EIN2_ARATH
ID EIN2_ARATH Reviewed; 1294 AA.
AC Q9S814;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ethylene-insensitive protein 2 {ECO:0000303|PubMed:10381874};
DE Short=AtEIN2 {ECO:0000303|PubMed:10381874};
DE Short=EIN-2 {ECO:0000303|PubMed:10381874};
DE AltName: Full=Cytokinin-resistant protein AtCKR1;
DE AltName: Full=Protein ORESARA 3 {ECO:0000303|PubMed:9351240};
DE Contains:
DE RecName: Full=EIN2-CEND {ECO:0000303|PubMed:23132950};
DE AltName: Full=EIN2C {ECO:0000303|PubMed:26496608};
GN Name=EIN2 {ECO:0000303|PubMed:10381874};
GN Synonyms=CKR1, ORE3 {ECO:0000303|PubMed:9351240};
GN OrderedLocusNames=At5g03280 {ECO:0000312|Araport:AT5G03280};
GN ORFNames=F12E4.10 {ECO:0000312|EMBL:CAB83284.1},
GN MOK16.19 {ECO:0000312|EMBL:BAB08388.1};
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 [GENOMIC DNA / MRNA], FUNCTION, DOMAIN, MUTAGENESIS OF
RP HIS-1143, AND DISRUPTION PHENOTYPE.
RX PubMed=10381874; DOI=10.1126/science.284.5423.2148;
RA Alonso J.M., Hirayama T., Roman G., Nourizadeh S., Ecker J.R.;
RT "EIN2, a bifunctional transducer of ethylene and stress responses in
RT Arabidopsis.";
RL Science 284:2148-2152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=7770519; DOI=10.1104/pp.107.4.1075;
RA Cary A.J., Liu W., Howell S.H.;
RT "Cytokinin action is coupled to ethylene in its effects on the inhibition
RT of root and hypocotyl elongation in Arabidopsis thaliana seedlings.";
RL Plant Physiol. 107:1075-1082(1995).
RN [6]
RP FUNCTION.
RX PubMed=9351240; DOI=10.1111/j.0960-7412.1997.00527.x;
RA Oh S.A., Park J.-H., Lee G.I., Paek K.H., Park S.K., Nam H.G.;
RT "Identification of three genetic loci controlling leaf senescence in
RT Arabidopsis thaliana.";
RL Plant J. 12:527-535(1997).
RN [7]
RP FUNCTION.
RX PubMed=12953109; DOI=10.1105/tpc.013060;
RA Hall A.E., Bleecker A.B.;
RT "Analysis of combinatorial loss-of-function mutants in the Arabidopsis
RT ethylene receptors reveals that the ers1 etr1 double mutant has severe
RT developmental defects that are EIN2 dependent.";
RL Plant Cell 15:2032-2041(2003).
RN [8]
RP FUNCTION.
RX PubMed=15010611; DOI=10.1023/b:plan.0000019064.55734.52;
RA Tamaoki M., Nakajima N., Kubo A., Aono M., Matsuyama T., Saji H.;
RT "Transcriptome analysis of O3-exposed Arabidopsis reveals that multiple
RT signal pathways act mutually antagonistically to induce gene expression.";
RL Plant Mol. Biol. 53:443-456(2003).
RN [9]
RP FUNCTION.
RX PubMed=14973160; DOI=10.1105/tpc.019661;
RA Seifert G.J., Barber C., Wells B., Roberts K.;
RT "Growth regulators and the control of nucleotide sugar flux.";
RL Plant Cell 16:723-730(2004).
RN [10]
RP FUNCTION.
RX PubMed=15272873; DOI=10.1111/j.1365-313x.2004.02156.x;
RA De Paepe A., Vuylsteke M., Van Hummelen P., Zabeau M., Van Der Straeten D.;
RT "Transcriptional profiling by cDNA-AFLP and microarray analysis reveals
RT novel insights into the early response to ethylene in Arabidopsis.";
RL Plant J. 39:537-559(2004).
