RPS4_ARATH
ID RPS4_ARATH Reviewed; 1217 AA.
AC Q9XGM3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Disease resistance protein RPS4 {ECO:0000303|PubMed:10571887};
DE AltName: Full=Probable NAD(+) hydrolase RPS4;
DE EC=3.2.2.6 {ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
DE AltName: Full=Resistance to Pseudomonas syringae 4 {ECO:0000303|PubMed:10571887};
DE AltName: Full=TIR-NBS-LRR class disease resistance protein {ECO:0000312|EMBL:AED95221.1};
GN Name=RPS4 {ECO:0000303|PubMed:10571887};
GN OrderedLocusNames=At5g45250 {ECO:0000312|Araport:AT5G45250};
GN ORFNames=K9E15.1 {ECO:0000312|EMBL:BAB10246.1};
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:CAB50708.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ALTERNATIVE SPLICING.
RC STRAIN=cv. Columbia;
RX PubMed=10571887; DOI=10.1046/j.1365-313x.1999.t01-1-00600.x;
RA Gassmann W., Hinsch M.E., Staskawicz B.J.;
RT "The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-
RT LRR family of disease-resistance genes.";
RL Plant J. 20:265-277(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15469494; DOI=10.1111/j.1365-313x.2004.02213.x;
RA Kwon S.I., Koczan J.M., Gassmann W.;
RT "Two Arabidopsis srfr (suppressor of rps4-RLD) mutants exhibit avrRps4-
RT specific disease resistance independent of RPS4.";
RL Plant J. 40:366-375(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1172-LYS-LYS-1173 AND
RP 1184-LYS-LYS-1185.
RX PubMed=17997306; DOI=10.1016/j.cub.2007.10.042;
RA Wirthmueller L., Zhang Y., Jones J.D., Parker J.E.;
RT "Nuclear accumulation of the Arabidopsis immune receptor RPS4 is necessary
RT for triggering EDS1-dependent defense.";
RL Curr. Biol. 17:2023-2029(2007).
RN [6]
RP ALTERNATIVE SPLICING, AND INDUCTION BY AVRRPS4.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=17951452; DOI=10.1104/pp.107.108720;
RA Zhang X.C., Gassmann W.;
RT "Alternative splicing and mRNA levels of the disease resistance gene RPS4
RT are induced during defense responses.";
RL Plant Physiol. 145:1577-1587(2007).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia, cv. RLD, and cv. Wassilewskija;
RX PubMed=19519800; DOI=10.1111/j.1365-313x.2009.03949.x;
RA Narusaka M., Shirasu K., Noutoshi Y., Kubo Y., Shiraishi T., Iwabuchi M.,
RA Narusaka Y.;
RT "RRS1 and RPS4 provide a dual Resistance-gene system against fungal and
RT bacterial pathogens.";
RL Plant J. 60:218-226(2009).
RN [8]
RP DOMAIN, AND MUTAGENESIS OF ASP-26; ARG-28; 49-ASP--ASP-53; ARG-54; SER-68;
RP TYR-79; TRP-84; CYS-85; GLU-88; ASP-94; CYS-95; 97-ASP-GLU-98; GLU-111;
RP PRO-112; 113-SER-THR-114; ARG-116; 129-MET-ALA-130; 133-ASP-GLU-134;
RP ARG-135; 136-LYS--LYS-138; TRP-139; LYS-140 AND GLU-160.
RX PubMed=19132868; DOI=10.1094/mpmi-22-2-0157;
RA Swiderski M.R., Birker D., Jones J.D.;
RT "The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain
RT involved in cell death induction.";
RL Mol. Plant Microbe Interact. 22:157-165(2009).
RN [9]
RP INTERACTION WITH SRFR1, AND SUBCELLULAR LOCATION.
RX PubMed=21079790; DOI=10.1371/journal.ppat.1001172;
RA Kim S.H., Gao F., Bhattacharjee S., Adiasor J.A., Nam J.C., Gassmann W.;
RT "The Arabidopsis resistance-like gene SNC1 is activated by mutations in
RT SRFR1 and contributes to resistance to the bacterial effector AvrRps4.";
RL PLoS Pathog. 6:E1001172-E1001172(2010).
