ECT2_ARATH
ID ECT2_ARATH Reviewed; 667 AA.
AC Q9LJE5; A0A178VBC2; Q3MK93; Q8H0S7;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=YTH domain-containing protein ECT2 {ECO:0000305};
DE AltName: Full=Protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 2 {ECO:0000303|PubMed:16113215};
GN Name=ECT2 {ECO:0000303|PubMed:16113215};
GN OrderedLocusNames=At3g13460 {ECO:0000312|Araport:AT3G13460};
GN ORFNames=MRP15.12 {ECO:0000312|EMBL:BAB01753.1};
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 CIPK1.
RC STRAIN=cv. Columbia;
RX PubMed=16113215; DOI=10.1104/pp.105.065649;
RA Ok S.H., Jeong H.J., Bae J.M., Shin J.S., Luan S., Kim K.N.;
RT "Novel CIPK1-associated proteins in Arabidopsis contain an evolutionarily
RT conserved C-terminal region that mediates nuclear localization.";
RL Plant Physiol. 139:138-150(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
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 [6]
RP IDENTIFICATION BY 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, BINDING TO N6-METHYLADENOSINE
RP (M6A)-CONTAINING RNA, TISSUE SPECIFICITY, MUTAGENESIS OF TRP-464, 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).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, BINDING TO N6-METHYLADENOSINE
RP (M6A)-CONTAINING RNA, TISSUE SPECIFICITY, AND MUTAGENESIS OF TRP-521 AND
RP TRP-534.
RX PubMed=29716990; DOI=10.1105/tpc.17.00934;
RA Wei L.H., Song P., Wang Y., Lu Z., Tang Q., Yu Q., Xiao Y., Zhang X.,
RA Duan H.C., Jia G.;
RT "The m6A reader ECT2 controls trichome morphology by affecting mRNA
RT stability in Arabidopsis.";
RL Plant Cell 30:968-985(2018).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, BINDING TO N6-METHYLADENOSINE
RP (M6A)-CONTAINING RNA, AND MUTAGENESIS OF TRP-464; TRP-521 AND TRP-526.
RX PubMed=29618631; DOI=10.1105/tpc.17.00854;
RA Scutenaire J., Deragon J.M., Jean V., Benhamed M., Raynaud C., Favory J.J.,
RA Merret R., Bousquet-Antonelli C.;
RT "The YTH domain protein ECT2 is an m6A reader required for normal trichome
RT branching in Arabidopsis.";
RL Plant Cell 30:986-1005(2018).
CC -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC containing RNAs, and regulates mRNA stability (Probable)
CC (PubMed:29716990, PubMed:29618631). M6A is a modification present at
CC internal sites of mRNAs and some non-coding RNAs and plays a role in
CC mRNA stability and processing (Probable) (PubMed:29716990,
CC PubMed:29618631). Binds preferentially in the 3'UTRs of target genes
CC (PubMed:29716990). May play dual roles in regulating 3'UTR processing
CC in the nucleus and facilitating mRNA stability in the cytoplasm
CC (PubMed:29716990). Required for the correct timing of leaf formation
CC and normal leaf morphology (PubMed:29643069). Functions redundantly
CC with ECT3 (PubMed:29643069). Required for proper trichome branching and
CC morphology (PubMed:29643069, PubMed:29716990, PubMed:29618631).
CC Controls trichome morphology by binding transcripts related to trichome
CC morphogenesis and affecting their stability (PubMed:29716990,
CC PubMed:29618631). {ECO:0000269|PubMed:29618631,
CC ECO:0000269|PubMed:29643069, ECO:0000269|PubMed:29716990,
CC ECO:0000305|PubMed:29643069}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CIPK1.
CC {ECO:0000269|PubMed:16113215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29618631,
CC ECO:0000269|PubMed:29643069}. Nucleus {ECO:0000269|PubMed:29716990}.
CC Note=Localizes to cytoplasmic foci upon drought stress
CC (PubMed:29643069). Relocates to cytoplasmic stress granules upon heat
CC stress (PubMed:29618631). {ECO:0000269|PubMed:29618631,
CC ECO:0000269|PubMed:29643069}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apex, at the sites of leaf
CC formation, and in emerging leaves (PubMed:29643069). Highly expressed
CC in rapidly developing tissues (PubMed:29716990).
CC {ECO:0000269|PubMed:29643069, ECO:0000269|PubMed:29716990}.
CC -!- DISRUPTION PHENOTYPE: Aberrant trichome branching with an increase in
CC number of spikes (PubMed:29643069, PubMed:29716990). The double mutant
CC plants ect2 and ect3 exhibit delayed timing of leaf formation and
CC altered leaf morphology (PubMed:29643069).
CC {ECO:0000269|PubMed:29643069, ECO:0000269|PubMed:29716990}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY44715.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AY894118; AAY44715.1; ALT_SEQ; mRNA.
