ID   MGN2_ORYSJ              Reviewed;         160 AA.
AC   P49030; Q0INV7; Q2QTQ3; Q9AXD9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Protein mago nashi homolog 2 {ECO:0000305};
DE            Short=OsMAGO2 {ECO:0000303|PubMed:24416299};
DE   AltName: Full=Mago nashi-like protein 2 {ECO:0000305};
GN   Name=MAGO2 {ECO:0000303|PubMed:24416299};
GN   OrderedLocusNames=Os12g0287200 {ECO:0000312|EMBL:BAT16753.1},
GN   LOC_Os12g18880 {ECO:0000312|EMBL:ABA97757.1};
GN   ORFNames=OsJ_35789 {ECO:0000312|EMBL:EEE53054.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Shoot;
RX   PubMed=11444698; DOI=10.1139/g01-025;
RA   Swidzinski J.A., Zaplachinski S.T., Chuong S.D., Wong J.F., Muench D.G.;
RT   "Molecular characterization and expression analysis of a highly conserved
RT   rice mago nashil homolog.";
RL   Genome 44:394-400(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH Y14A AND Y14B.
RX   PubMed=24416299; DOI=10.1371/journal.pone.0084842;
RA   Gong P., Zhao M., He C.;
RT   "Slow co-evolution of the MAGO and Y14 protein families is required for the
RT   maintenance of their obligate heterodimerization mode.";
RL   PLoS ONE 9:E84842-E84842(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH Y14B.
RX   PubMed=25230811; DOI=10.1111/tpj.12672;
RA   Gong P., Quan H., He C.;
RT   "Targeting MAGO proteins with a peptide aptamer reinforces their essential
RT   roles in multiple rice developmental pathways.";
RL   Plant J. 80:905-914(2014).
RN   [10]
RP   FUNCTION, INTERACTION WITH Y14A AND Y14B, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=24820023; DOI=10.1104/pp.114.237958;
RA   Gong P., He C.;
RT   "Uncovering divergence of rice exon junction complex core heterodimer gene
RT   duplication reveals their essential role in growth, development, and
RT   reproduction.";
RL   Plant Physiol. 165:1047-1061(2014).
CC   -!- FUNCTION: Core component of the splicing-dependent multiprotein exon
CC       junction complex (EJC) deposited at splice junctions on mRNAs. The EJC
CC       is a dynamic structure consisting of core proteins and several
CC       peripheral nuclear and cytoplasmic associated factors that join the
CC       complex only transiently either during EJC assembly or during
CC       subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC       junction in the mature mRNA for the gene expression machinery and the
CC       core components remain bound to spliced mRNAs throughout all stages of
CC       mRNA metabolism thereby influencing downstream processes including
CC       nuclear mRNA export, subcellular mRNA localization, translation
CC       efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14
CC       heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping
CC       the ATP-bound EJC core onto spliced mRNA in a stable conformation. The
CC       MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading
CC       to EJC disassembly in the cytoplasm (By similarity). EJC core
CC       heterodimers play essential roles in plant growth and development, and
CC       pollen and seed development (PubMed:25230811, PubMed:24820023). The
CC       MAGO-Y14 heterodimer selectively binds to the UDT1 (UNDEVELOPED TAPETUM
CC       1) pre-mRNA transcript and regulates the splicing of UDT1, a key
CC       regulator in stamen development (PubMed:24820023).
CC       {ECO:0000250|UniProtKB:P61326, ECO:0000269|PubMed:24820023,
CC       ECO:0000269|PubMed:25230811}.
CC   -!- SUBUNIT: Heterodimer with Y14A (PubMed:24416299, PubMed:25230811,
CC       PubMed:24820023). Heterodimer with Y14B (PubMed:24416299,
CC       PubMed:24820023). Part of the mRNA splicing-dependent exon junction
CC       complex (EJC); the core complex contains MLN51/CASC3, EIF4A3, MAGO and
CC       Y14 (Probable). {ECO:0000269|PubMed:24416299,
CC       ECO:0000269|PubMed:24820023, ECO:0000269|PubMed:25230811,
CC       ECO:0000305|PubMed:24416299}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24820023}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P61326}. Note=Nucleocytoplasmic shuttling
CC       protein. Travels to the cytoplasm as part of the exon junction complex
CC       (EJC) bound to mRNA. {ECO:0000250|UniProtKB:P61326}.
CC   -!- TISSUE SPECIFICITY: Expressed in root, leaf and developing seed tissue.
CC       {ECO:0000269|PubMed:11444698}.
CC   -!- INDUCTION: Induced by gibberellin, abscisic acid (ABA), auxin and
CC       brassinosteroid. {ECO:0000269|PubMed:24820023}.
CC   -!- SIMILARITY: Belongs to the mago nashi family. {ECO:0000305}.
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DR   EMBL; AF338343; AAK08102.1; -; mRNA.
DR   EMBL; KF051008; AHX83794.1; -; mRNA.
DR   EMBL; DP000011; ABA97757.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29608.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT16753.1; -; Genomic_DNA.
DR   EMBL; CM000149; EEE53054.1; -; Genomic_DNA.
DR   EMBL; AK063847; BAG88890.1; -; mRNA.
DR   RefSeq; XP_015618267.1; XM_015762781.1.
DR   AlphaFoldDB; P49030; -.
DR   SMR; P49030; -.
DR   STRING; 4530.OS12T0287200-01; -.
DR   PaxDb; P49030; -.
DR   PRIDE; P49030; -.
DR   EnsemblPlants; Os12t0287200-01; Os12t0287200-01; Os12g0287200.
DR   GeneID; 4351998; -.
DR   Gramene; Os12t0287200-01; Os12t0287200-01; Os12g0287200.
DR   KEGG; osa:4351998; -.
DR   eggNOG; KOG3392; Eukaryota.
DR   HOGENOM; CLU_109497_1_1_1; -.
DR   InParanoid; P49030; -.
DR   OMA; IRKEMWI; -.
DR   OrthoDB; 1373136at2759; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   Genevisible; P49030; OS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
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   Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW   Nonsense-mediated mRNA decay; Nucleus; Reference proteome; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN           1..160
FT                   /note="Protein mago nashi homolog 2"
FT                   /id="PRO_0000174154"
SQ   SEQUENCE   160 AA;  18430 MW;  45F740742D0FF0FD CRC64;
     MATGGAAGED VPGGGEFYLR YYVGHKGKFG HEFLEFEFRP DGKLRYANNS NYKNDTMIRK
     EVFVSPSVLR EARRIIQESE IMKEDDNNWP EPDRVGRQEL EIVMGNEHIS FTTSKIGSLV
     DVQTSKDPEG LRIFYYLVQD LKCFVFSLIN LHFKIKPIQS