RN [10]
RP INTERACTION WITH EDS1, 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 [11]
RP INTERACTION WITH EDS1.
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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22454454; DOI=10.1105/tpc.112.096198;
RA Mang H.G., Qian W., Zhu Y., Qian J., Kang H.G., Klessig D.F., Hua J.;
RT "Abscisic acid deficiency antagonizes high-temperature inhibition of
RT disease resistance through enhancing nuclear accumulation of resistance
RT proteins SNC1 and RPS4 in Arabidopsis.";
RL Plant Cell 24:1271-1284(2012).
RN [13]
RP MISCELLANEOUS.
RX PubMed=22248079; DOI=10.1111/j.1365-313x.2012.04906.x;
RA Xu F., Xu S., Wiermer M., Zhang Y., Li X.;
RT "The cyclin L homolog MOS12 and the MOS4-associated complex are required
RT for the proper splicing of plant resistance genes.";
RL Plant J. 70:916-928(2012).
RN [14]
RP FUNCTION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=24146667; DOI=10.3389/fpls.2013.00403;
RA Heidrich K., Tsuda K., Blanvillain-Baufume S., Wirthmueller L., Bautor J.,
RA Parker J.E.;
RT "Arabidopsis TNL-WRKY domain receptor RRS1 contributes to temperature-
RT conditioned RPS4 auto-immunity.";
RL Front. Plant Sci. 4:403-403(2013).
RN [15]
RP REVIEW.
RX PubMed=25506347; DOI=10.3389/fpls.2014.00606;
RA Cesari S., Bernoux M., Moncuquet P., Kroj T., Dodds P.N.;
RT "A novel conserved mechanism for plant NLR protein pairs: the 'integrated
RT decoy' hypothesis.";
RL Front. Plant Sci. 5:606-606(2014).
RN [16]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
RN [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439793; DOI=10.1126/science.aax1771;
RA Wan L., Essuman K., Anderson R.G., Sasaki Y., Monteiro F., Chung E.H.,
RA Osborne Nishimura E., DiAntonio A., Milbrandt J., Dangl J.L.,
RA Nishimura M.T.;
RT "TIR domains of plant immune receptors are NAD+-cleaving enzymes that
RT promote cell death.";
RL Science 365:799-803(2019).
RN [18]
RP CRYSTALLIZATION OF 11-178.
RX PubMed=24192368; DOI=10.1107/s1744309113026614;
RA Wan L., Zhang X., Williams S.J., Ve T., Bernoux M., Sohn K.H., Jones J.D.,
RA Dodds P.N., Kobe B.;
RT "Crystallization and preliminary X-ray diffraction analyses of the TIR
RT domains of three TIR-NB-LRR proteins that are involved in disease
RT resistance in Arabidopsis thaliana.";
RL Acta Crystallogr. F 69:1275-1280(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 11-178 IN COMPLEX WITH RRS1,
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF ARG-30; SER-33; HIS-34 AND LYS-242.