RN [11]
RP INTERACTION WITH EER5; CSN3; CSN6A AND CSN6B.
RX PubMed=18429939; DOI=10.1111/j.1365-313x.2008.03521.x;
RA Christians M.J., Robles L.M., Zeller S.M., Larsen P.B.;
RT "The eer5 mutation, which affects a novel proteasome-related subunit,
RT indicates a prominent role for the COP9 signalosome in resetting the
RT ethylene-signaling pathway in Arabidopsis.";
RL Plant J. 55:467-477(2008).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ETR1.
RX PubMed=19769567; DOI=10.1042/bj20091102;
RA Bisson M.M., Bleckmann A., Allekotte S., Groth G.;
RT "EIN2, the central regulator of ethylene signalling, is localized at the ER
RT membrane where it interacts with the ethylene receptor ETR1.";
RL Biochem. J. 424:1-6(2009).
RN [13]
RP FUNCTION, INTERACTION WITH ETP1 AND ETP2, AND DOMAIN.
RX PubMed=19196655; DOI=10.1101/gad.1765709;
RA Qiao H., Chang K.N., Yazaki J., Ecker J.R.;
RT "Interplay between ethylene, ETP1/ETP2 F-box proteins, and degradation of
RT EIN2 triggers ethylene responses in Arabidopsis.";
RL Genes Dev. 23:512-521(2009).
RN [14]
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 [15]
RP INTERACTION WITH ETR1; ERS1; ETR2; ERS2 AND EIN4.
RX PubMed=20591837; DOI=10.1093/mp/ssq036;
RA Bisson M.M., Groth G.;
RT "New insight in ethylene signaling: autokinase activity of ETR1 modulates
RT the interaction of receptors and EIN2.";
RL Mol. Plant 3:882-889(2010).
RN [16]
RP FUNCTION.
RX PubMed=20647342; DOI=10.1105/tpc.110.076588;
RA An F., Zhao Q., Ji Y., Li W., Jiang Z., Yu X., Zhang C., Han Y., He W.,
RA Liu Y., Zhang S., Ecker J.R., Guo H.;
RT "Ethylene-induced stabilization of ETHYLENE INSENSITIVE3 and EIN3-LIKE1 is
RT mediated by proteasomal degradation of EIN3 binding F-box 1 and 2 that
RT requires EIN2 in Arabidopsis.";
RL Plant Cell 22:2384-2401(2010).
RN [17]
RP FUNCTION.
RX DOI=10.1007/s13258-011-0044-y;
RA Kim J.H., Chung K.M., Woo H.R.;
RT "Three positive regulators of leaf senescence in Arabidopsis, ORE1, ORE3
RT and ORE9, play roles in crosstalk among multiple hormone-mediated
RT senescence pathways.";
RL Genes Genomics 33:373-381(2011).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MRF3/ECIP1.
RC STRAIN=cv. Columbia;
RX PubMed=21631530; DOI=10.1111/j.1365-3040.2011.02363.x;
RA Lei G., Shen M., Li Z.G., Zhang B., Duan K.X., Wang N., Cao Y.R.,
RA Zhang W.K., Ma B., Ling H.Q., Chen S.Y., Zhang J.S.;
RT "EIN2 regulates salt stress response and interacts with a MA3 domain-
RT containing protein ECIP1 in Arabidopsis.";
RL Plant Cell Environ. 34:1678-1692(2011).
RN [19]
RP FUNCTION (EIN2-CEND), SUBCELLULAR LOCATION (EIN2-CEND), SUBCELLULAR
RP LOCATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=23070300; DOI=10.1038/cr.2012.145;
RA Wen X., Zhang C., Ji Y., Zhao Q., He W., An F., Jiang L., Guo H.;
RT "Activation of ethylene signaling is mediated by nuclear translocation of
RT the cleaved EIN2 carboxyl terminus.";
RL Cell Res. 22:1613-1616(2012).
