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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
 
 
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