EDS1C_ARATH
ID EDS1C_ARATH Reviewed; 623 AA.
AC Q9SU72; B9DFM5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Protein EDS1 {ECO:0000305};
DE AltName: Full=Enhanced disease susceptibility 1 {ECO:0000303|PubMed:10077677};
GN Name=EDS1 {ECO:0000303|PubMed:10077677};
GN Synonyms=EDS1-90 {ECO:0000303|PubMed:22072959},
GN EDS1A {ECO:0000303|PubMed:16040633};
GN OrderedLocusNames=At3g48090 {ECO:0000312|Araport:AT3G48090};
GN ORFNames=T17F15.40 {ECO:0000312|EMBL:CAB41130.1};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, AND
RP INDUCTION BY PATHOGEN AND SALICYLIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=10077677; DOI=10.1073/pnas.96.6.3292;
RA Falk A., Feys B.J., Frost L.N., Jones J.D., Daniels M.J., Parker J.E.;
RT "EDS1, an essential component of R gene-mediated disease resistance in
RT Arabidopsis has homology to eukaryotic lipases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3292-3297(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia, cv. Gu-0, and cv. Wei-0;
RX PubMed=19064707; DOI=10.1534/genetics.108.097279;
RA Caldwell K.S., Michelmore R.W.;
RT "Arabidopsis thaliana genes encoding defense signaling and recognition
RT proteins exhibit contrasting evolutionary dynamics.";
RL Genetics 181:671-684(2009).
RN [3]
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 [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 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Rosette leaf;
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).
RN [7]
RP FUNCTION, INTERACTION WITH PAD4, SUBUNIT, AND MUTAGENESIS OF GLU-466.
RX PubMed=11574472; DOI=10.1093/emboj/20.19.5400;
RA Feys B.J., Moisan L.J., Newman M.-A., Parker J.E.;
RT "Direct interaction between the Arabidopsis disease resistance signaling
RT proteins, EDS1 and PAD4.";
RL EMBO J. 20:5400-5411(2001).
RN [8]
RP INTERACTION WITH SAG101 AND PAD4, AND SUBCELLULAR LOCATION.
RX PubMed=16040633; DOI=10.1105/tpc.105.033910;
RA Feys B.J., Wiermer M., Bhat R.A., Moisan L.J., Medina-Escobar N., Neu C.,
RA Cabral A., Parker J.E.;
RT "Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals within an
RT ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity.";
RL Plant Cell 17:2601-2613(2005).
RN [9]
RP FUNCTION.
RX PubMed=19578402; DOI=10.1371/journal.pgen.1000545;
RA Venugopal S.C., Jeong R.D., Mandal M.K., Zhu S., Chandra-Shekara A.C.,
RA Xia Y., Hersh M., Stromberg A.J., Navarre D., Kachroo A., Kachroo P.;
RT "Enhanced disease susceptibility 1 and salicylic acid act redundantly to
RT regulate resistance gene-mediated signaling.";
RL PLoS Genet. 5:E1000545-E1000545(2009).
RN [10]
RP FUNCTION.
RX PubMed=20617163; DOI=10.1371/journal.ppat.1000970;
RA Garcia A.V., Blanvillain-Baufume S., Huibers R.P., Wiermer M., Li G.,
RA Gobbato E., Rietz S., Parker J.E.;
RT "Balanced nuclear and cytoplasmic activities of EDS1 are required for a
RT complete plant innate immune response.";
RL PLoS Pathog. 6:E1000970-E1000970(2010).
RN [11]
RP FUNCTION, INTERACTION WITH PAD4 AND SAG101, MUTAGENESIS OF LEU-262 AND
RP GLU-466, AND SUBUNIT.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=21434927; DOI=10.1111/j.1469-8137.2011.03675.x;
RA Rietz S., Stamm A., Malonek S., Wagner S., Becker D., Medina-Escobar N.,
RA Vlot A.C., Feys B.J., Niefind K., Parker J.E.;
RT "Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to and
RT dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis immunity.";
RL New Phytol. 191:107-119(2011).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALICYLIC ACID AND VIRUS
RP INFECTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=22072959; DOI=10.1371/journal.ppat.1002318;
RA Zhu S., Jeong R.-D., Venugopal S.C., Lapchyk L., Navarre D., Kachroo A.,
RA Kachroo P.;
RT "SAG101 forms a ternary complex with EDS1 and PAD4 and is required for
RT resistance signaling against turnip crinkle virus.";
RL PLoS Pathog. 7:E1002318-E1002318(2011).
