; IPR036605; Mago_nashi_sf.
DR PANTHER; PTHR12638; PTHR12638; 1.
DR Pfam; PF02792; Mago_nashi; 1.
DR SUPFAM; SSF89817; SSF89817; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Reference proteome; RNA-binding;
KW Transport.
FT CHAIN 1..147
FT /note="Protein mago nashi"
FT /id="PRO_0000174144"
FT MUTAGEN 19
FT /note="G->R: In allele mago-1; zygotic lethal."
FT /evidence="ECO:0000269|PubMed:8026338"
FT MUTAGEN 21
FT /note="E->K: In allele mago-93D; expression of rolled/MAPK
FT in developing eye and wing tissue is severely reduced, and
FT photoreceptor differentiation is impaired."
FT /evidence="ECO:0000269|PubMed:20946982"
FT MUTAGEN 91
FT /note="I->T: In allele mago-WE7; zygotic lethal."
FT /evidence="ECO:0000269|PubMed:8026338"
FT STRAND 6..16
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1OO0"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:1OO0"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2X1G"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1OO0"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1RK8"
FT HELIX 117..142
FT /evidence="ECO:0007829|PDB:1OO0"
SQ SEQUENCE 147 AA; 17311 MW; B9A2CBFCC5EBEFED CRC64;
MSTEDFYLRY YVGHKGKFGH EFLEFEFRPD GKLRYANNSN YKNDTMIRKE AFVHQSVMEE
LKRIIIDSEI MQEDDLPWPP PDRVGRQELE IVIGDEHISF TTSKTGSLVD VNRSKDPEGL
RCFYYLVQDL KCLVFSLIGL HFKIKPI
