ECT4_ARATH
ID ECT4_ARATH Reviewed; 605 AA.
AC A0A1P8AS03; Q94A30; Q9ZVU7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=YTH domain-containing protein ECT4 {ECO:0000305};
DE AltName: Full=Protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 4 {ECO:0000303|PubMed:29643069};
GN Name=ECT4 {ECO:0000303|PubMed:29643069};
GN OrderedLocusNames=At1g55500 {ECO:0000312|EMBL:ANM59432.1};
GN ORFNames=T5A14.10 {ECO:0000312|EMBL:AAD10646.1};
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=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 [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] (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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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). {ECO:0000269|PubMed:29643069,
CC ECO:0000305|PubMed:29643069}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29643069}.
CC Note=Localizes to cytoplasmic foci upon drought stress.
CC {ECO:0000269|PubMed:29643069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1P8AS03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1P8AS03-2; Sequence=VSP_059898, VSP_059899;
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: No visible phenotype under normal growth
CC conditions, but the delayed leaf emergence and leaf morphology defect
CC of the double mutant ect2 and ect3 is enhanced in the triple mutant
CC ect2, ect3 and ect4. {ECO:0000269|PubMed:29643069}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10646.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005223; AAD10646.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33253.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59432.1; -; Genomic_DNA.
DR EMBL; AY050425; AAK91441.1; -; mRNA.
DR EMBL; BT002240; AAN72251.1; -; mRNA.
DR PIR; C96597; C96597.
DR RefSeq; NP_001321789.1; NM_001333714.1. [A0A1P8AS03-1]
DR RefSeq; NP_564692.1; NM_104425.1. [A0A1P8AS03-2]
DR AlphaFoldDB; A0A1P8AS03; -.
DR SMR; A0A1P8AS03; -.
DR STRING; 3702.AT1G55500.2; -.
DR ProteomicsDB; 247059; -. [A0A1P8AS03-1]
DR EnsemblPlants; AT1G55500.1; AT1G55500.1; AT1G55500. [A0A1P8AS03-2]
DR EnsemblPlants; AT1G55500.5; AT1G55500.5; AT1G55500. [A0A1P8AS03-1]
DR GeneID; 841997; -.
DR Gramene; AT1G55500.1; AT1G55500.1; AT1G55500. [A0A1P8AS03-2]
DR Gramene; AT1G55500.5; AT1G55500.5; AT1G55500. [A0A1P8AS03-1]
DR KEGG; ath:AT1G55500; -.
DR Araport; AT1G55500; -.
DR HOGENOM; CLU_017795_5_1_1; -.
DR OrthoDB; 1523251at2759; -.
DR PRO; PR:A0A1P8AS03; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A1P8AS03; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..605
FT /note="YTH domain-containing protein ECT4"
FT /id="PRO_0000445526"
FT DOMAIN 414..551
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 249..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420..422
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 426
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 436..437
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 469
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 493
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 498
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 506
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 1..43
FT /note="Missing (in isoform 2)"
FT /id="VSP_059898"
FT VAR_SEQ 103..115
FT /note="Missing (in isoform 2)"
FT /id="VSP_059899"
SQ SEQUENCE 605 AA; 66591 MW; 472DCB20F5075E47 CRC64;
MSTVAPPADQ AADVLKKLSL DSKSRTLEIP EPTKKTGVYQ YGAMDSNGQV PSFDRSLSPM
LPSDALDPSV FYVPNVYQQP YYYGYGSDYT GYTNSESVDM TSGAYGENAS LVYPQGYGYA
AFPYSPATSP APQLGGDGQL YGAQQYQYPF PLTASSGPFA SSVPASTQSK LSTNKAANSA
SAGIPKGMNG SAPVKPLNQS ALYGNSALGG GLAAGYQDPR YSYDGFYTPV SWHDGSNFSD
VQRSVSGSGV ASSYSKANNN VPATRNQNSS SNSHYTSMYQ PASMTGYAAQ GYYDRVSPNK
SYGQYGSTVR SGMGYGSSGY GSRTNERGWL NTDNKYRSRG RGNSYFYGNE NIDGLNELNR
GPRAKGTKAT EEVSSEEVKK QTFDESNTEE TVTCVLPDRE ECNRDDFPVE YKDAKFFIIK
SYSEDDVHKS IKYNVWASTP NGNKKLDAAY QEAQQKSSGC PVFLFFSVNA SGQFIGLAEM
KGPVDFNKNI EYWQQDKWTG SFPLKWHILK DVPNSLLKHI TLEYNENKPV TNSRDTQEVK
LEQGLKVVKI FKEHNSKTCI LDDFSFYEAR QKTILEKKAK QQQSQKQVWE GKTNDEKPGT
VDSTM
