Y14A_ORYSJ
ID Y14A_ORYSJ Reviewed; 204 AA.
AC B7FAL5; A0A023T669; Q0DKW1; Q688D4;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=RNA-binding protein Y14A {ECO:0000305};
DE Short=OsY14a {ECO:0000303|PubMed:24416299};
DE AltName: Full=RNA-binding protein 8A {ECO:0000305};
GN Name=Y14A {ECO:0000303|PubMed:24416299};
GN Synonyms=RBM8 {ECO:0000303|PubMed:24416299};
GN OrderedLocusNames=Os05g0140500 {ECO:0000312|EMBL:BAS92191.1},
GN LOC_Os05g04850 {ECO:0000305};
GN ORFNames=OSJNBb0111O13.11 {ECO:0000312|EMBL:AAU10777.1};
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] (ISOFORM 3), AND INTERACTION WITH MAGO1 AND
RP MAGO2.
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. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH MAGO1.
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 [8]
RP FUNCTION, INTERACTION WITH MAGO1 AND MAGO2, AND SUBCELLULAR LOCATION.
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:Q9Y5S9, ECO:0000269|PubMed:24820023,
CC ECO:0000269|PubMed:25230811}.
CC -!- SUBUNIT: Heterodimer with MAGO1 (PubMed:24416299, PubMed:25230811,
CC PubMed:24820023). Heterodimer with MAGO2 (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: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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B7FAL5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B7FAL5-2; Sequence=VSP_058950;
CC Name=3;
CC IsoId=B7FAL5-3; Sequence=VSP_058949;
CC -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU10777.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KF051016; AHX83802.1; -; mRNA.
DR EMBL; AC137621; AAU10777.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008211; BAF16512.2; -; Genomic_DNA.
DR EMBL; AP014961; BAS92190.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92191.1; -; Genomic_DNA.
DR EMBL; AK243594; BAH01663.1; -; mRNA.
DR RefSeq; XP_015637539.1; XM_015782053.1. [B7FAL5-1]
DR AlphaFoldDB; B7FAL5; -.
DR SMR; B7FAL5; -.
DR STRING; 4530.OS05T0140500-01; -.
DR PaxDb; B7FAL5; -.
DR PRIDE; B7FAL5; -.
DR EnsemblPlants; Os05t0140500-01; Os05t0140500-01; Os05g0140500. [B7FAL5-1]
DR EnsemblPlants; Os05t0140500-02; Os05t0140500-02; Os05g0140500. [B7FAL5-3]
DR GeneID; 4337757; -.
DR Gramene; Os05t0140500-01; Os05t0140500-01; Os05g0140500. [B7FAL5-1]
DR Gramene; Os05t0140500-02; Os05t0140500-02; Os05g0140500. [B7FAL5-3]
DR KEGG; osa:4337757; -.
DR eggNOG; KOG0130; Eukaryota.
DR HOGENOM; CLU_012062_18_1_1; -.
DR OMA; NIHHEAT; -.
DR OrthoDB; 1444995at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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; IEA:EnsemblPlants.
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 Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing;
KW mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Reference proteome;
KW RNA-binding; Translation regulation; Transport.
FT CHAIN 1..204
FT /note="RNA-binding protein Y14A"
FT /id="PRO_0000440125"
FT DOMAIN 101..179
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 COMPBIAS 11..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 13..81
FT /note="Missing (in isoform 3)"
FT /id="VSP_058949"
FT VAR_SEQ 143..204
FT /note="GYALIEYETFEEAQAAIKALDGTELLTQIISVDWAFSNGPVKRRNIRKRSPR
FT RSRSPPRRRY -> VCLFQYCNVSSPVAAL (in isoform 2)"
FT /id="VSP_058950"
SQ SEQUENCE 204 AA; 22104 MW; F4598747E6D9D181 CRC64;
MAAVTNADVE AVDFDPDDDD LMDEDAADPT PAPAPRLRST IAGGGGGGGG GDDGQRKTKG
RGFRDDAAPR DSRLAGAGRA SDFDSLGSDG GPGPVRSIEG WIVLVTGVHE EAQEDDLHNI
FRDFGQVKNL HLNLDRRTGF VKGYALIEYE TFEEAQAAIK ALDGTELLTQ IISVDWAFSN
GPVKRRNIRK RSPRRSRSPP RRRY