RN [13]
RP INTERACTION WITH AVRRPS4 AND RPS4, AND SUBCELLULAR LOCATION.
RX PubMed=22158818; DOI=10.1126/science.1211641;
RA Heidrich K., Wirthmueller L., Tasset C., Pouzet C., Deslandes L.,
RA Parker J.E.;
RT "Arabidopsis EDS1 connects pathogen effector recognition to cell
RT compartment-specific immune responses.";
RL Science 334:1401-1404(2011).
RN [14]
RP FUNCTION, INTERACTION WITH RPS4; RPS6; SNC1; SRFR1; AVRRPS4 AND HOPA1,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22158819; DOI=10.1126/science.1211592;
RA Bhattacharjee S., Halane M.K., Kim S.H., Gassmann W.;
RT "Pathogen effectors target Arabidopsis EDS1 and alter its interactions with
RT immune regulators.";
RL Science 334:1405-1408(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP FUNCTION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22316300; DOI=10.1094/mpmi-05-11-0111;
RA Moreau M., Degrave A., Vedel R., Bitton F., Patrit O., Renou J.-P.,
RA Barny M.-A., Fagard M.;
RT "EDS1 contributes to nonhost resistance of Arabidopsis thaliana against
RT Erwinia amylovora.";
RL Mol. Plant Microbe Interact. 25:421-430(2012).
RN [17]
RP INTERACTION WITH VICTR.
RX PubMed=23275581; DOI=10.1105/tpc.112.107235;
RA Kim T.H., Kunz H.H., Bhattacharjee S., Hauser F., Park J., Engineer C.,
RA Liu A., Ha T., Parker J.E., Gassmann W., Schroeder J.I.;
RT "Natural variation in small molecule-induced TIR-NB-LRR signaling induces
RT root growth arrest via EDS1- and PAD4-complexed R protein VICTR in
RT Arabidopsis.";
RL Plant Cell 24:5177-5192(2012).
RN [18]
RP FUNCTION.
RX PubMed=24331460; DOI=10.1016/j.chom.2013.11.006;
RA Wagner S., Stuttmann J., Rietz S., Guerois R., Brunstein E., Bautor J.,
RA Niefind K., Parker J.E.;
RT "Structural basis for signaling by exclusive EDS1 heteromeric complexes
RT with SAG101 or PAD4 in plant innate immunity.";
RL Cell Host Microbe 14:619-630(2013).
RN [19]
RP FUNCTION.
RX PubMed=24755512; DOI=10.1104/pp.114.239665;
RA Breitenbach H.H., Wenig M., Wittek F., Jorda L., Maldonado-Alconada A.M.,
RA Sarioglu H., Colby T., Knappe C., Bichlmeier M., Pabst E., Mackey D.,
RA Parker J.E., Vlot A.C.;
RT "Contrasting roles of the apoplastic aspartyl protease APOPLASTIC, ENHANCED
RT DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in
RT Arabidopsis systemic acquired resistance.";
RL Plant Physiol. 165:791-809(2014).
CC -!- FUNCTION: Positive regulator of basal resistance and of effector-
CC triggered immunity specifically mediated by TIR-NB-LRR (TNL) resistance
CC proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR
CC resistance protein interactions constitutes the first step in
CC resistance activation (PubMed:22158819). Acts redundantly with
CC salicylic acid to regulate resistance gene-mediated signaling
CC (PubMed:19578402). Triggers early plant defenses and hypersensitive
CC response independently of PAD4, and then recruits PAD4 to potentiate
CC plant defenses through the accumulation of salicylic acid
CC (PubMed:11574472). Nuclear localization is essential for basal and TNL-
CC conditioned immunity and for reprogramming defense gene expression,
CC while cytoplasmic EDS1 is required to induce a complete immune response
CC (PubMed:20617163). Heterodimerization with PAD4 and/or SGA101 is
CC necessary for TNL-mediated effector-triggered immunity
CC (PubMed:24331460). Contributes to nonhost resistance against
CC E.amylovora (PubMed:22316300). Loss of EDS1-PAD4 interaction
CC compromises basal but not TNL-triggered resistance (PubMed:21434927).
CC Necessary for systemic acquired resistance (SAR) signal generation and
CC perception (PubMed:24755512). Has no direct lipase activity
CC (PubMed:16040633). Putative lipase activity is dispensable for immune
CC functions (PubMed:24331460). {ECO:0000269|PubMed:10077677,
CC ECO:0000269|PubMed:11574472, ECO:0000269|PubMed:19578402,
CC ECO:0000269|PubMed:20617163, ECO:0000269|PubMed:21434927,
CC ECO:0000269|PubMed:22158819, ECO:0000269|PubMed:22316300,
CC ECO:0000269|PubMed:24755512, ECO:0000305|PubMed:16040633}.