RN [20]
RP INTERACTION WITH CTR1, PHOSPHORYLATION AT SER-645; SER-659; SER-757;
RP THR-819; SER-924 AND SER-1283, MUTAGENESIS OF SER-645 AND SER-924,
RP SUBCELLULAR LOCATION, SUBCELLULAR LOCATION (EIN2-CEND), AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=23132950; DOI=10.1073/pnas.1214848109;
RA Ju C., Yoon G.M., Shemansky J.M., Lin D.Y., Ying Z.I., Chang J.,
RA Garrett W.M., Kessenbrock M., Groth G., Tucker M.L., Cooper B.,
RA Kieber J.J., Chang C.;
RT "CTR1 phosphorylates the central regulator EIN2 to control ethylene hormone
RT signaling from the ER membrane to the nucleus in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19486-19491(2012).
RN [21]
RP SUBCELLULAR LOCATION, SUBCELLULAR LOCATION (EIN2-CEND), PROTEOLYTIC
RP PROCESSING, PHOSPHORYLATION AT SER-645; SER-659 AND SER-757, AND
RP MUTAGENESIS OF SER-645.
RX PubMed=22936567; DOI=10.1126/science.1225974;
RA Qiao H., Shen Z., Huang S.S., Schmitz R.J., Urich M.A., Briggs S.P.,
RA Ecker J.R.;
RT "Processing and subcellular trafficking of ER-tethered EIN2 control
RT response to ethylene gas.";
RL Science 338:390-393(2012).
RN [22]
RP REVIEW.
RX PubMed=23239828; DOI=10.1093/mp/sss150;
RA Ji Y., Guo H.;
RT "From endoplasmic reticulum (ER) to nucleus: EIN2 bridges the gap in
RT ethylene signaling.";
RL Mol. Plant 6:11-14(2013).
RN [23]
RP FUNCTION (EIN2-CEND), MUTAGENESIS OF 1262-LEU--LEU-1269, SUBCELLULAR
RP LOCATION (EIN2-CEND), AND INTERACTION WITH XRN4/EIN5; PAB2; PAB4 AND PAB8
RP (EIN2-CEND).
RX PubMed=26496607; DOI=10.1016/j.cell.2015.09.037;
RA Li W., Ma M., Feng Y., Li H., Wang Y., Ma Y., Li M., An F., Guo H.;
RT "EIN2-directed translational regulation of ethylene signaling in
RT Arabidopsis.";
RL Cell 163:670-683(2015).
RN [24]
RP FUNCTION (EIN2-CEND), AND SUBCELLULAR LOCATION (EIN2-CEND).
RX PubMed=26496608; DOI=10.1016/j.cell.2015.09.036;
RA Merchante C., Brumos J., Yun J., Hu Q., Spencer K.R., Enriquez P.,
RA Binder B.M., Heber S., Stepanova A.N., Alonso J.M.;
RT "Gene-specific translation regulation mediated by the hormone-signaling
RT molecule EIN2.";
RL Cell 163:684-697(2015).
RN [25]
RP INTERACTION WITH ETR1, DOMAIN, SUBCELLULAR LOCATION (EIN2-CEND), AND
RP MUTAGENESIS OF 1262-LEU--LEU-1269.
RX PubMed=25843012; DOI=10.1016/j.molp.2015.03.014;
RA Bisson M.M., Groth G.;
RT "Targeting plant ethylene responses by controlling essential protein-
RT protein interactions in the ethylene pathway.";
RL Mol. Plant 8:1165-1174(2015).
RN [26]
RP SUBCELLULAR LOCATION, AND INDUCTION BY HYPOXIA.
