EML1_ARATH
ID EML1_ARATH Reviewed; 327 AA.
AC Q9C7C4; Q9LH54;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein EMSY-LIKE 1 {ECO:0000303|PubMed:21830950};
DE Short=AtEML1 {ECO:0000303|PubMed:21830950};
GN Name=EML1 {ECO:0000303|PubMed:21830950};
GN OrderedLocusNames=At3g12140 {ECO:0000312|Araport:AT3G12140};
GN ORFNames=T21B14.4 {ECO:0000312|EMBL:AAG51060.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [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 1).
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;
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 FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP INTERACTION WITH EDM2, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21830950; DOI=10.1094/mpmi-05-11-0123;
RA Tsuchiya T., Eulgem T.;
RT "EMSY-like genes are required for full RPP7-mediated race-specific immunity
RT and basal defense in Arabidopsis.";
RL Mol. Plant Microbe Interact. 24:1573-1581(2011).
CC -!- FUNCTION: Probably involved in the regulation of chromatin states
CC (Probable). Contributes to RPP7-mediated and basal immunity, especially
CC against Hyaloperonospora arabidopsidis isolate Hiks1. Regulates
CC negatively EDM2-dependent floral transition (PubMed:21830950).
CC {ECO:0000269|PubMed:21830950, ECO:0000305|PubMed:21830950}.
CC -!- SUBUNIT: Isoform 1 interacts with EDM2 in nucleus.
CC {ECO:0000269|PubMed:21830950}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21830950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=v1 {ECO:0000303|PubMed:21830950}, v2
CC {ECO:0000303|PubMed:21830950};
CC IsoId=Q9C7C4-1; Sequence=Displayed;
CC Name=2; Synonyms=v3 {ECO:0000303|PubMed:21830950};
CC IsoId=Q9C7C4-2; Sequence=VSP_057383;
CC -!- DISRUPTION PHENOTYPE: Reduced resistance to Hyaloperonospora
CC arabidopsidis isolate Hiks1. Slight early flowering phenotype.
CC {ECO:0000269|PubMed:21830950}.
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DR EMBL; AP002063; BAB01962.1; -; Genomic_DNA.
DR EMBL; AC069473; AAG51060.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75155.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75156.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75157.1; -; Genomic_DNA.
DR EMBL; BT002758; AAO22586.1; -; mRNA.
DR EMBL; AK226347; BAE98495.1; -; mRNA.
DR RefSeq; NP_001030677.1; NM_001035600.3. [Q9C7C4-2]
DR RefSeq; NP_187821.1; NM_112049.3. [Q9C7C4-1]
DR RefSeq; NP_850568.1; NM_180237.3. [Q9C7C4-1]
DR AlphaFoldDB; Q9C7C4; -.
DR SMR; Q9C7C4; -.
DR IntAct; Q9C7C4; 1.
DR STRING; 3702.AT3G12140.3; -.
DR iPTMnet; Q9C7C4; -.
DR PaxDb; Q9C7C4; -.
DR PRIDE; Q9C7C4; -.
DR ProteomicsDB; 220357; -. [Q9C7C4-1]
DR EnsemblPlants; AT3G12140.1; AT3G12140.1; AT3G12140. [Q9C7C4-1]
DR EnsemblPlants; AT3G12140.2; AT3G12140.2; AT3G12140. [Q9C7C4-1]
DR EnsemblPlants; AT3G12140.3; AT3G12140.3; AT3G12140. [Q9C7C4-2]
DR GeneID; 820389; -.
DR Gramene; AT3G12140.1; AT3G12140.1; AT3G12140. [Q9C7C4-1]
DR Gramene; AT3G12140.2; AT3G12140.2; AT3G12140. [Q9C7C4-1]
DR Gramene; AT3G12140.3; AT3G12140.3; AT3G12140. [Q9C7C4-2]
DR KEGG; ath:AT3G12140; -.
DR Araport; AT3G12140; -.
DR TAIR; locus:2099287; AT3G12140.
DR eggNOG; KOG4675; Eukaryota.
DR HOGENOM; CLU_038636_0_0_1; -.
DR OMA; VHETWEW; -.
DR PhylomeDB; Q9C7C4; -.
DR PRO; PR:Q9C7C4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C7C4; baseline and differential.
DR Genevisible; Q9C7C4; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
DR Gene3D; 1.10.1240.40; -; 1.
DR InterPro; IPR014002; Agenet_dom_plant.
DR InterPro; IPR033485; EMSY-LIKE_plant.
DR InterPro; IPR005491; ENT_dom.
DR InterPro; IPR036142; ENT_dom-like_sf.
DR PANTHER; PTHR33432; PTHR33432; 1.
DR Pfam; PF03735; ENT; 1.
DR SMART; SM00743; Agenet; 1.
DR SMART; SM01191; ENT; 1.
DR SUPFAM; SSF158639; SSF158639; 1.
DR PROSITE; PS51138; ENT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome.
FT CHAIN 1..327
FT /note="Protein EMSY-LIKE 1"
FT /id="PRO_0000431791"
FT DOMAIN 1..88
FT /note="ENT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00476"
FT REGION 206..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..58
FT /evidence="ECO:0000255"
FT COILED 281..306
FT /evidence="ECO:0000255"
FT COMPBIAS 238..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4K2F0"
FT VAR_SEQ 313..327
FT /note="DGDPPYSHDHPMPQG -> GNNNKSTLRLVCNLRIIYYLPLNFCVMMIISSI
FT ITNLILGKIIRELIHTCSACDFSVTCKQLNSLKYRSSS (in isoform 2)"
FT /id="VSP_057383"
SQ SEQUENCE 327 AA; 36912 MW; 1ADB5C2391939CC7 CRC64;
METQIHQLEQ EAYTAVLRAF KAQSDAISWE KESLITELRK ELRVSDDEHR ELLSRVNKDD
TIQRIRDWRQ GGASQITRHA TIQPFDVLPS PTFSAARKKQ KTFPSYNPSI GATGNRSFNN
RLVSSGISGN ESAEALIGRK VWTKWPEDNH FYEAIITQYN ADEGRHALVY DIHAANETWE
WVDLKEIPPE DIRWDGEESG VALNIGHGSA SFRGNRRGQI HGGRGRGPRI HQPRRELVPP
PTQQNGSGGR RTSSDDIELF NTDSLVKEVE RVFDSTHPDP LELDKAKKML KEHEQALIAA
IARLADTSDG EMDGDPPYSH DHPMPQG