CC -!- SUBUNIT: Homodimer (PubMed:11574472, PubMed:22158819). Interacts with
CC RPS4, RPS6, SNC1, SRFR1, AvrRps4 and HopA1 (PubMed:22158818,
CC PubMed:22158819). Part of a nuclear complex made of EDS1, PAD4 and
CC SAG101, that can be redirected to the cytoplasm in the presence of an
CC extranuclear form of EDS1 (PubMed:22072959).Interacts (via N-terminus)
CC with PAD4 (via N-terminus) (PubMed:11574472, PubMed:21434927,
CC PubMed:22072959). Interacts (via N-terminus) with SAG101
CC (PubMed:16040633, PubMed:21434927, PubMed:22072959). EDS1-SAG101 and
CC EDS1-PAD4 form separate complexes in pathogen-unchallenged cells
CC (PubMed:16040633, PubMed:21434927). Part of a nuclear protein complex
CC made of VICTR, PAD4 and EDS1 (PubMed:23275581). Interacts with VICTR
CC (PubMed:23275581). {ECO:0000269|PubMed:11574472,
CC ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:21434927,
CC ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:22158819,
CC ECO:0000269|PubMed:23275581, ECO:0000269|PubMed:24331460}.
CC -!- INTERACTION:
CC Q9SU72; Q94KL5: BLH4; NbExp=3; IntAct=EBI-1390454, EBI-1153797;
CC Q9SU72; Q05466: HAT4; NbExp=3; IntAct=EBI-1390454, EBI-4428728;
CC Q9SU72; Q8RXD6: HUB1; NbExp=4; IntAct=EBI-1390454, EBI-2012188;
CC Q9SU72; Q9S745: PAD4; NbExp=8; IntAct=EBI-1390454, EBI-1390441;
CC Q9SU72; Q38845: PP2AA1; NbExp=3; IntAct=EBI-1390454, EBI-1645478;
CC Q9SU72; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-1390454, EBI-4424877;
CC Q9SU72; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1390454, EBI-4426144;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16040633,
CC ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:22158819}. Cytoplasm
CC {ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:22072959,
CC ECO:0000269|PubMed:22158818, ECO:0000269|PubMed:22158819}. Microsome
CC {ECO:0000269|PubMed:22158819}. Note=Found in both the nucleus and
CC diffuse in the cytosol when associated with PAD4, in the nucleus and in
CC punctate spots in the cytoplasm when interacting with SRFR1, SNC1 or
CC RPS4, only in the nucleus when associated with SAG101 and in the
CC cytosol when it dimerizes. Found in the nucleus when interacting with
CC VICTR and PAD4. Interacts with AvrRps4 and HopA1 effectors in
CC microsomes. {ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:22072959,
CC ECO:0000269|PubMed:22158819, ECO:0000269|PubMed:23275581}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SU72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SU72-2; Sequence=VSP_057262;
CC -!- INDUCTION: Up-regulated by salicylic acid or upon turnip crinkle virus
CC or avirulent bacterial pathogen infection.
CC {ECO:0000269|PubMed:10077677, ECO:0000269|PubMed:22072959}.
CC -!- DISRUPTION PHENOTYPE: No effect on RPS4-mediated resistance against
CC avrRps4 bacteria, due to the redundancy with EDS1B.
CC {ECO:0000269|PubMed:22072959}.
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DR EMBL; EF470650; ABR45989.1; -; Genomic_DNA.
DR EMBL; EF470654; ABR45993.1; -; Genomic_DNA.
DR EMBL; EF470663; ABR46002.1; -; Genomic_DNA.
DR EMBL; AL049658; CAB41130.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78366.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78367.1; -; Genomic_DNA.
DR EMBL; AY046025; AAK76699.1; -; mRNA.
DR EMBL; AY150423; AAN12884.1; -; mRNA.
DR EMBL; AK316830; BAH19542.1; -; mRNA.
DR PIR; T06674; T06674.
DR RefSeq; NP_001030829.1; NM_001035752.1. [Q9SU72-2]
DR RefSeq; NP_190392.1; NM_114678.4. [Q9SU72-1]
DR AlphaFoldDB; Q9SU72; -.
DR SASBDB; Q9SU72; -.
DR SMR; Q9SU72; -.
DR ComplexPortal; CPX-1321; EDS1-SAG101 complex, variant EDS1.