RC STRAIN=cv. Columbia;
RX PubMed=24744375; DOI=10.1126/science.1247357;
RA Williams S.J., Sohn K.H., Wan L., Bernoux M., Sarris P.F., Segonzac C.,
RA Ve T., Ma Y., Saucet S.B., Ericsson D.J., Casey L.W., Lonhienne T.,
RA Winzor D.J., Zhang X., Coerdt A., Parker J.E., Dodds P.N., Kobe B.,
RA Jones J.D.;
RT "Structural basis for assembly and function of a heterodimeric plant immune
RT receptor.";
RL Science 344:299-303(2014).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the AvrRps4 type III effector avirulence protein from P.syringae
CC (PubMed:10571887, PubMed:15469494, PubMed:19519800). Resistance
CC proteins guard the plant against pathogens that contain an appropriate
CC avirulence protein via an indirect interaction with this avirulence
CC protein (PubMed:10571887, PubMed:15469494, PubMed:19519800). That
CC triggers a defense system including the hypersensitive response, which
CC restricts the pathogen growth (PubMed:10571887, PubMed:15469494,
CC PubMed:19519800). Probably acts as a NAD(+) hydrolase (NADase): in
CC response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose
CC (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system
CC that promotes cell death (PubMed:31439792, PubMed:31439793). The
CC combined presence of both regular and alternative RPS4 transcripts with
CC truncated open reading frames (ORFs) is necessary for function
CC (PubMed:17951452). RPS4 function is regulated at multiple levels,
CC including gene expression, alternative splicing, and protein stability
CC (PubMed:17951452). When over-expressed, confers temperature-conditioned
CC EDS1-dependent auto-immunity (PubMed:24146667). Heterodimerization with
CC RRS1 is required to form a functional complex to recognize AvrRps4 and
CC PopP2 (PubMed:24744375). Abscisic acid deficiency enhances nuclear
CC accumulation of RPS4 and its cell death-inducing activity
CC (PubMed:22454454). {ECO:0000269|PubMed:10571887,
CC ECO:0000269|PubMed:15469494, ECO:0000269|PubMed:17951452,
CC ECO:0000269|PubMed:19519800, ECO:0000269|PubMed:22454454,
CC ECO:0000269|PubMed:24146667, ECO:0000269|PubMed:24744375,
CC ECO:0000269|PubMed:31439792, ECO:0000269|PubMed:31439793,
CC ECO:0000305|PubMed:17951452, ECO:0000305|PubMed:19519800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
CC -!- SUBUNIT: Interacts with EDS1 (PubMed:22158818, PubMed:22158819).
CC Interacts with SRFR1 (PubMed:21079790). Interacts with RRS1
CC (PubMed:24744375). {ECO:0000269|PubMed:21079790,
CC ECO:0000269|PubMed:22158818, ECO:0000269|PubMed:22158819,
CC ECO:0000269|PubMed:24744375}.
CC -!- INTERACTION:
CC Q9XGM3; Q9XGM3: RPS4; NbExp=6; IntAct=EBI-16102886, EBI-16102886;
CC Q9XGM3; P0DKH5: RRS1; NbExp=18; IntAct=EBI-16102886, EBI-15211292;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:17997306}. Cytoplasm {ECO:0000269|PubMed:22158818}.
CC Nucleus {ECO:0000269|PubMed:17997306, ECO:0000269|PubMed:22158818,
CC ECO:0000269|PubMed:22454454}. Note=Nuclear accumulation is necessary
CC for triggering EDS1-dependent defense (PubMed:17997306). Found in
CC microsomes when interacting with SRFR1 (PubMed:21079790). Accumulates
CC in the cytoplasm and the nucleus, when associated with EDS1
CC (PubMed:22158818). Accumulates in nucleus at 22 degrees Celsius, but
CC not at 28 degrees Celsius (PubMed:22454454).
CC {ECO:0000269|PubMed:17997306, ECO:0000269|PubMed:21079790,
CC ECO:0000269|PubMed:22158818, ECO:0000269|PubMed:22454454}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.
CC {ECO:0000269|PubMed:10571887, ECO:0000269|PubMed:17951452};
CC Name=1;
CC IsoId=Q9XGM3-1; Sequence=Displayed;
CC -!- INDUCTION: Up-regulated by AvrRps4 in an EDS1-dependent manner.
CC {ECO:0000269|PubMed:17951452}.
CC -!- DOMAIN: The TIR domain is a signaling domain involved in cell death
CC induction (PubMed:19132868). It is involved in homo- and
CC heterodimerization, but other domains also contribute to the
CC interaction (PubMed:24744375). The LRR domain may interact directly
CC with pathogen-derived elicitors (PubMed:10571887).
CC {ECO:0000269|PubMed:19132868, ECO:0000269|PubMed:24744375,
CC ECO:0000305|PubMed:10571887}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- DISRUPTION PHENOTYPE: Loss of resistance to P.syringae expressing
CC AvrRps4. {ECO:0000269|PubMed:15469494}.
CC -!- MISCELLANEOUS: MOS12 and the MOS4-associated complex (MAC) are required
CC for the proper splicing of R genes and contribute in the alternative
CC splicing of RPS4. {ECO:0000269|PubMed:22248079}.
CC -!- MISCELLANEOUS: Only two amino-acid changes (N195D and Y950H) are linked
CC to a change from a resistant strain (cv. Columbia or cv. Landsberg
CC erecta) to a susceptible one (cv. RLD). {ECO:0000269|PubMed:10571887}.