RC STRAIN=cv. Columbia;
RX PubMed=25822663; DOI=10.1371/journal.pgen.1005143;
RA Xie L.-J., Chen Q.-F., Chen M.-X., Yu L.-J., Huang L., Chen L., Wang F.-Z.,
RA Xia F.-N., Zhu T.-R., Wu J.-X., Yin J., Liao B., Shi J., Zhang J.-H.,
RA Aharoni A., Yao N., Shu W., Xiao S.;
RT "Unsaturation of very-long-chain ceramides protects plant from hypoxia-
RT induced damages by modulating ethylene signaling in Arabidopsis.";
RL PLoS Genet. 11:e1005143-e1005143(2015).
RN [27]
RP FUNCTION, FUNCTION (EIN2-CEND), SUBCELLULAR LOCATION (EIN2-CEND), AND
RP TISSUE SPECIFICITY.
RX PubMed=26507893; DOI=10.1093/jxb/erv438;
RA Zhang Y., Liu J., Chai J., Xing D.;
RT "Mitogen-activated protein kinase 6 mediates nuclear translocation of ORE3
RT to promote ORE9 gene expression in methyl jasmonate-induced leaf
RT senescence.";
RL J. Exp. Bot. 67:83-94(2016).
RN [28]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ENAP1.
RC STRAIN=cv. Columbia;
RX PubMed=27694846; DOI=10.1038/ncomms13018;
RA Zhang F., Qi B., Wang L., Zhao B., Rode S., Riggan N.D., Ecker J.R.,
RA Qiao H.;
RT "EIN2-dependent regulation of acetylation of histone H3K14 and non-
RT canonical histone H3K23 in ethylene signalling.";
RL Nat. Commun. 7:13018-13018(2016).
RN [29]
RP FUNCTION, MUTAGENESIS OF SER-645, DISRUPTION PHENOTYPE, AND INTERACTION
RP WITH ENAP1.
RC STRAIN=cv. Columbia;
RX PubMed=28874528; DOI=10.1073/pnas.1707937114;
RA Zhang F., Wang L., Qi B., Zhao B., Ko E.E., Riggan N.D., Chin K., Qiao H.;
RT "EIN2 mediates direct regulation of histone acetylation in the ethylene
RT response.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:10274-10279(2017).
RN [30]
RP REGULATION BY EEN AND EIN6.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=31418686; DOI=10.7554/elife.47835;
RA Zander M., Willige B.C., He Y., Nguyen T.A., Langford A.E., Nehring R.,
RA Howell E., McGrath R., Bartlett A., Castanon R., Nery J.R., Chen H.,
RA Zhang Z., Jupe F., Stepanova A., Schmitz R.J., Lewsey M.G., Chory J.,
RA Ecker J.R.;
RT "Epigenetic silencing of a multifunctional plant stress regulator.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Central factor in signaling pathways regulated by ethylene
CC (ET) and involved in various processes including development, plant
CC defense, senescence, nucleotide sugar flux, and tropisms
CC (PubMed:27694846, PubMed:28874528). Necessary for ethylene-mediated
CC gene regulation, and for the induction of some genes by ozone. Acts
CC downstream of ET receptors, and upstream of ethylene regulated
CC transcription factors. Required for cytokinin-mediated processes. Seems
CC to be implicated in cross-talk between ET, jasmonate and other
CC pathways. Probably not involved in iron uptake (PubMed:10381874,
CC PubMed:12953109, PubMed:14973160, PubMed:15010611, PubMed:15272873,
CC PubMed:7770519, PubMed:9351240). Has a short half-life and undergoes
CC rapid proteasome-mediated turnover in the absence of ethylene
CC (PubMed:19196655). Required for ethylene-induced EIN3 stabilization via
CC proteasomal degradation of EBF1/EBF2 proteins (PubMed:20647342).
