EDS1L_ARATH
ID EDS1L_ARATH Reviewed; 623 AA.
AC Q9XF23;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Protein EDS1L {ECO:0000305};
DE AltName: Full=Enhanced disease susceptibility 1-like;
GN Name=EDS1 {ECO:0000312|EMBL:AAD20950.1};
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|EMBL:AAD20950.1};
RN [1] {ECO:0000312|EMBL:AAD20950.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION BY PATHOGEN AND
RP SALICYLIC ACID.
RC STRAIN=cv. Landsberg erecta;
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] {ECO:0000312|EMBL:ABR45991.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Di-0, and cv. Landsberg erecta;
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 FUNCTION, INTERACTION WITH PAD4, AND SUBUNIT.
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP CRYSTALLIZATION IN COMPLEX WITH SAG101.
RX PubMed=21301097; DOI=10.1107/s1744309110051249;
RA Wagner S., Rietz S., Parker J.E., Niefind K.;
RT "Crystallization and preliminary crystallographic analysis of Arabidopsis
RT thaliana EDS1, a key component of plant immunity, in complex with its
RT signalling partner SAG101.";
RL Acta Crystallogr. F 67:245-248(2011).
RN [10] {ECO:0000312|PDB:4NFU}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-623 IN COMPLEX WITH SAG101,
RP INTERACTION WITH SAG101 AND PAD4, DOMAIN, AND MUTAGENESIS OF PHE-47;
RP SER-123; ASP-187; VAL-189; ILE-254; LEU-258; PHE-261; LEU-262 AND HIS-317.
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).
CC -!- FUNCTION: Positive regulator of basal resistance and of effector-
CC triggered immunity specifically mediated by TIR-NB-LRR 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). Triggers early plant defenses
CC and hypersensitive response independently of PAD4, and then recruits
CC PAD4 to potentiate plant defenses through the accumulation of salicylic
CC acid (PubMed:11574472). Nuclear localization is essential for basal and
CC TIR-NB-LRR-conditioned immunity and for reprogramming defense gene
CC expression, while cytoplasmic EDS1 is required to induce a complete
CC immune response (PubMed:20617163). Heterodimerization with PAD4 or
CC SGA101 is necessary for TNL-mediated effector-triggered immunity
CC (PubMed:24331460). Contributes to nonhost resistance against
CC E.amylovora (PubMed:22316300). Has no direct lipase activity
CC (PubMed:16040633). {ECO:0000269|PubMed:10077677,
CC ECO:0000269|PubMed:11574472, ECO:0000269|PubMed:20617163,
CC ECO:0000269|PubMed:22158819, ECO:0000269|PubMed:22316300,
CC ECO:0000269|PubMed:24331460, ECO:0000305|PubMed:16040633}.
CC -!- SUBUNIT: Homodimer (PubMed:11574472, PubMed:22158819, PubMed:24331460).
CC Interacts with RPS4, RPS6, SNC1, SRFR1, AvrRps4 and HopA1
CC (PubMed:22158818, PubMed:22158819). Interacts with PAD4 (via N-
CC terminus) (PubMed:11574472, PubMed:24331460). Interacts with SAG101
CC (PubMed:16040633, PubMed:24331460). EDS1-SAG101 and EDS1-PAD4 form
CC separate complexes in pathogen-unchallenged cells (PubMed:16040633).
CC {ECO:0000269|PubMed:11574472, ECO:0000269|PubMed:16040633,
CC ECO:0000269|PubMed:22158819, ECO:0000269|PubMed:24331460}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16040633,
CC ECO:0000269|PubMed:22158819}. Cytoplasm {ECO:0000269|PubMed:16040633,
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. Interacts with AvrRps4 and HopA1 effectors
CC in microsomes. {ECO:0000269|PubMed:16040633,
CC ECO:0000269|PubMed:22158819}.
CC -!- INDUCTION: Up-regulated by salicylic acid or upon avirulent bacterial
CC pathogen infection. {ECO:0000269|PubMed:10077677}.
CC -!- DOMAIN: The N-terminal domain (1-384) is necessary and sufficient for
CC interaction with SAG101. {ECO:0000269|PubMed:24331460}.
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DR EMBL; AF128407; AAD20950.1; -; Genomic_DNA.
DR EMBL; EF470652; ABR45991.1; -; Genomic_DNA.
DR EMBL; EF470656; ABR45995.1; -; Genomic_DNA.
DR PIR; T48859; T48859.
DR PDB; 4NFU; X-ray; 2.21 A; A=2-623.
DR PDB; 6I8G; X-ray; 2.34 A; A=1-623.
