MGN_ARATH
ID MGN_ARATH Reviewed; 150 AA.
AC O23676; A0A023T774;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Protein mago nashi homolog {ECO:0000305};
DE Short=AtMAGO {ECO:0000303|PubMed:24416299};
GN Name=MAGO {ECO:0000303|PubMed:24416299};
GN OrderedLocusNames=At1g02140 {ECO:0000312|Araport:AT1G02140};
GN ORFNames=T7I23.7 {ECO:0000312|EMBL:AAC24371.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH Y14.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH PYM.
RX PubMed=16953428; DOI=10.1007/s00425-006-0385-y;
RA Park N.I., Muench D.G.;
RT "Biochemical and cellular characterization of the plant ortholog of PYM, a
RT protein that interacts with the exon junction complex core proteins Mago
RT and Y14.";
RL Planta 225:625-639(2007).
RN [7]
RP INTERACTION WITH Y14, AND SUBCELLULAR LOCATION.
RX PubMed=19435936; DOI=10.1105/tpc.108.060434;
RA Koroleva O.A., Calder G., Pendle A.F., Kim S.H., Lewandowska D.,
RA Simpson C.G., Jones I.M., Brown J.W.S., Shaw P.J.;
RT "Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of exon
RT junction complex: fast relocation to nucleolus and splicing speckles under
RT hypoxia.";
RL Plant Cell 21:1592-1606(2009).
RN [8]
RP INTERACTION WITH PYM, AND TISSUE SPECIFICITY.
RX PubMed=21676911; DOI=10.1093/jxb/err202;
RA Mufarrege E.F., Gonzalez D.H., Curi G.C.;
RT "Functional interconnections of Arabidopsis exon junction complex proteins
RT and genes at multiple steps of gene expression.";
RL J. Exp. Bot. 62:5025-5036(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP FUNCTION, INTERACTION WITH EIF4A3 AND Y14, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26867216; DOI=10.1371/journal.pone.0148200;
RA Cilano K., Mazanek Z., Khan M., Metcalfe S., Zhang X.N.;
RT "A new mutation, hap1-2, reveals a C terminal domain function in AtMago
RT protein and its biological effects in male gametophyte development in
RT Arabidopsis thaliana.";
RL PLoS ONE 11:E0148200-E0148200(2016).
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). Can increase in
CC vitro the expression from reporter constructs that contain leader
CC introns required for the expression of different genes. In association
CC with MAGO and PYM, participates in intron-mediated enhancement of gene
CC expression (PubMed:21676911). The MAGO-Y14 heterodimer works
CC synergistically with the NMD pathway to regulate male gametophyte
CC development (PubMed:26867216). {ECO:0000250|UniProtKB:P61326,
CC ECO:0000269|PubMed:21676911, ECO:0000269|PubMed:26867216}.
CC -!- SUBUNIT: Heterodimer with Y14 (PubMed:19435936, PubMed:26867216). Part
CC of the mRNA splicing-dependent exon junction complex (EJC); the core
CC complex contains MLN51/CASC3, EIF4A3, MAGO and Y14 (Probable).
CC Interacts with PYM (PubMed:16953428, PubMed:21676911). The interaction
CC with PYM is direct and dissociates the EJC from spliced mRNAs
CC (Probable). Interacts with EIF4A3 (PubMed:26867216).
CC {ECO:0000269|PubMed:16953428, ECO:0000269|PubMed:19435936,
CC ECO:0000269|PubMed:21676911, ECO:0000269|PubMed:26867216,
CC ECO:0000305|PubMed:16953428, ECO:0000305|PubMed:24416299}.
CC -!- INTERACTION:
CC O23676; O23160: MYB73; NbExp=3; IntAct=EBI-4443810, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19435936}.
CC Nucleus speckle {ECO:0000269|PubMed:19435936}. Nucleus
CC {ECO:0000269|PubMed:26867216}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:26867216}. 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 and shoot meristems, cotyledons,
CC vascular tissues of leaves, receptacle of flowers and siliques, and
CC pollen grains. {ECO:0000269|PubMed:21676911}.
CC -!- DISRUPTION PHENOTYPE: Male sterility due to pollen abortion after
CC meiosis. {ECO:0000269|PubMed:26867216}.
CC -!- SIMILARITY: Belongs to the mago nashi family. {ECO:0000305}.
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DR EMBL; KF051000; AHX83786.1; -; mRNA.
DR EMBL; U89959; AAC24371.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27388.1; -; Genomic_DNA.
DR EMBL; AY065157; AAL38333.1; -; mRNA.
DR EMBL; AY114602; AAM47921.1; -; mRNA.
DR EMBL; AY087464; AAM65009.1; -; mRNA.
DR PIR; C86153; C86153.
DR RefSeq; NP_171716.1; NM_100094.3.
DR AlphaFoldDB; O23676; -.
DR SMR; O23676; -.
DR BioGRID; 22800; 21.
DR IntAct; O23676; 8.
DR STRING; 3702.AT1G02140.1; -.
DR iPTMnet; O23676; -.
DR PaxDb; O23676; -.
DR PRIDE; O23676; -.
DR ProteomicsDB; 250929; -.
DR EnsemblPlants; AT1G02140.1; AT1G02140.1; AT1G02140.
DR GeneID; 837560; -.
DR Gramene; AT1G02140.1; AT1G02140.1; AT1G02140.
DR KEGG; ath:AT1G02140; -.
DR Araport; AT1G02140; -.
DR TAIR; locus:2205630; AT1G02140.
DR eggNOG; KOG3392; Eukaryota.
DR HOGENOM; CLU_109497_1_1_1; -.
DR InParanoid; O23676; -.
DR OMA; IRKEMWI; -.
DR OrthoDB; 1373136at2759; -.
DR PhylomeDB; O23676; -.
DR PRO; PR:O23676; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23676; baseline and differential.
DR Genevisible; O23676; AT.
DR GO; GO:0035145; C:exon-exon junction complex; IPI:TAIR.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; HDA:TAIR.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
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:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0010628; P:positive regulation of gene expression; IEP:TAIR.
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 Acetylation; Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Reference proteome; RNA-binding;
KW Translation regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..150
FT /note="Protein mago nashi homolog"
FT /id="PRO_0000174152"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 150 AA; 17458 MW; D59631DD4997CAF7 CRC64;
MAAEEATEFY LRYYVGHKGK FGHEFLEFEF REDGKLRYAN NSNYKNDTII RKEVFLTPAV
LKECKRIVSE SEILKEDDNN WPEPDRVGKQ ELEIVLGNEH ISFATSKIGS LVDCQSSNDP
EGLRIFYYLV QDLKCLVFSL ISLHFKIKPI