CC Regulates the leaf senescence induced by methyl jasmonate, ethylene and
CC abscisic acid (Ref.17, PubMed:15010611). Required during salt stress to
CC confer resistance (PubMed:21631530). {ECO:0000269|PubMed:10381874,
CC ECO:0000269|PubMed:12953109, ECO:0000269|PubMed:14973160,
CC ECO:0000269|PubMed:15010611, ECO:0000269|PubMed:15272873,
CC ECO:0000269|PubMed:19196655, ECO:0000269|PubMed:20647342,
CC ECO:0000269|PubMed:21631530, ECO:0000269|PubMed:27694846,
CC ECO:0000269|PubMed:28874528, ECO:0000269|PubMed:7770519,
CC ECO:0000269|PubMed:9351240, ECO:0000269|Ref.17}.
CC -!- FUNCTION: [EIN2-CEND]: Trafficking signal inducing ethylene response.
CC The nuclear localization is both necessary and sufficient to activate
CC EIN3-mediated transcription and ethylene responses (PubMed:23070300).
CC Involved in ethylene (ET)-mediated signaling pathways by triggering
CC histone acetylation of H3K14 and H3K23 in an ENAP1-dependent manner,
CC thus influencing the expression of ethylene-responsive genes
CC (PubMed:27694846, PubMed:28874528). Necessary and sufficient for 3'-
CC UTR-mediated translational repression of EBF1 and EBF2 mRNAs. Ethylene
CC induces EIN2-CEND to associate with 3' UTRs in cytoplasmic foci and
CC target EBF1/2 mRNAs to cytoplasmic processing-body (P-body)
CC (PubMed:26496607, PubMed:26496608). MPK6 regulates the cleavage and
CC nuclear translocation of EIN2-CEND under methyl jasmonate treatment
CC (PubMed:26507893). Required for EIN3 accumulation (PubMed:26507893).
CC {ECO:0000269|PubMed:23070300, ECO:0000269|PubMed:26496607,
CC ECO:0000269|PubMed:26496608, ECO:0000269|PubMed:26507893,
CC ECO:0000269|PubMed:27694846, ECO:0000269|PubMed:28874528}.
CC -!- SUBUNIT: Interacts (via NLS) with ETR1 (PubMed:19769567,
CC PubMed:25843012). Interacts (via C-terminus) with EER5 and the COP9
CC signalosome subunits CSN3, CSN6A and CSN6B (PubMed:18429939). Interacts
CC with ETP1 and ETP2 (PubMed:19196655). Interacts with CTR1
CC (PubMed:23132950). Interacts with all members of the ethylene receptor
CC family, including ETR1, ETR2, ERS1, ERS2 and EIN4 (PubMed:20591837).
CC Binds to MRF3/ECIP1 (PubMed:21631530). {ECO:0000269|PubMed:18429939,
CC ECO:0000269|PubMed:19196655, ECO:0000269|PubMed:19769567,
CC ECO:0000269|PubMed:20591837, ECO:0000269|PubMed:21631530,
CC ECO:0000269|PubMed:23132950, ECO:0000269|PubMed:25843012}.
CC -!- SUBUNIT: [EIN2-CEND]: Interacts with several P-body components, such as
CC XRN4/EIN5, PAB2, PAB4 and PAB8 (PubMed:26496607). Binds to ENAP1 in the
CC presence of ethylene; this reaction facilitates its association with
CC histone (PubMed:27694846, PubMed:28874528).
CC {ECO:0000269|PubMed:26496607, ECO:0000269|PubMed:27694846,
CC ECO:0000269|PubMed:28874528}.