DR PDB; 6I8H; X-ray; 3.68 A; A=1-623.
DR PDB; 6Q6Z; X-ray; 3.48 A; A=1-623.
DR PDBsum; 4NFU; -.
DR PDBsum; 6I8G; -.
DR PDBsum; 6I8H; -.
DR PDBsum; 6Q6Z; -.
DR AlphaFoldDB; Q9XF23; -.
DR SMR; Q9XF23; -.
DR ESTHER; arath-eds1; Plant_lipase_EDS1-like.
DR ABCD; Q9XF23; 3 sequenced antibodies.
DR ExpressionAtlas; Q9XF23; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Microsome; Nucleus; Plant defense.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SU72"
FT CHAIN 2..623
FT /note="Protein EDS1L"
FT /id="PRO_0000431441"
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:0000250|UniProtKB:Q9SU72"
FT MUTAGEN 47
FT /note="F->W: No effect on basal resistance; when associated
FT with A-123, A-187, M-189 and A-317."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 123
FT /note="S->A: No effect on basal resistance; when associated
FT with A-187 and A-317. No effect on basal resistance; when
FT associated with F-47, A-187, M-189 and A-317."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 187
FT /note="D->A: No effect on basal resistance; when associated
FT with A-123 and A-317. No effect on basal resistance; when
FT associated with F-47, A-123, M-189 and A-317."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 189
FT /note="V->M: No effect on basal resistance; when associated
FT with W-47, A-123, A-187 and A-317."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 254
FT /note="I->A: No effect on interactions with SAG101 or PAD4.
FT Loss of interaction with SAG101 but no effect on
FT homodimerization; when associated with A-258 and A-262, or
FT A-258; A-261 and A-262."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 258
FT /note="L->A: No effect on interactions with SAG101 or PAD4.
FT Strongly reduced interaction with SAG101; when associated
FT with A-262. Loss of interaction with SAG101 but no effect
FT on homodimerization; when associated with A-254 and A-262,
FT or A-254; A-261 and A-262."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 261
FT /note="F->A: No effect on interactions with SAG101 or PAD4.
FT Loss of interaction with SAG101 but no effect on
FT homodimerization; when associated with A-254; A-258 and A-
FT 262."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 262
FT /note="L->A: No effect on interactions with SAG101 or PAD4.
FT Strongly reduced interaction with SAG101; when associated
FT with A-258. Loss of interaction with SAG101 but no effect
FT on homodimerization; when associated with A-254 and A-258,
FT or A-254; A-258 and A-261."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 317
FT /note="H->A: No effect on basal resistance; when associated
FT with A-123 and A-187. No effect on basal resistance; when
FT associated with F-47, A-123, A-187 and M-189."
FT /evidence="ECO:0000269|PubMed:24331460"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 222..247
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 352..379
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 416..440
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 452..475
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 492..506
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 513..522
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 548..555
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 560..563
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 564..579
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 585..589
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 594..600
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 604..608
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:4NFU"
SQ SEQUENCE 623 AA; 71572 MW; 661941E27A3E9FAD CRC64;
MAFEALTGIN GDLITRSWSA SKQAYLTERY HKEEAGAVVI FAFQPSFSEK DFFDPDNKSS
FGEIKLNRVQ FPCMRKIGKG DVATVNEAFL KNLEAVIDPR TSFQASVEMA VRSRKQIVFT
GHSSGGATAI LATVWYLEKY FIRNPNVYLE PRCVTFGAPL VGDSIFSHAL GREKWSRFFV
NFVTRFDIVP RITLARKASV EETLPHVLAQ LDPRNSSVQE SEQRITEFYT SVMRDTSTVA
NQAVCELTGS AEAILETLSS FLELSPYRPA GTFVFSTEKR LVAVNNSDAI LQMLFYTCQA
SDEQEWSLIP FRSIRDHHSY EELVQSMGMK LFNHLDGENS IESSLNDLGV STRGRQYVQA
ALEEEKKRVE NQKKIIQVIQ QERFLKKLAW IEDEYKPKCQ AHKNGYYDSF KVSNEENDFK
ANVKRAELAG VFDEVLGLLK KCQLPDEFEG DIDWIKLATR YRRLVEPLDI ANYHRHLKNE
DTGPYMKRGR PTRYIYAQRG YEHHILKPNG MIAEDVFWNK VNGLNLGLQL EEIQETLKNS
GSECGSCFWA EVEELKGKPY EEVEVRVKTL EGMLREWITA GEVDEKEIFL EGSTFRKWWI
TLPKNHKSHS PLRDYMMDEI TDT
