MGN_MOUSE
ID MGN_MOUSE Reviewed; 146 AA.
AC P61327; A2A8E0; O35169; P50606;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein mago nashi homolog;
GN Name=Magoh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9479507; DOI=10.1006/geno.1997.5126;
RA Zhao X.F., Colaizzo-Anas T., Nowak N.J., Shows T.B., Elliott R.W.,
RA Aplan P.D.;
RT "The mammalian homologue of mago nashi encodes a serum-inducible protein.";
RL Genomics 47:319-322(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=23917022; DOI=10.4161/rna.25827;
RA Singh K.K., Wachsmuth L., Kulozik A.E., Gehring N.H.;
RT "Two mammalian MAGOH genes contribute to exon junction complex composition
RT and nonsense-mediated decay.";
RL RNA Biol. 10:1291-1298(2013).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Plays a redundant role with MAGOHB as core component of
CC the exon junction complex (EJC) and in the nonsense-mediated decay
CC (NMD) pathway. The EJC is a dynamic structure consisting of core
CC proteins and several peripheral nuclear and cytoplasmic associated
CC factors that join the complex only transiently either during EJC
CC assembly or during subsequent mRNA metabolism. The EJC marks the
CC position of the exon-exon junction in the mature mRNA for the gene
CC expression machinery and the core components remain bound to spliced
CC mRNAs throughout all stages of mRNA metabolism thereby influencing
CC downstream processes including nuclear mRNA export, subcellular mRNA
CC localization, translation efficiency and nonsense-mediated mRNA decay
CC (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of
CC EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a
CC stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC
CC key regulator PYM1 leading to EJC disassembly in the cytoplasm and
CC translation enhancement of EJC-bearing spliced mRNAs by recruiting them
CC to the ribosomal 48S preinitiation complex. Involved in the splicing
CC modulation of BCL2L1/Bcl-X (and probably other apoptotic genes);
CC specifically inhibits formation of proapoptotic isoforms; the function
CC is different from the established EJC assembly.
CC {ECO:0000250|UniProtKB:P61326}.
CC -!- SUBUNIT: Heterodimer with RBM8A. Core component of the mRNA splicing-
CC dependent exon junction complex (EJC); the core complex contains CASC3,
CC EIF4A3, MAGOH or MAGOHB, and RBM8A. Interacts with PYM1; the
CC interaction is direct and dissociates the EJC from spliced mRNAs.
CC Identified in a complex composed of the EJC core, UPF3B and UPF2. The
CC EJC core can also interact with UPF3A (in vitro). Identified in the
CC spliceosome C complex. {ECO:0000250|UniProtKB:P61326}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61326}. Nucleus
CC speckle {ECO:0000250|UniProtKB:P61326}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61326}. Note=Detected in granule-like
CC structures in the dendroplasm. Travels to the cytoplasm as part of the
CC exon junction complex (EJC) bound to mRNA. Colocalizes with the core
CC EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
CC {ECO:0000250|UniProtKB:P61326, ECO:0000250|UniProtKB:Q27W02}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, heart, liver, lung,
CC spleen and testis. {ECO:0000269|PubMed:23917022}.
CC -!- SIMILARITY: Belongs to the mago nashi family. {ECO:0000305}.
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DR EMBL; AF007862; AAB66722.1; -; mRNA.
DR EMBL; AF035939; AAC40044.1; -; mRNA.
DR EMBL; AK011512; BAB27668.1; -; mRNA.
DR EMBL; AL611936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL30768.1; -; Genomic_DNA.
DR EMBL; BC018176; AAH18176.1; -; mRNA.
DR CCDS; CCDS18441.1; -.
DR RefSeq; NP_001269666.1; NM_001282737.1.
DR AlphaFoldDB; P61327; -.
DR SMR; P61327; -.
DR BioGRID; 201297; 66.
DR ComplexPortal; CPX-635; Exon junction core complex, Magoh variant.
DR ComplexPortal; CPX-638; Exon junction subcomplex magoh-y14.
DR IntAct; P61327; 26.
DR STRING; 10090.ENSMUSP00000030348; -.
DR iPTMnet; P61327; -.
DR PhosphoSitePlus; P61327; -.
DR EPD; P61327; -.
DR MaxQB; P61327; -.
DR PaxDb; P61327; -.
DR PeptideAtlas; P61327; -.
DR PRIDE; P61327; -.
DR ProteomicsDB; 293470; -.
DR TopDownProteomics; P61327; -.
DR Antibodypedia; 4217; 309 antibodies from 33 providers.
DR DNASU; 17149; -.
DR Ensembl; ENSMUST00000030348; ENSMUSP00000030348; ENSMUSG00000028609.
DR GeneID; 17149; -.
DR KEGG; mmu:17149; -.
DR UCSC; uc008uaj.2; mouse.
DR CTD; 4116; -.
DR MGI; MGI:1330312; Magoh.
DR VEuPathDB; HostDB:ENSMUSG00000028609; -.
DR eggNOG; KOG3392; Eukaryota.
DR GeneTree; ENSGT00390000003156; -.
DR HOGENOM; CLU_109497_1_1_1; -.
DR InParanoid; P61327; -.
DR OMA; IRKEMWI; -.
DR OrthoDB; 1373136at2759; -.
DR PhylomeDB; P61327; -.
DR TreeFam; TF300128; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 17149; 24 hits in 69 CRISPR screens.
DR ChiTaRS; Magoh; mouse.
DR PRO; PR:P61327; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P61327; protein.
DR Bgee; ENSMUSG00000028609; Expressed in animal zygote and 65 other tissues.
DR Genevisible; P61327; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:1990501; C:exon-exon junction subcomplex mago-y14; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007292; P:female gamete generation; NAS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISO:MGI.
DR GO; GO:2000622; P:regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Reference proteome; RNA-binding;
KW Spliceosome; Translation regulation; Transport.
FT CHAIN 1..146
FT /note="Protein mago nashi homolog"
FT /id="PRO_0000174147"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61326"
SQ SEQUENCE 146 AA; 17164 MW; FFAD0B075E045875 CRC64;
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL
KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT TSKIGSLIDV NQSKDPEGLR
VFYYLVQDLK CLVFSLIGLH FKIKPI