CC -!- INTERACTION:
CC Q9S814; Q9LJ68: ETP1; NbExp=4; IntAct=EBI-2437287, EBI-1238820;
CC Q9S814; Q9LJ74: ETP2; NbExp=2; IntAct=EBI-2437287, EBI-2437385;
CC Q9S814; P49333: ETR1; NbExp=2; IntAct=EBI-2437287, EBI-1606682;
CC -!- SUBCELLULAR LOCATION: [Ethylene-insensitive protein 2]: Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:19769567,
CC ECO:0000269|PubMed:22936567, ECO:0000269|PubMed:23070300,
CC ECO:0000269|PubMed:23132950}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [EIN2-CEND]: Nucleus
CC {ECO:0000269|PubMed:22936567, ECO:0000269|PubMed:23070300,
CC ECO:0000269|PubMed:23132950, ECO:0000269|PubMed:25822663,
CC ECO:0000269|PubMed:26496607, ECO:0000269|PubMed:26496608,
CC ECO:0000269|PubMed:26507893}. Cytoplasm {ECO:0000269|PubMed:23070300,
CC ECO:0000269|PubMed:25843012, ECO:0000269|PubMed:26496607,
CC ECO:0000269|PubMed:26496608}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25822663, ECO:0000269|PubMed:25843012}.
CC Note=Perception of ethylene or methyl jasmonate leads to proteolytic
CC cleavage allowing the C-terminal domain to localize to the nucleus
CC while the N-terminus remains at the endoplasmic reticulum membrane.
CC Apart from nuclear localization, some association with endoplasmic
CC membranes and some speckles are also observed in the cytoplasm. During
CC hypoxia (e.g. submergences), translocates from endoplasmic reticulum
CC (ER) to the nucleus via a ceramides-triggered and CTR1-dependent manner
CC (PubMed:25822663). {ECO:0000269|PubMed:22936567,
CC ECO:0000269|PubMed:23070300, ECO:0000269|PubMed:23132950,
CC ECO:0000269|PubMed:25822663, ECO:0000269|PubMed:25843012,
CC ECO:0000269|PubMed:26496607, ECO:0000269|PubMed:26496608,
CC ECO:0000269|PubMed:26507893}.
CC -!- TISSUE SPECIFICITY: [EIN2-CEND]: Localized to the guard cells after
CC methyl jasmonate treatment. {ECO:0000269|PubMed:26507893}.
CC -!- INDUCTION: Accumuates upon hypoxia (e.g. submergences)
CC (PubMed:25822663). Expression level is enhanced by a chromatin-
CC dependent epigenetic regulatory mechanism involving both EEN and
CC REF6/EIN6 (PubMed:31418686). {ECO:0000269|PubMed:25822663,
CC ECO:0000269|PubMed:31418686}.
CC -!- DOMAIN: The N-terminal (1-560) region seems to be regulated by upstream
CC components of the ET signal transduction pathway, and may in turn
CC regulate the C-terminal region. The C-terminal (454-1294) region
CC regulates downstream events of ET and jasmonate signaling pathways, and
CC can confer constitutive responses to ET. The C-terminal (1047-1294)
CC region is necessary and sufficient for interactions with ETP1 and ETP2
CC (PubMed:19196655). The nuclear localization signal (1262-1269) is
CC required for interaction with ETR1 (PubMed:25843012).
CC {ECO:0000269|PubMed:10381874, ECO:0000269|PubMed:19196655,
CC ECO:0000269|PubMed:25843012}.
CC -!- PTM: Phosphorylated by CTR1 on at least 4 sites. Phosphorylation of
CC Ser-645 and Ser-924 is involved in repressing EIN2 signaling. Loss of
CC phosphorylation results in nuclear localization of the C-terminus of
CC EIN2. {ECO:0000269|PubMed:23132950}.
CC -!- DISRUPTION PHENOTYPE: Complete ethylene insensitivity
CC (PubMed:10381874). Extreme salt sensitivity during seed germination and
CC plant growth leading to epinastic backward growth of leaf blade and
CC petiole, and small rosette size (PubMed:21631530). Reduced ethylene-
CC induced histone acetylation of H3K14 and H3K23 associated with a lower
CC induction of ethylene-responsive genes (PubMed:27694846,
CC PubMed:28874528). {ECO:0000269|PubMed:10381874,
CC ECO:0000269|PubMed:21631530, ECO:0000269|PubMed:27694846,
CC ECO:0000269|PubMed:28874528}.