CC -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative genomics
CC of disease resistance gene homologs;
CC URL="http://niblrrs.ucdavis.edu";
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DR EMBL; AJ243468; CAB50708.1; -; Genomic_DNA.
DR EMBL; AB020744; BAB10246.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95221.1; -; Genomic_DNA.
DR PIR; T51140; T51140.
DR RefSeq; NP_199338.1; NM_123893.2. [Q9XGM3-1]
DR PDB; 4C6R; X-ray; 2.05 A; A/B/C/D=11-178.
DR PDB; 4C6T; X-ray; 2.65 A; B/D=11-178.
DR PDBsum; 4C6R; -.
DR PDBsum; 4C6T; -.
DR AlphaFoldDB; Q9XGM3; -.
DR SMR; Q9XGM3; -.
DR BioGRID; 19810; 2.
DR DIP; DIP-61677N; -.
DR IntAct; Q9XGM3; 3.
DR STRING; 3702.AT5G45250.1; -.
DR iPTMnet; Q9XGM3; -.
DR PaxDb; Q9XGM3; -.
DR PRIDE; Q9XGM3; -.
DR ProteomicsDB; 226512; -. [Q9XGM3-1]
DR EnsemblPlants; AT5G45250.1; AT5G45250.1; AT5G45250. [Q9XGM3-1]
DR GeneID; 834561; -.
DR Gramene; AT5G45250.1; AT5G45250.1; AT5G45250. [Q9XGM3-1]
DR KEGG; ath:AT5G45250; -.
DR Araport; AT5G45250; -.
DR TAIR; locus:2158475; AT5G45250.
DR eggNOG; ENOG502SI7S; Eukaryota.
DR HOGENOM; CLU_001561_0_3_1; -.
DR OMA; HERKVLV; -.
DR OrthoDB; 992188at2759; -.
DR PhylomeDB; Q9XGM3; -.
DR PRO; PR:Q9XGM3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XGM3; baseline and differential.
DR Genevisible; Q9XGM3; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IDA:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11017; PTHR11017; 1.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Hydrolase;
KW Leucine-rich repeat; Membrane; NAD; Nucleotide-binding; Nucleus;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1217
FT /note="Disease resistance protein RPS4"
FT /id="PRO_0000431365"
FT DOMAIN 14..175
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 211..472
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 581..606
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 614..636
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 637..659
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 682..706
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 708..728
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 729..749
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 750..774
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 796..818
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 819..842
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 843..860
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 861..887
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REGION 33..34
FT /note="Important for interaction with RRS1"
FT /evidence="ECO:0000269|PubMed:24744375"
FT REGION 1161..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1170..1177
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT ACT_SITE 88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 23..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT MUTAGEN 26
FT /note="D->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 28
FT /note="R->E: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 30
FT /note="R->A: Increased homodimerization and stronger cell
FT death induction."
FT /evidence="ECO:0000269|PubMed:24744375"
FT MUTAGEN 33
FT /note="S->A: Loss of TIR domain homodimerization. Loss of
FT TIR domain heterodimerization; when associated with A-25 in
FT RRS1. Loss of cell death induction."
FT /evidence="ECO:0000269|PubMed:24744375"
FT MUTAGEN 34
FT /note="H->A: Loss of TIR domain homodimerization. Loss of
FT TIR domain heterodimerization with RRS1. Loss of cell death
FT induction."
FT /evidence="ECO:0000269|PubMed:24744375"
FT MUTAGEN 49..50
FT /note="DD->AA: Decreased cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 49
FT /note="D->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 50..53
FT /note="DYED->NYQN: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 54
FT /note="R->N: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 68
FT /note="S->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 79
FT /note="Y->A,F: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 84
FT /note="W->A: Increased cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 85
FT /note="C->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 88
FT /note="E->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 94
FT /note="D->N: No effect on cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 95
FT /note="C->A: No effect on cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 97..98
FT /note="DE->KK: No effect on cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 97..98
FT /note="DE->QN: Increased cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 111
FT /note="E->K: Increased cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 112
FT /note="P->A,K: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 113..114
FT /note="ST->EE: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 116
FT /note="R->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 129..130
FT /note="Missing: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 133..134
FT /note="DE->NQ: Increased cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 134
FT /note="E->A,K: Increased cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 135
FT /note="R->E: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 136..138
FT /note="Missing: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 137
FT /note="K->E: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 139
FT /note="W->A,F: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 140
FT /note="K->N: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 160
FT /note="E->A: Loss of cell death."