DR ComplexPortal; CPX-1324; EDS1-PAD4 complex, variant EDS1.
DR ComplexPortal; CPX-1325; EDS1-PAD4-SAG101 complex, variant EDS1.
DR IntAct; Q9SU72; 9.
DR STRING; 3702.AT3G48090.1; -.
DR ESTHER; arath-eds1; Plant_lipase_EDS1-like.
DR iPTMnet; Q9SU72; -.
DR PaxDb; Q9SU72; -.
DR PRIDE; Q9SU72; -.
DR ProteomicsDB; 222074; -. [Q9SU72-1]
DR DNASU; 823964; -.
DR EnsemblPlants; AT3G48090.1; AT3G48090.1; AT3G48090. [Q9SU72-1]
DR EnsemblPlants; AT3G48090.2; AT3G48090.2; AT3G48090. [Q9SU72-2]
DR GeneID; 823964; -.
DR Gramene; AT3G48090.1; AT3G48090.1; AT3G48090. [Q9SU72-1]
DR Gramene; AT3G48090.2; AT3G48090.2; AT3G48090. [Q9SU72-2]
DR KEGG; ath:AT3G48090; -.
DR Araport; AT3G48090; -.
DR TAIR; locus:2097855; AT3G48090.
DR eggNOG; ENOG502QR4E; Eukaryota.
DR HOGENOM; CLU_016367_1_0_1; -.
DR InParanoid; Q9SU72; -.
DR OMA; GDNIFNH; -.
DR OrthoDB; 372547at2759; -.
DR PhylomeDB; Q9SU72; -.
DR PRO; PR:Q9SU72; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SU72; baseline and differential.
DR Genevisible; Q9SU72; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0106093; C:EDS1 disease-resistance complex; IDA:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016298; F:lipase activity; ISS:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0010618; P:aerenchyma formation; IMP:TAIR.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:ComplexPortal.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
DR GO; GO:0000304; P:response to singlet oxygen; IGI:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:ComplexPortal.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR044214; EDS1-like.
DR InterPro; IPR041266; EDS1_EP.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR47090; PTHR47090; 2.
DR Pfam; PF18117; EDS1_EP; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Hydrolase; Microsome; Nucleus; Plant defense;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..623
FT /note="Protein EDS1"
FT /id="PRO_0000431440"
FT COILED 358..383
FT /evidence="ECO:0000255"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P19515"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P19515"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P19515"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /id="VSP_057262"
FT MUTAGEN 262
FT /note="L->P: Loss of interaction with PAD4, but no effect
FT on dimerization or interaction with SAG101."
FT /evidence="ECO:0000269|PubMed:21434927"
FT MUTAGEN 466
FT /note="E->K: In eds1-1; loss of interaction with PAD4 and
FT SAG101, but no effect on dimerization."
FT /evidence="ECO:0000269|PubMed:11574472,
FT ECO:0000269|PubMed:21434927"
SQ SEQUENCE 623 AA; 71690 MW; F9B321D5DF77D96B CRC64;
MAFEALTGIN GDLITRSWSA SKQAYLTERY HKEEAGAVVI FAFQPSFSEK DFFDPDNKSS
FGEIKLNRVQ FPCMRKIGKG DVATVNEAFL KNLEAIIDPR TSFQASVEMA VRSRKQIVFT
GHSSGGATAI LATVWYLEKY FIRNPNVYLE PRCVTFGAPL VGDSIFSHAL GREKWSRFFV
NFVSRFDIVP RIMLARKASV EETLPHVLAQ LDPRKSSVQE SEQRITEFYT RVMRDTSTVA
NQAVCELTGS AEAFLETLSS FLELSPYRPA GTFVFSTEKR LVAVNNSDAI LQMLFYTSQA
SDEQEWSLIP FRSIRDHHSY EELVQSMGKK LFNHLDGENS IESTLNDLGV STRGRQYVQA
ALEEEKKRVE NQKKIIQVIE QERFLKKLAW IEDEYKPKCQ AHKNGYYDSF KVSNEENDFK
ANVKRAELAG VFDEVLGLMK KCQLPDEFEG DIDWIKLATR YRRLVEPLDI ANYHRHLKNE
DTGPYMKRGR PTRYIYAQRG YEHYILKPNG MIAEDVFWNK VNGLNLGLQL EEIQETLKNS
GSECGSCFWA EVEELKGKPY EEVEVRVKTL EGMLGEWITD GEVDDKEIFL EGSTFRKWWI
TLPKNHKSHS PLRDYMMDEI TDT