CC -!- MISCELLANEOUS: 'Oresara' means 'long living' in Korean.
CC {ECO:0000305|PubMed:9351240}.
CC -!- SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family. {ECO:0000305}.
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DR EMBL; AF141202; AAD41076.1; -; Genomic_DNA.
DR EMBL; AF141203; AAD41077.1; -; mRNA.
DR EMBL; AB005240; BAB08388.1; -; Genomic_DNA.
DR EMBL; AL162751; CAB83284.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90580.1; -; Genomic_DNA.
DR PIR; T48349; T48349.
DR RefSeq; NP_195948.1; NM_120406.5.
DR AlphaFoldDB; Q9S814; -.
DR SMR; Q9S814; -.
DR BioGRID; 17165; 12.
DR IntAct; Q9S814; 3.
DR STRING; 3702.AT5G03280.1; -.
DR TCDB; 2.A.55.2.8; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR iPTMnet; Q9S814; -.
DR PaxDb; Q9S814; -.
DR PRIDE; Q9S814; -.
DR ProteomicsDB; 220445; -.
DR EnsemblPlants; AT5G03280.1; AT5G03280.1; AT5G03280.
DR GeneID; 831889; -.
DR Gramene; AT5G03280.1; AT5G03280.1; AT5G03280.
DR KEGG; ath:AT5G03280; -.
DR Araport; AT5G03280; -.
DR TAIR; locus:2142594; AT5G03280.
DR eggNOG; KOG1291; Eukaryota.
DR HOGENOM; CLU_006509_0_0_1; -.
DR InParanoid; Q9S814; -.
DR OMA; QMNANRN; -.
DR OrthoDB; 666470at2759; -.
DR PhylomeDB; Q9S814; -.
DR PRO; PR:Q9S814; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S814; baseline and differential.
DR Genevisible; Q9S814; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0001736; P:establishment of planar polarity; IGI:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0016573; P:histone acetylation; IMP:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IMP:UniProtKB.
DR GO; GO:0043972; P:histone H3-K23 acetylation; IMP:UniProtKB.
DR GO; GO:0009871; P:jasmonic acid and ethylene-dependent systemic resistance, ethylene mediated signaling pathway; TAS:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0048765; P:root hair cell differentiation; IGI:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR InterPro; IPR017187; EIN2.
DR InterPro; IPR001046; NRAMP_fam.
DR PANTHER; PTHR11706; PTHR11706; 1.
DR Pfam; PF01566; Nramp; 1.
DR PIRSF; PIRSF037378; EIN2; 1.
DR PRINTS; PR00447; NATRESASSCMP.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Chromatin regulator; Cytokinin signaling pathway;
KW Cytoplasm; Endoplasmic reticulum; Ethylene signaling pathway; Membrane;
KW Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..1294
FT /note="Ethylene-insensitive protein 2"
FT /id="PRO_0000212604"
FT CHAIN 646..1294
FT /note="EIN2-CEND"
FT /evidence="ECO:0000269|PubMed:22936567"
FT /id="PRO_0000435290"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..1294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 534..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23132950"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23132950"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23132950"
FT MOD_RES 819
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23132950"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23132950"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23132950"
FT MUTAGEN 645
FT /note="S->A: Constitutive of ethylene response in absence
FT of ethylene associated with an increased histone
FT acetylation of H3K14 and H3K23. 85% decreased
FT phosphorylation and constitutive activation of ethylene
FT response; when associated with A-924."
FT /evidence="ECO:0000269|PubMed:22936567,
FT ECO:0000269|PubMed:23132950, ECO:0000269|PubMed:28874528"
FT MUTAGEN 645
FT /note="S->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:22936567"
FT MUTAGEN 924
FT /note="S->A: 85% decreased phosphorylation and constitutive
FT activation of ethylene response; when associated with A-
FT 645."
