RPS2_ARATH
ID RPS2_ARATH Reviewed; 909 AA.
AC Q42484; O82096; Q8L3R0; Q8L3W3; Q8L4X9; Q8L4Y0; Q8L587; Q8L5B3; Q8LKZ8;
AC Q8LKZ9; Q8LL00; Q8LL01; Q9ASP5;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Disease resistance protein RPS2;
DE AltName: Full=Resistance to Pseudomonas syringae protein 2;
GN Name=RPS2; OrderedLocusNames=At4g26090; ORFNames=F20B18.200;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8091210; DOI=10.1126/science.8091210;
RA Bent A.F., Kunkel B.N., Dahlbeck D., Brown K.L., Schmidt R., Giraudat J.,
RA Leung J., Staskawicz B.J.;
RT "RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of plant disease
RT resistance genes.";
RL Science 265:1856-1860(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
RA Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
RT "The A. thaliana disease resistance gene RPS2 encodes a protein containing
RT a nucleotide-binding site and leucine-rich repeats.";
RL Cell 78:1089-1099(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=cv. Po-1;
RX PubMed=11333251; DOI=10.1093/genetics/158.1.439;
RA Banerjee D., Zhang X., Bent A.F.;
RT "The leucine-rich repeat domain can determine effective interaction between
RT RPS2 and other host factors in Arabidopsis RPS2-mediated disease
RT resistance.";
RL Genetics 158:439-450(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=cv. Ab-7, cv. Ang-0, cv. BG-4, cv. Bla-2, cv. Bur-0, cv. C2-1,
RC cv. Co-1, cv. Ct-1, cv. Cvi-0, cv. D2-9, cv. Fm-17, cv. G2-1, cv. Gott-20,
RC cv. Gr-6, cv. Hs-12, cv. Kas-1, cv. KNO-2, cv. Mt-0, cv. Po-1, cv. Pog-0,
RC cv. Pu-8, cv. RLD, cv. Tamm-17, cv. Tsu-0, cv. Wu-0, cv. Yo-0, and
RC cv. Zu-0;
RX PubMed=12618410; DOI=10.1093/genetics/163.2.735;
RA Mauricio R., Stahl E.A., Korves T., Tian D., Kreitman M., Bergelson J.;
RT "Natural selection for polymorphism in the disease resistance gene rps2 of
RT Arabidopsis thaliana.";
RL Genetics 163:735-746(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 184-352.
RC STRAIN=cv. Nd-1;
RX PubMed=9670562; DOI=10.1046/j.1365-313x.1998.00138.x;
RA Speulman E., Bouchez D., Holub E.B., Beynon J.L.;
RT "Disease resistance gene homologs correlate with disease resistance loci of
RT Arabidopsis thaliana.";
RL Plant J. 14:467-474(1998).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-353.
RX PubMed=8986840; DOI=10.1073/pnas.93.26.15497;
RA Leister R.T., Ausubel F.M., Katagiri F.;
RT "Molecular recognition of pathogen attack occurs inside of plant cells in
RT plant disease resistance specified by the Arabidopsis genes RPS2 and
RT RPM1.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15497-15502(1996).
RN [11]
RP IDENTIFICATION IN A COMPLEX CONTAINING AVRRPT2 AND AVRB.
RX PubMed=10849351; DOI=10.1046/j.1365-313x.2000.00744.x;
RA Leister R.T., Katagiri F.;
RT "A resistance gene product of the nucleotide binding site -- leucine rich
RT repeats class can form a complex with bacterial avirulence proteins in
RT vivo.";
RL Plant J. 22:345-354(2000).
RN [12]
RP MUTAGENESIS OF 7-LEU--ARG-25; 38-LEU--THR-40; LYS-188; THR-189; THR-190 AND
RP 262-GLU-GLU-263.
RX PubMed=11148296; DOI=10.2307/3871247;
RA Tao Y., Yuan F., Leister R.T., Ausubel F.M., Katagiri F.;
RT "Mutational analysis of the Arabidopsis nucleotide binding site-leucine-
RT rich repeat resistance gene RPS2.";
RL Plant Cell 12:2541-2554(2000).
RN [13]
RP MUTANTS 204C; 205C; 206C; 209C; 210C AND 211C.
RX PubMed=11204781; DOI=10.1094/mpmi.2001.14.2.181;
RA Axtell M.J., McNellis T.W., Mudgett M.B., Hsu C.S., Staskawicz B.J.;
RT "Mutational analysis of the Arabidopsis RPS2 disease resistance gene and
RT the corresponding pseudomonas syringae avrRpt2 avirulence gene.";
RL Mol. Plant Microbe Interact. 14:181-188(2001).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AVRRPT2 AND RIN4.