FT /evidence="ECO:0000269|PubMed:19132868"
FT MUTAGEN 242
FT /note="K->A: Loss of pathogen effectors recognition."
FT /evidence="ECO:0000269|PubMed:24744375"
FT MUTAGEN 1172..1173
FT /note="KK->AA: Loss of nuclear localization; when
FT associated with 1172-A-A-1173."
FT /evidence="ECO:0000269|PubMed:17997306"
FT MUTAGEN 1184..1185
FT /note="KK->AA: Loss of nuclear localization; when
FT associated with 1184-A-A-1185."
FT /evidence="ECO:0000269|PubMed:17997306"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4C6R"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:4C6R"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:4C6R"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:4C6R"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4C6R"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4C6R"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:4C6R"
SQ SEQUENCE 1217 AA; 137726 MW; B69B959ADA976E25 CRC64;
METSSISTVE DKPPQHQVFI NFRGADLRRR FVSHLVTALK LNNINVFIDD YEDRGQPLDV
LLKRIEESKI VLAIFSGNYT ESVWCVRELE KIKDCTDEGT LVAIPIFYKL EPSTVRDLKG
KFGDRFRSMA KGDERKKKWK EAFNLIPNIM GIIIDKKSVE SEKVNEIVKA VKTALTGIPP
EGSHNAVVGA LGNSNAGTSS GDKKHETFGN EQRLKDLEEK LDRDKYKGTR IIGVVGMPGI
GKTTLLKELY KTWQGKFSRH ALIDQIRVKS KHLELDRLPQ MLLGELSKLN HPHVDNLKDP
YSQLHERKVL VVLDDVSKRE QIDALREILD WIKEGKEGSR VVIATSDMSL TNGLVDDTYM
VQNLNHRDSL QLFHYHAFID DQANPQKKDF MKLSEGFVHY ARGHPLALKV LGGELNKKSM
DHWNSKMKKL AQSPSPNIVS VFQVSYDELT TAQKDAFLDI ACFRSQDKDY VESLLASSDL
GSAEAMSAVK SLTDKFLINT CDGRVEMHDL LYKFSREVDL KASNQDGSRQ RRLWLHQHII
KGGIINVLQN KMKAANVRGI FLDLSEVEDE TSLDRDHFIN MGNLRYLKFY NSHCPQECKT
NNKINIPDKL KLPLKEVRCL HWLKFPLETL PNDFNPINLV DLKLPYSEME QLWEGDKDTP
CLRWVDLNHS SKLCSLSGLS KAEKLQRLNL EGCTTLKAFP HDMKKMKMLA FLNLKGCTSL
ESLPEMNLIS LKTLTLSGCS TFKEFPLISD NIETLYLDGT AISQLPMNME KLQRLVVLNM
KDCKMLEEIP GRVGELKALQ ELILSDCLNL KIFPEIDISF LNILLLDGTA IEVMPQLPSV
QYLCLSRNAK ISCLPVGISQ LSQLKWLDLK YCTSLTSVPE FPPNLQCLDA HGCSSLKTVS
KPLARIMPTE QNHSTFIFTN CENLEQAAKE EITSYAQRKC QLLSYARKRY NGGLVSESLF
STCFPGCEVP SWFCHETVGS ELEVKLLPHW HDKKLAGIAL CAVVSCLDPQ DQVSRLSVTC
TFKVKDEDKS WVAYTCPVGS WTRHGGGKDK IELDHVFIGY TSCPHTIKCH EEGNSDECNP
TEASLKFTVT GGTSENGKYK VLKCGLSLVY AKDKDKNSAL ETKYDMLIGK SFQETSEGVD
GRVKKTKGKY VMPVEKNFQE TTEGVDGRVN KKKKTRMDNG RPKKKQRSGR DDNQTRMQVE
LQEGNINSVI MHTVKNF
