ECT3_ARATH
ID ECT3_ARATH Reviewed; 495 AA.
AC F4K1Z0; Q93ZP1; Q9FNR2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=YTH domain-containing protein ECT3 {ECO:0000305};
DE AltName: Full=Protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 3 {ECO:0000303|PubMed:29643069};
GN Name=ECT3 {ECO:0000303|PubMed:29643069};
GN OrderedLocusNames=At5g61020 {ECO:0000312|Araport:AT5G61020};
GN ORFNames=MAF19.3 {ECO:0000312|EMBL:BAB10365.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, BINDING TO N6-METHYLADENOSINE
RP (M6A)-CONTAINING RNA, TISSUE SPECIFICITY, MUTAGENESIS OF TRP-283, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29643069; DOI=10.1105/tpc.17.00833;
RA Arribas-Hernandez L., Bressendorff S., Hansen M.H., Poulsen C., Erdmann S.,
RA Brodersen P.;
RT "An m6A-YTH module controls developmental timing and morphogenesis in
RT Arabidopsis.";
RL Plant Cell 30:952-967(2018).
CC -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC containing RNAs, and regulates mRNA stability (Probable). M6A is a
CC modification present at internal sites of mRNAs and some non-coding
CC RNAs and plays a role in mRNA stability and processing (Probable).
CC Required for the correct timing of leaf formation and normal leaf
CC morphology (PubMed:29643069). Required for proper trichome branching
CC and morphology (PubMed:29643069). Functions redundantly with ECT2
CC (PubMed:29643069). {ECO:0000269|PubMed:29643069,
CC ECO:0000305|PubMed:29643069}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29643069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K1Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K1Z0-2; Sequence=VSP_059897;
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apex, at the sites of leaf
CC formation, and in emerging leaves. {ECO:0000269|PubMed:29643069}.
CC -!- DISRUPTION PHENOTYPE: Aberrant trichome branching with an increase in
CC number of spikes (PubMed:29643069). The double mutant plants ect2 and
CC ect3 exhibit delayed timing of leaf formation and altered leaf
CC morphology (PubMed:29643069). {ECO:0000269|PubMed:29643069}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006696; BAB10365.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97412.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97413.1; -; Genomic_DNA.
DR EMBL; AY056421; AAL08277.1; -; mRNA.
DR EMBL; AY065413; AAL38854.1; -; mRNA.
DR EMBL; AY096551; AAM20201.1; -; mRNA.
DR EMBL; AK226952; BAE99022.1; -; mRNA.
DR RefSeq; NP_568932.2; NM_125495.2. [F4K1Z0-2]
DR RefSeq; NP_851236.1; NM_180905.3. [F4K1Z0-1]
DR AlphaFoldDB; F4K1Z0; -.
DR SMR; F4K1Z0; -.
DR STRING; 3702.AT5G61020.1; -.
DR iPTMnet; F4K1Z0; -.
DR PaxDb; F4K1Z0; -.
DR PRIDE; F4K1Z0; -.
DR ProteomicsDB; 222057; -. [F4K1Z0-1]
DR EnsemblPlants; AT5G61020.1; AT5G61020.1; AT5G61020. [F4K1Z0-1]
DR EnsemblPlants; AT5G61020.2; AT5G61020.2; AT5G61020. [F4K1Z0-2]
DR GeneID; 836223; -.
DR Gramene; AT5G61020.1; AT5G61020.1; AT5G61020. [F4K1Z0-1]
DR Gramene; AT5G61020.2; AT5G61020.2; AT5G61020. [F4K1Z0-2]
DR KEGG; ath:AT5G61020; -.
DR Araport; AT5G61020; -.
DR TAIR; locus:2159391; AT5G61020.
DR eggNOG; KOG1901; Eukaryota.
DR HOGENOM; CLU_017795_1_0_1; -.
DR InParanoid; F4K1Z0; -.
DR OMA; EHASKAC; -.
DR OrthoDB; 714585at2759; -.
DR PRO; PR:F4K1Z0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K1Z0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0061157; P:mRNA destabilization; IBA:GO_Central.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 1.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..495
FT /note="YTH domain-containing protein ECT3"
FT /id="PRO_0000445525"
FT DOMAIN 261..398
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT BINDING 267..269
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 273
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 283..284
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000269|PubMed:29643069"
FT BINDING 316
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 340
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 345
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 353
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9LJE5"
FT VAR_SEQ 31..32
FT /note="Missing (in isoform 2)"
FT /id="VSP_059897"
FT MUTAGEN 283
FT /note="W->A: Reduces binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:29643069"
FT CONFLICT 51
FT /note="A -> G (in Ref. 3; AAL08277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55226 MW; 0908CD5574F2FC2E CRC64;
MANPDHVSDV LHNLSIDPTT KALAPDSETK LQGAYGGNGN DFLLNDELVE ATKIGKPSLL
SKDGGVTKDK GSNLKKLGYQ SAAYNAKGSY GKGAYAYGYY PPAYQYPRHG YTGSYASGKT
NLQYQYLTQQ GRSAGNGQSY GGYMDNIYSN YGMCGPYTNG YGYGSYGYDS WKYMPNWYAV
NNTYKPRNGY HGYGKENIEG LNEMNRGPRA KGFNSQDGSK VMAVSLKEQR VTETEKLSED
VSLLDPKDYN KIDFPETYTE AKFYVIKSYS EDDIHKSIKY SVWSSTPNGN KKLDASYNEA
KQKSDGCPVF LLFSVNTSGQ FVGLAEMVGP VDFNKTVEYW QQDKWIGCFP VKWHFVKDIP
NSSLRHITLE NNENKPVTNS RDTQEVKLEQ GIKVIKIFKD HASKTCILDD FEFYENRQKI
IQERKSKHLQ IKKQTLVANA DKGVMSKINL VKPQESTTAS EDAAALGVAA EVTKESKVVK
ETELPVEKNA VATAC
