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Protein

Protein mago nashi

Gene

mago

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:14973490, PubMed:24967911). Involved in exon definition of genes containing long introns, including the rolled/MAPK gene (PubMed:20946982, PubMed:20946983). The mago-tsu heterodimer interacts with the EJC key regulator Pym leading to EJC disassembly in the cytoplasm (PubMed:24967911). Has a role in oskar mRNA localization to the posterior pole of the developing oocyte, and may also be involved in polarization of the oocyte microtubule cytoskeleton (PubMed:8026338, PubMed:9272960).5 Publications

GO - Molecular functioni

GO - Biological processi

  • cell-cell signaling Source: FlyBase
  • epidermal growth factor receptor signaling pathway Source: FlyBase
  • maintenance of pole plasm mRNA location Source: FlyBase
  • microtubule cytoskeleton organization Source: FlyBase
  • mRNA export from nucleus Source: FlyBase
  • mRNA splicing, via spliceosome Source: FlyBase
  • negative regulation of transposition, DNA-mediated Source: FlyBase
  • oocyte axis specification Source: FlyBase
  • oocyte microtubule cytoskeleton organization Source: FlyBase
  • oocyte microtubule cytoskeleton polarization Source: FlyBase
  • oogenesis Source: FlyBase
  • pole plasm assembly Source: FlyBase
  • pole plasm oskar mRNA localization Source: FlyBase
  • pole plasm protein localization Source: FlyBase
  • positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  • positive regulation of Ras protein signal transduction Source: FlyBase
  • protein localization Source: FlyBase
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • RNA splicing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-109688. Cleavage of Growing Transcript in the Termination Region.
R-DME-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-DME-72163. mRNA Splicing - Major Pathway.
R-DME-72187. mRNA 3'-end processing.
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Protein mago nashi
Gene namesi
Name:magoImported
Synonyms:mgnImported
ORF Names:CG9401
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0002736. mago.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: Part of the EJC assembled on mRNAs in the nucleus and remains part of the complex when mRNA moves into the cytoplasm.

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: FlyBase
  • cytoplasm Source: FlyBase
  • exon-exon junction complex Source: FlyBase
  • nucleus Source: FlyBase
  • pole plasm Source: FlyBase
  • precatalytic spliceosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191G → R in allele mago-1; zygotic lethal. 1 Publication
Mutagenesisi21 – 211E → K in allele mago-93D; expression of rolled/MAPK in developing eye and wing tissue is severely reduced, and photoreceptor differentiation is impaired. 1 Publication
Mutagenesisi91 – 911I → T in allele mago-WE7; zygotic lethal. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Protein mago nashiPRO_0000174144Add
BLAST

Proteomic databases

PaxDbiP49028.
PRIDEiP49028.

Expressioni

Developmental stagei

Expressed both maternally and zygotically (PubMed:8026338). Localizes to the posterior pole of the oocyte during stage 9 of oogenesis (PubMed:14973490).2 Publications

Gene expression databases

BgeeiP49028.
GenevisibleiP49028. DM.

Interactioni

Subunit structurei

Heterodimer with tsu/RBM8A (PubMed:12704080, PubMed:12730685, PubMed:14968132). Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains btz/CASC3, eIF4AIII, mago and tsu/RBM8A (PubMed:14973490). Interacts with Pym (via N-terminus); the interaction is direct (PubMed:24967911, PubMed:14968132). Interacts with eIF4AIII (PubMed:14973490).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tsuQ9V5356EBI-159609,EBI-172458

Protein-protein interaction databases

BioGridi63039. 6 interactions.
DIPiDIP-23439N.
IntActiP49028. 6 interactions.
MINTiMINT-788898.
STRINGi7227.FBpp0071497.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1611Combined sources
Beta strandi19 – 279Combined sources
Beta strandi31 – 388Combined sources
Beta strandi47 – 537Combined sources
Helixi55 – 6814Combined sources
Helixi70 – 723Combined sources
Beta strandi75 – 784Combined sources
Beta strandi83 – 9311Combined sources
Beta strandi96 – 1027Combined sources
Helixi108 – 1136Combined sources
Beta strandi114 – 1163Combined sources
Helixi117 – 14226Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HL6X-ray2.50B/D1-147[»]
1OO0X-ray1.85A1-147[»]
1RK8X-ray1.90B1-147[»]
2X1GX-ray3.35B/D1-147[»]
ProteinModelPortaliP49028.
SMRiP49028. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49028.

Family & Domainsi

Sequence similaritiesi

Belongs to the mago nashi family.Curated

Phylogenomic databases

eggNOGiKOG3392. Eukaryota.
ENOG4111FJ7. LUCA.
GeneTreeiENSGT00390000003156.
InParanoidiP49028.
KOiK12877.
OMAiKEDDTNW.
OrthoDBiEOG7F24VD.
PhylomeDBiP49028.

Family and domain databases

Gene3Di3.30.1560.10. 1 hit.
InterProiIPR004023. Mago_nashi.
[Graphical view]
PANTHERiPTHR12638. PTHR12638. 1 hit.
PfamiPF02792. Mago_nashi. 1 hit.
[Graphical view]
SUPFAMiSSF89817. SSF89817. 1 hit.

Sequencei

Sequence statusi: Complete.