DR EMBL; AP000603; BAB01753.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75358.1; -; Genomic_DNA.
DR EMBL; AY123992; AAM74503.1; -; mRNA.
DR EMBL; BT002179; AAN72190.1; -; mRNA.
DR EMBL; AK227250; BAE99285.1; -; mRNA.
DR RefSeq; NP_187955.2; NM_112192.5.
DR AlphaFoldDB; Q9LJE5; -.
DR SMR; Q9LJE5; -.
DR IntAct; Q9LJE5; 1.
DR STRING; 3702.AT3G13460.1; -.
DR iPTMnet; Q9LJE5; -.
DR PaxDb; Q9LJE5; -.
DR PRIDE; Q9LJE5; -.
DR ProteomicsDB; 222056; -.
DR EnsemblPlants; AT3G13460.1; AT3G13460.1; AT3G13460.
DR GeneID; 820548; -.
DR Gramene; AT3G13460.1; AT3G13460.1; AT3G13460.
DR KEGG; ath:AT3G13460; -.
DR Araport; AT3G13460; -.
DR TAIR; locus:2092815; AT3G13460.
DR eggNOG; KOG1901; Eukaryota.
DR HOGENOM; CLU_017795_5_1_1; -.
DR InParanoid; Q9LJE5; -.
DR OrthoDB; 437588at2759; -.
DR PhylomeDB; Q9LJE5; -.
DR PRO; PR:Q9LJE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJE5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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 Cytoplasm; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..667
FT /note="YTH domain-containing protein ECT2"
FT /id="PRO_0000445524"
FT DOMAIN 442..579
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 264..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 448..450
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 454
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 464..465
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:29618631,
FT ECO:0000269|PubMed:29643069"
FT BINDING 497
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 521
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:29618631,
FT ECO:0000269|PubMed:29716990"
FT BINDING 526
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:29618631"
FT BINDING 534
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:29716990"
FT MUTAGEN 464
FT /note="W->A: Reduces binding to N6-methyladenosine (m6A)-
FT containing RNAs. Abolishes binding to N6-methyladenosine
FT (m6A)-containing RNAs; when associated with A-521 and A-
FT 526."
FT /evidence="ECO:0000269|PubMed:29618631,
FT ECO:0000269|PubMed:29643069"
FT MUTAGEN 521
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs; when associated with A-534. Abolishes
FT binding to N6-methyladenosine (m6A)-containing RNAs; when
FT associated with A-464 and A-526."
FT /evidence="ECO:0000269|PubMed:29618631,
FT ECO:0000269|PubMed:29716990"
FT MUTAGEN 526
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs; when associated with A-464 and A-521."
FT /evidence="ECO:0000269|PubMed:29618631"
FT MUTAGEN 534
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs; when associated with A-521."
FT /evidence="ECO:0000269|PubMed:29716990"
FT CONFLICT 199
FT /note="G -> A (in Ref. 4; AAN72190 and 5; BAE99285)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="E -> G (in Ref. 4; AAN72190 and 5; BAE99285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 72475 MW; 30AD740C806B1044 CRC64;
MATVAPPADQ ATDLLQKLSL DSPAKASEIP EPNKKTAVYQ YGGVDVHGQV PSYDRSLTPM
LPSDAADPSV CYVPNPYNPY QYYNVYGSGQ EWTDYPAYTN PEGVDMNSGI YGENGTVVYP
QGYGYAAYPY SPATSPAPQL GGEGQLYGAQ QYQYPNYFPN SGPYASSVAT PTQPDLSANK
PAGVKTLPAD SNNVASAAGI TKGSNGSAPV KPTNQATLNT SSNLYGMGAP GGGLAAGYQD
PRYAYEGYYA PVPWHDGSKY SDVQRPVSGS GVASSYSKSS TVPSSRNQNY RSNSHYTSVH
QPSSVTGYGT AQGYYNRMYQ NKLYGQYGST GRSALGYGSS GYDSRTNGRG WAATDNKYRS
WGRGNSYYYG NENNVDGLNE LNRGPRAKGT KNQKGNLDDS LEVKEQTGES NVTEVGEADN
TCVVPDREQY NKEDFPVDYA NAMFFIIKSY SEDDVHKSIK YNVWASTPNG NKKLAAAYQE
AQQKAGGCPI FLFFSVNASG QFVGLAEMTG PVDFNTNVEY WQQDKWTGSF PLKWHIVKDV
PNSLLKHITL ENNENKPVTN SRDTQEVKLE QGLKIVKIFK EHSSKTCILD DFSFYEVRQK
TILEKKAKQT QKQVSEEKVT DEKKESATAE SASKESPAAV QTSSDVKVAE NGSVAKPVTG
DVVANGC
