Y14_ARATH
ID Y14_ARATH Reviewed; 202 AA.
AC F4I9J7; Q8LG23; Q94AZ6; Q9C8K3;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=RNA-binding protein Y14 {ECO:0000305};
DE Short=AtY14 {ECO:0000303|PubMed:24416299};
DE AltName: Full=RNA-binding protein 8A {ECO:0000305};
GN Name=Y14 {ECO:0000303|PubMed:24416299};
GN Synonyms=RBM8 {ECO:0000303|PubMed:24416299};
GN OrderedLocusNames=At1g51510 {ECO:0000312|Araport:AT1G51510};
GN ORFNames=F5D21.5 {ECO:0000312|EMBL:AAG52616.1};
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 MAGO.
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 MAGO AND EIF4A3, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, 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 [10]
RP FUNCTION, AND INTERACTION WITH MAGO.
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:Q9Y5S9,
CC ECO:0000269|PubMed:21676911, ECO:0000269|PubMed:26867216}.
CC -!- SUBUNIT: Heterodimer with MAGO (PubMed:24416299, PubMed:19435936,
CC PubMed:26867216). Part of the mRNA splicing-dependent exon junction
CC complex (EJC); the core complex contains MLN51/CASC3, EIF4A3, MAGO and
CC Y14 (Probable). Interacts with PYM (PubMed:16953428, PubMed:21676911).
CC The interaction with PYM is direct and dissociates the EJC from spliced
CC mRNAs (Probable). Weekly interacts with EIF4A3 (PubMed:19435936).
CC {ECO:0000269|PubMed:16953428, ECO:0000269|PubMed:19435936,
CC ECO:0000269|PubMed:21676911, ECO:0000269|PubMed:24416299,
CC ECO:0000269|PubMed:26867216, ECO:0000305|PubMed:16953428,
CC ECO:0000305|PubMed:24416299}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19435936}.
CC Nucleus speckle {ECO:0000269|PubMed:19435936}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y5S9}. Note=Nucleocytoplasmic shuttling
CC protein. Travels to the cytoplasm as part of the exon junction complex
CC (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q9Y5S9}.
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 -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52616.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK73941.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM16181.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; KF051012; AHX83798.1; -; mRNA.
DR EMBL; AC024261; AAG52616.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32675.1; -; Genomic_DNA.
DR EMBL; AY045583; AAK73941.1; ALT_FRAME; mRNA.
DR EMBL; AY094025; AAM16181.1; ALT_FRAME; mRNA.
DR EMBL; AY084501; AAM61070.1; -; mRNA.
DR PIR; E96553; E96553.
DR RefSeq; NP_564591.1; NM_104029.4.
DR AlphaFoldDB; F4I9J7; -.
DR SMR; F4I9J7; -.
DR IntAct; F4I9J7; 1.
DR STRING; 3702.AT1G51510.1; -.
DR iPTMnet; F4I9J7; -.
DR PaxDb; F4I9J7; -.
DR PRIDE; F4I9J7; -.
DR ProteomicsDB; 242523; -.
DR EnsemblPlants; AT1G51510.1; AT1G51510.1; AT1G51510.
DR GeneID; 841576; -.
DR Gramene; AT1G51510.1; AT1G51510.1; AT1G51510.
DR KEGG; ath:AT1G51510; -.
DR Araport; AT1G51510; -.
DR TAIR; locus:2033888; AT1G51510.
DR eggNOG; KOG0130; Eukaryota.
DR HOGENOM; CLU_012062_18_1_1; -.
DR InParanoid; F4I9J7; -.
DR OMA; DMELEHT; -.
DR OrthoDB; 1444995at2759; -.
DR PRO; PR:F4I9J7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I9J7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0035145; C:exon-exon junction complex; IPI:TAIR.
DR GO; GO:0016604; C:nuclear body; HDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA: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: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; 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 Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Translation regulation; Transport.
FT CHAIN 1..202
FT /note="RNA-binding protein Y14"
FT /id="PRO_0000440124"
FT DOMAIN 95..173
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 62
FT /note="E -> D (in Ref. 5; AAM61070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22438 MW; 0DD406A25A360978 CRC64;
MANIESEAVD FEPEEDDLMD EEGTAIDGAD VSPRAGHPRL KSAIAGANGE SAKKTKGRGF
REEKDSDRQR RLSSRDFESL GSDGRPGPQR SVEGWIILVS GVHEETQEED ITNAFGDFGE
IKNLNLNLDR RSGYVKGYAL IEYEKKEEAQ SAISAMNGAE LLTQNVSVDW AFSSGPSGGE
SYRRKNSRYG RSQRSRSPRR RY
