EML3_ARATH
ID EML3_ARATH Reviewed; 397 AA.
AC F4K2F0; Q9LXT7;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Protein EMSY-LIKE 3 {ECO:0000303|PubMed:21830950};
DE Short=AtEML3 {ECO:0000303|PubMed:21830950};
GN Name=EML3 {ECO:0000303|PubMed:21830950};
GN OrderedLocusNames=At5g13020 {ECO:0000312|Araport:AT5G13020};
GN ORFNames=T24H18.190 {ECO:0000312|EMBL:CAB88266.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [4]
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 [5]
RP FUNCTION, 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 basal immunity (PubMed:21830950).
CC {ECO:0000269|PubMed:21830950, ECO:0000305|PubMed:21830950}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C7C4,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88266.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353013; CAB88266.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91842.1; -; Genomic_DNA.
DR PIR; T49916; T49916.
DR RefSeq; NP_196806.2; NM_121305.4.
DR AlphaFoldDB; F4K2F0; -.
DR SMR; F4K2F0; -.
DR STRING; 3702.AT5G13020.1; -.
DR iPTMnet; F4K2F0; -.
DR PaxDb; F4K2F0; -.
DR PRIDE; F4K2F0; -.
DR ProteomicsDB; 222660; -.
DR EnsemblPlants; AT5G13020.1; AT5G13020.1; AT5G13020.
DR GeneID; 831142; -.
DR Gramene; AT5G13020.1; AT5G13020.1; AT5G13020.
DR KEGG; ath:AT5G13020; -.
DR Araport; AT5G13020; -.
DR TAIR; locus:2182345; AT5G13020.
DR eggNOG; KOG4675; Eukaryota.
DR HOGENOM; CLU_038636_0_1_1; -.
DR InParanoid; F4K2F0; -.
DR OMA; FPRIHND; -.
DR OrthoDB; 620151at2759; -.
DR PRO; PR:F4K2F0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K2F0; baseline and differential.
DR Genevisible; F4K2F0; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0031491; F:nucleosome binding; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:TAIR.
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 Coiled coil; Nucleus; Phosphoprotein; Plant defense; Reference proteome.
FT CHAIN 1..397
FT /note="Protein EMSY-LIKE 3"
FT /id="PRO_0000431793"
FT DOMAIN 50..137
FT /note="ENT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00476"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 81..107
FT /evidence="ECO:0000255"
FT COILED 363..389
FT /evidence="ECO:0000255"
FT MOTIF 175..182
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 23..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 397 AA; 43653 MW; A9A496E91603BE62 CRC64;
MDYRPSDSSG TDDDLPPSHQ GRYQRNARPT GNGRPSVLNS APLSRVHNEM ETQIHLIEQE
AYSSILRAFK AQSDAITWEK ESLITELRKE LRVSDEEHRE LLSRVNADEM IRRIREWRKA
NSLQSSVPQL VHDAPSPAVS GSRKKQKTSQ SIASLAMGPP SPSLHPSMQP SSSALRRGGP
PPGPKTKKPK TSMQYPSTGI AGRPQAGALT NEPGESGSYD PLVGRKVWTK WPDDNQYYEA
VITDYNPVEG RHALVYDINS ANETWEWVNL KEISPGDIRW EGEDPGISRK GGHPGQGRGT
KTMARGGPAS NAGGRGRGSM RMQQPKTQNG IGKKALGEIE ILHTETLLKE VEKVFGSVNP
NPAEVEKAKR VLRDHELALM DAIAKLEEIS DGESGNI