P49028-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEDFYLRY YVGHKGKFGH EFLEFEFRPD GKLRYANNSN YKNDTMIRKE
60 70 80 90 100
AFVHQSVMEE LKRIIIDSEI MQEDDLPWPP PDRVGRQELE IVIGDEHISF
110 120 130 140
TTSKTGSLVD VNRSKDPEGL RCFYYLVQDL KCLVFSLIGL HFKIKPI
Length:147
Mass (Da):17,311
Last modified:February 1, 1996 - v1
Checksum:iB9A2CBFCC5EBEFED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03559 Genomic DNA. Translation: AAC13746.1.
AE013599 Genomic DNA. Translation: AAF46677.1.
AY071060 mRNA. Translation: AAL48682.1.
RefSeqiNP_476636.1. NM_057288.4.
UniGeneiDm.19970.

Genome annotation databases

EnsemblMetazoaiFBtr0071569; FBpp0071497; FBgn0002736.
GeneIDi37402.
KEGGidme:Dmel_CG9401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03559 Genomic DNA. Translation: AAC13746.1.
AE013599 Genomic DNA. Translation: AAF46677.1.
AY071060 mRNA. Translation: AAL48682.1.
RefSeqiNP_476636.1. NM_057288.4.
UniGeneiDm.19970.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HL6X-ray2.50B/D1-147[»]
1OO0X-ray1.85A1-147[»]
1RK8X-ray1.90B1-147[»]
2X1GX-ray3.35B/D1-147[»]
ProteinModelPortaliP49028.
SMRiP49028. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63039. 6 interactions.
DIPiDIP-23439N.
IntActiP49028. 6 interactions.
MINTiMINT-788898.
STRINGi7227.FBpp0071497.

Proteomic databases

PaxDbiP49028.
PRIDEiP49028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071569; FBpp0071497; FBgn0002736.
GeneIDi37402.
KEGGidme:Dmel_CG9401.

Organism-specific databases

CTDi37402.
FlyBaseiFBgn0002736. mago.

Phylogenomic databases

eggNOGiKOG3392. Eukaryota.
ENOG4111FJ7. LUCA.
GeneTreeiENSGT00390000003156.
InParanoidiP49028.
KOiK12877.
OMAiKEDDTNW.
OrthoDBiEOG7F24VD.
PhylomeDBiP49028.

Enzyme and pathway databases

ReactomeiR-DME-109688. Cleavage of Growing Transcript in the Termination Region.
R-DME-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-DME-72163. mRNA Splicing - Major Pathway.
R-DME-72187. mRNA 3'-end processing.
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP49028.
GenomeRNAii37402.
NextBioi803461.
PROiP49028.

Gene expression databases

BgeeiP49028.
GenevisibleiP49028. DM.

Family and domain databases

Gene3Di3.30.1560.10. 1 hit.
InterProiIPR004023. Mago_nashi.
[Graphical view]
PANTHERiPTHR12638. PTHR12638. 1 hit.
PfamiPF02792. Mago_nashi. 1 hit.
[Graphical view]
SUPFAMiSSF89817. SSF89817. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mago nashi locus encodes an essential product required for germ plasm assembly in Drosophila."
    Newmark P.A., Boswell R.E.
    Development 120:1303-1313(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLY-19 AND ILE-91.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila."
    Newmark P.A., Mohr S.E., Gong L., Boswell R.E.
    Development 124:3197-3207(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The mago nashi gene is required for the polarisation of the oocyte and the formation of perpendicular axes in Drosophila."
    Micklem D.R., Dasgupta R., Elliott H., Gergely F., Davidson C., Brand A., Gonzalez-Reyes A., St Johnston D.
    Curr. Biol. 7:468-478(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay."
    Palacios I.M., Gatfield D., St Johnston D., Izaurralde E.
    Nature 427:753-757(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE EJC COMPLEX, INTERACTION WITH EIF4AIII, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  8. "Exon junction complex subunits are required to splice Drosophila MAP kinase, a large heterochromatic gene."
    Roignant J.Y., Treisman J.E.
    Cell 143:238-250(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-21.
  9. "The exon junction complex controls the splicing of MAPK and other long intron-containing transcripts in Drosophila."
    Ashton-Beaucage D., Udell C.M., Lavoie H., Baril C., Lefrancois M., Chagnon P., Gendron P., Caron-Lizotte O., Bonneil E., Thibault P., Therrien M.
    Cell 143:251-262(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The EJC binding and dissociating activity of PYM is regulated in Drosophila."
    Ghosh S., Obrdlik A., Marchand V., Ephrussi A.
    PLoS Genet. 10:E1004455-E1004455(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PYM.
  11. "Crystal structure of the Drosophila Mago nashi-Y14 complex."
    Shi H., Xu R.-M.
    Genes Dev. 17:971-976(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH TSU.
  12. "A novel mode of RBD-protein recognition in the Y14-Mago complex."
    Fribourg S., Gatfield D., Izaurralde E., Conti E.
    Nat. Struct. Biol. 10:433-439(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH TSU, FUNCTION, SUBCELLULAR LOCATION.
  13. "Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex."
    Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.
    EMBO Rep. 5:304-310(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH TSU AND PYM.

Entry informationi

Entry nameiMGN_DROME
AccessioniPrimary (citable) accession number: P49028
Secondary accession number(s): Q9W2L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

'Mago nashi' means 'without grandchildren' in Japanese.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.