FT /evidence="ECO:0000269|PubMed:23132950"
FT MUTAGEN 1143
FT /note="H->P: In ein2-9; lower sensitivity to ethylene."
FT /evidence="ECO:0000269|PubMed:10381874"
FT MUTAGEN 1262..1269
FT /note="LKRYKRRL->KPKKKRKV: No effect on nuclear
FT translocation but loss of translational repression
FT function."
FT /evidence="ECO:0000269|PubMed:26496607"
FT MUTAGEN 1262..1269
FT /note="Missing: Loss of nuclear localization, EIN2-CEND
FT functions and interaction with ETR1."
FT /evidence="ECO:0000269|PubMed:25843012,
FT ECO:0000269|PubMed:26496607"
SQ SEQUENCE 1294 AA; 140956 MW; 1A806303B8B8E71B CRC64;
MEAEIVNVRP QLGFIQRMVP ALLPVLLVSV GYIDPGKWVA NIEGGARFGY DLVAITLLFN
FAAILCQYVA ARISVVTGKH LAQICNEEYD KWTCMFLGIQ AEFSAILLDL TMVVGVAHAL
NLLFGVELST GVFLAAMDAF LFPVFASFLE NGMANTVSIY SAGLVLLLYV SGVLLSQSEI
PLSMNGVLTR LNGESAFALM GLLGASIVPH NFYIHSYFAG ESTSSSDVDK SSLCQDHLFA
IFGVFSGLSL VNYVLMNAAA NVFHSTGLVV LTFHDALSLM EQVFMSPLIP VVFLMLLFFS
SQITALAWAF GGEVVLHDFL KIEIPAWLHR ATIRILAVAP ALYCVWTSGA DGIYQLLIFT
QVLVAMMLPC SVIPLFRIAS SRQIMGVHKI PQVGEFLALT TFLGFLGLNV VFVVEMVFGS
SDWAGGLRWN TVMGTSIQYT TLLVSSCASL CLILWLAATP LKSASNRAEA QIWNMDAQNA
LSYPSVQEEE IERTETRRNE DESIVRLESR VKDQLDTTSV TSSVYDLPEN ILMTDQEIRS
SPPEERELDV KYSTSQVSSL KEDSDVKEQS VLQSTVVNEV SDKDLIVETK MAKIEPMSPV
EKIVSMENNS KFIEKDVEGV SWETEEATKA APTSNFTVGS DGPPSFRSLS GEGGSGTGSL
SRLQGLGRAA RRHLSAILDE FWGHLYDFHG QLVAEARAKK LDQLFGTDQK SASSMKADSF
GKDISSGYCM SPTAKGMDSQ MTSSLYDSLK QQRTPGSIDS LYGLQRGSSP SPLVNRMQML
GAYGNTTNNN NAYELSERRY SSLRAPSSSE GWEHQQPATV HGYQMKSYVD NLAKERLEAL
QSRGEIPTSR SMALGTLSYT QQLALALKQK SQNGLTPGPA PGFENFAGSR SISRQSERSY
YGVPSSGNTD TVGAAVANEK KYSSMPDISG LSMSARNMHL PNNKSGYWDP SSGGGGYGAS
YGRLSNESSL YSNLGSRVGV PSTYDDISQS RGGYRDAYSL PQSATTGTGS LWSRQPFEQF
GVAERNGAVG EELRNRSNPI NIDNNASSNV DAEAKLLQSF RHCILKLIKL EGSEWLFGQS
DGVDEELIDR VAAREKFIYE AEAREINQVG HMGEPLISSV PNCGDGCVWR ADLIVSFGVW
CIHRVLDLSL MESRPELWGK YTYVLNRLQG VIDPAFSKLR TPMTPCFCLQ IPASHQRASP
TSANGMLPPA AKPAKGKCTT AVTLLDLIKD VEMAISCRKG RTGTAAGDVA FPKGKENLAS
VLKRYKRRLS NKPVGMNQDG PGSRKNVTAY GSLG
