RBM8A_DROME
ID RBM8A_DROME Reviewed; 165 AA.
AC Q9V535; Q8SZA6; Q95X08;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=RNA-binding protein 8A;
DE AltName: Full=Protein tsunagi;
GN Name=tsu {ECO:0000312|FlyBase:FBgn0033378};
GN Synonyms=Y14 {ECO:0000303|PubMed:12730685};
GN ORFNames=CG8781 {ECO:0000312|FlyBase:FBgn0033378};
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] {ECO:0000305, ECO:0000312|EMBL:AAL29185.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAGO, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11691839; DOI=10.1101/gad.927001;
RA Mohr S.E., Dillon S.T., Boswell R.E.;
RT "The RNA-binding protein Tsunagi interacts with Mago Nashi to establish
RT polarity and localize oskar mRNA during Drosophila oogenesis.";
RL Genes Dev. 15:2886-2899(2001).
RN [2] {ECO:0000312|EMBL:AAF58987.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF58987.1}
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] {ECO:0000312|EMBL:AAL48627.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48627.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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, IDENTIFICATION IN THE EJC COMPLEX, AND INTERACTION WITH EIF4AIII.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGO, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 47-156 IN COMPLEX WITH MAGO.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MAGO 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 (PubMed:11691839).
CC {ECO:0000269|PubMed:11691839, ECO:0000269|PubMed:12730685,
CC ECO:0000269|PubMed:20946982, ECO:0000269|PubMed:20946983,
CC ECO:0000269|PubMed:24967911}.
CC -!- SUBUNIT: Heterodimer (via RRM domain) with mago (PubMed:11691839,
CC PubMed:12730685, PubMed:12704080). Part of the mRNA splicing-dependent
CC exon junction complex (EJC) complex; the core complex contains
CC btz/CASC3, eIF4AIII, mago and tsu/RBM8A (PubMed:14973490). Interacts
CC with Pym (via N-terminus); the interaction is direct (PubMed:24967911,
CC PubMed:14968132). Interacts with eIF4AIII (PubMed:14973490).
CC {ECO:0000269|PubMed:11691839, ECO:0000269|PubMed:12704080,
CC ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:14968132,
CC ECO:0000269|PubMed:14973490, ECO:0000269|PubMed:24967911}.
CC -!- INTERACTION:
CC Q9V535; P49028: mago; NbExp=6; IntAct=EBI-172458, EBI-159609;
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 throughout development. Localizes to the
CC posterior pole of the oocyte during stages 1-9 of oogenesis.
CC {ECO:0000269|PubMed:11691839}.
CC -!- DOMAIN: The RNA recognition motif (RRM) is involved in the interaction
CC with mago. The RNA-binding activity of such domains is therefore
CC uncertain. {ECO:0000269|PubMed:12730685}.
CC -!- DISRUPTION PHENOTYPE: Developing photoreceptor cell clusters express
CC reduced levels of rolled/MAPK and fail to differentiate normally.
CC {ECO:0000269|PubMed:20946982, ECO:0000269|PubMed:20946983}.
CC -!- MISCELLANEOUS: 'Tsunagi' means 'connection' or 'link' in Japanese.
CC {ECO:0000303|PubMed:11691839}.
CC -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
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DR EMBL; AF173550; AAL29185.1; -; mRNA.
DR EMBL; AE013599; AAF58987.1; -; Genomic_DNA.
DR EMBL; AY071005; AAL48627.1; -; mRNA.
DR RefSeq; NP_610454.2; NM_136610.4.
DR PDB; 1HL6; X-ray; 2.50 A; A/C=1-165.
DR PDB; 1OO0; X-ray; 1.85 A; B=47-156.
DR PDB; 1RK8; X-ray; 1.90 A; A=1-165.
DR PDB; 2X1G; X-ray; 3.35 A; A/C=1-165.
DR PDBsum; 1HL6; -.
DR PDBsum; 1OO0; -.
DR PDBsum; 1RK8; -.
DR PDBsum; 2X1G; -.
DR AlphaFoldDB; Q9V535; -.
DR SMR; Q9V535; -.
DR BioGRID; 61762; 13.
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-24075N; -.
DR IntAct; Q9V535; 2.
DR STRING; 7227.FBpp0087648; -.
DR PaxDb; Q9V535; -.
DR PRIDE; Q9V535; -.
DR ABCD; Q9V535; 4 sequenced antibodies.
DR EnsemblMetazoa; FBtr0088567; FBpp0087648; FBgn0033378.
DR GeneID; 35924; -.
DR KEGG; dme:Dmel_CG8781; -.
DR UCSC; CG8781-RA; d. melanogaster.
DR CTD; 110124; -.
DR FlyBase; FBgn0033378; tsu.
DR VEuPathDB; VectorBase:FBgn0033378; -.
DR eggNOG; KOG0130; Eukaryota.
DR GeneTree; ENSGT00730000111185; -.
DR HOGENOM; CLU_012062_18_3_1; -.
DR InParanoid; Q9V535; -.
DR OMA; TIAVDWC; -.
DR OrthoDB; 1444995at2759; -.
DR PhylomeDB; Q9V535; -.
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; Q9V535; -.
DR BioGRID-ORCS; 35924; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; Q9V535; -.
DR GenomeRNAi; 35924; -.
DR PRO; PR:Q9V535; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033378; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q9V535; baseline and differential.
DR Genevisible; Q9V535; 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:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0046595; P:establishment of pole plasm mRNA localization; TAS:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0051170; P:import into nucleus; IDA:ComplexPortal.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP: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:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0051663; P:oocyte nucleus localization involved in oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS: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; cd12324; RRM_RBM8; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR008111; RNA-bd_8.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR033744; RRM_RBM8.
DR PANTHER; PTHR45894; PTHR45894; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR01738; RNABINDINGM8.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 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..165
FT /note="RNA-binding protein 8A"
FT /id="PRO_0000081765"
FT DOMAIN 73..151
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 86
FT /note="E -> G (in Ref. 1; AAL29185)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="N -> S (in Ref. 4; AAL48627)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="N -> R (in Ref. 1; AAL29185)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="K -> R (in Ref. 4; AAL48627)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="K -> M (in Ref. 1; AAL29185)"
FT /evidence="ECO:0000305"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1HL6"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1HL6"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1HL6"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1OO0"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1OO0"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1OO0"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:1OO0"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1OO0"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:1OO0"
SQ SEQUENCE 165 AA; 19010 MW; A47BE9ED37CCA045 CRC64;
MADVLDIDNA EEFEVDEDGD QGIVRLKEKA KHRKGRGFGS DSNTREAIHS YERVRNEDDD
ELEPGPQRSV EGWILFVTSI HEEAQEDEIQ EKFCDYGEIK NIHLNLDRRT GFSKGYALVE
YETHKQALAA KEALNGAEIM GQTIQVDWCF VKGPKRVKKS EKRRR
