ECT1_ARATH
ID ECT1_ARATH Reviewed; 428 AA.
AC Q3MK94; Q8W573; Q9SQR7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=YTH domain-containing protein ECT1 {ECO:0000305};
DE AltName: Full=Protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 1 {ECO:0000303|PubMed:16113215};
GN Name=ECT1 {ECO:0000303|PubMed:16113215};
GN OrderedLocusNames=At3g03950 {ECO:0000312|Araport:AT3G03950};
GN ORFNames=T11I18.6 {ECO:0000312|EMBL:AAF05854.1};
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] (ISOFORM 1), INTERACTION WITH CIPK1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
CC -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC containing RNAs, and regulates mRNA stability (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9LJE5}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CIPK1.
CC {ECO:0000269|PubMed:16113215}.
CC -!- INTERACTION:
CC Q3MK94; Q8RWC9: CIPK1; NbExp=4; IntAct=EBI-2368594, EBI-1748677;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16113215}. Cytoplasm
CC {ECO:0000269|PubMed:16113215}. Note=Localizes predominantly in the
CC nucleus. {ECO:0000269|PubMed:16113215}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3MK94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3MK94-2; Sequence=VSP_059896;
CC -!- TISSUE SPECIFICITY: Expressed in root apex, shoot apex, lateral root
CC primordia, stamens, carpels and trichomes.
CC {ECO:0000269|PubMed:16113215}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF05854.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY894117; AAY44714.1; -; mRNA.
DR EMBL; AC011698; AAF05854.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74016.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74017.1; -; Genomic_DNA.
DR EMBL; AF419591; AAL31923.1; -; mRNA.
DR EMBL; AY097342; AAM19858.1; -; mRNA.
DR EMBL; AK317103; BAH19792.1; -; mRNA.
DR RefSeq; NP_001030629.1; NM_001035552.2. [Q3MK94-1]
DR RefSeq; NP_850510.1; NM_180179.3. [Q3MK94-2]
DR AlphaFoldDB; Q3MK94; -.
DR SMR; Q3MK94; -.
DR IntAct; Q3MK94; 4.
DR STRING; 3702.AT3G03950.3; -.
DR iPTMnet; Q3MK94; -.
DR PaxDb; Q3MK94; -.
DR PRIDE; Q3MK94; -.
DR ProteomicsDB; 222055; -. [Q3MK94-1]
DR EnsemblPlants; AT3G03950.2; AT3G03950.2; AT3G03950. [Q3MK94-2]
DR EnsemblPlants; AT3G03950.3; AT3G03950.3; AT3G03950. [Q3MK94-1]
DR GeneID; 819550; -.
DR Gramene; AT3G03950.2; AT3G03950.2; AT3G03950. [Q3MK94-2]
DR Gramene; AT3G03950.3; AT3G03950.3; AT3G03950. [Q3MK94-1]
DR KEGG; ath:AT3G03950; -.
DR Araport; AT3G03950; -.
DR TAIR; locus:2095938; AT3G03950.
DR eggNOG; KOG1901; Eukaryota.
DR InParanoid; Q3MK94; -.
DR OMA; NFPETLV; -.
DR OrthoDB; 587912at2759; -.
DR PhylomeDB; Q3MK94; -.
DR PRO; PR:Q3MK94; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q3MK94; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS: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; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..428
FT /note="YTH domain-containing protein ECT1"
FT /id="PRO_0000445523"
FT DOMAIN 245..382
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT BINDING 251..253
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 257
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 267..268
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 300
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 324
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 329
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 337
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 42..45
FT /note="Missing (in isoform 2)"
FT /id="VSP_059896"
SQ SEQUENCE 428 AA; 48232 MW; E9BC918D9F94FDEC CRC64;
MAGAASSDRL VTSFPLLDTA DLFQDLSLGS DANEVPMNFT KGSFQHPYGH APYGASSHGS
ERRPNMNAGN LLNGGDSIGS YPWGYIPANY PSGGYPDPRF GYDRNSNHSS FSHLMNPHSS
QEVPSFDQLG YNDHLYSNHG LYGLYGNVID SGHAYGTFGY DSWKLGRGWY PVDGYRKTRS
FNHGRGYSDE KADRLNELCR GPRSSDFKNP QVLNSSMLDA MKQDVSAVDL QRYNGENFPE
SFVKAKFFVI KSYSEDDVHN CIKYGAWSST PTGNKKLNAA YYEAKENSQE CPVYLLFSVN
ASGQFVGLAE MVGPVDFNKT MEYWQQDKWI GCFPVKWHII KDIPNSLLRH ITLANNENKP
VTNSRDTQEV NLEHGTKIIK IFKEYMSKTC ILDDYKFYET RQKIIRDKKI KQKKQALDGA
SGETINLS