RX PubMed=12581526; DOI=10.1016/s0092-8674(03)00036-9;
RA Axtell M.J., Staskawicz B.J.;
RT "Initiation of RPS2-specified disease resistance in Arabidopsis is coupled
RT to the AvrRpt2-directed elimination of RIN4.";
RL Cell 112:369-377(2003).
RN [15]
RP FUNCTION.
RX PubMed=12581527; DOI=10.1016/s0092-8674(03)00040-0;
RA Mackey D., Belkhadir Y., Alonso J.M., Ecker J.R., Dangl J.L.;
RT "Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2
RT and modulates RPS2-mediated resistance.";
RL Cell 112:379-389(2003).
RN [16]
RP INTERACTION WITH NRP1, AND MUTAGENESIS OF GLY-182 AND THR-189.
RX DOI=10.1016/j.pmpp.2005.02.006;
RA Quirino B.F., Genger R., Ham J.H., Zabala G., Bent A.F.;
RT "Identification and functional analysis of Arabidopsis proteins that
RT interact with resistance gene product RPS2 in yeast.";
RL Physiol. Mol. Plant Pathol. 65:257-267(2004).
RN [17]
RP INTERACTION WITH MORC1/CRT1.
RX PubMed=18191794; DOI=10.1016/j.chom.2007.11.006;
RA Kang H.-G., Kuhl J.C., Kachroo P., Klessig D.F.;
RT "CRT1, an Arabidopsis ATPase that interacts with diverse resistance
RT proteins and modulates disease resistance to turnip crinkle virus.";
RL Cell Host Microbe 3:48-57(2008).
RN [18]
RP INTERACTION WITH TRAF1B.
RX PubMed=26867179; DOI=10.1016/j.chom.2016.01.005;
RA Huang S., Chen X., Zhong X., Li M., Ao K., Huang J., Li X.;
RT "Plant TRAF proteins regulate NLR immune receptor turnover.";
RL Cell Host Microbe 19:204-215(2016).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the AvrRpt2 type III effector avirulence protein from Pseudomonas
CC syringae. Resistance proteins guard the plant against pathogens that
CC contain an appropriate avirulence protein via an indirect interaction
CC with this avirulence protein. That triggers a defense system including
CC the hypersensitive response, which restricts the pathogen growth. Acts
CC via its interaction with RIN4, and probably triggers the plant
CC resistance when RIN4 is degraded by AvrRpt2.
CC {ECO:0000269|PubMed:12581527}.
CC -!- SUBUNIT: Interacts indirectly with RIN4. Found in a complex with
CC AvrRpt2 and AvrB (PubMed:10849351, PubMed:12581526). Interacts with
CC MORC1/CRT1 (PubMed:18191794). Binds to NRP1 (Ref.16). Interacts with
CC TRAF1B (PubMed:26867179). {ECO:0000269|PubMed:10849351,
CC ECO:0000269|PubMed:12581526, ECO:0000269|PubMed:18191794,
CC ECO:0000269|PubMed:26867179, ECO:0000269|Ref.16}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8986840}. Cell
CC membrane {ECO:0000269|PubMed:12581526}. Note=Not a peripheral membrane
CC protein. Has the biochemical properties of an integral membrane protein
CC without an obvious integral membrane primary structure.
CC {ECO:0000269|PubMed:12581526}.
CC -!- DOMAIN: The LRR repeats probably act as specificity determinant of
CC pathogen recognition. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domain is essential for the resistance to
CC AvrRpt2; the cultivars that do not display resistance showing specific
CC variations in this region.
CC -!- POLYMORPHISM: The polymorphism between the different cultivars
CC influence the specificity to the pathogen recognition. In cv. Po.1,
CC KNO2, BG-4 and Zu-0, RPS2 does not confer resistance to AvrRpt2.
CC {ECO:0000269|PubMed:11333251, ECO:0000269|PubMed:12618410}.
CC -!- SIMILARITY: Belongs to the disease resistance 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; U14158; AAA21874.1; -; Genomic_DNA.
DR EMBL; U12860; AAA50236.1; -; mRNA.
DR EMBL; AF368301; AAK38117.1; -; Genomic_DNA.
DR EMBL; AF487797; AAM90859.1; -; Genomic_DNA.
DR EMBL; AF487798; AAM90860.1; -; Genomic_DNA.
DR EMBL; AF487799; AAM90861.1; -; Genomic_DNA.
DR EMBL; AF487800; AAM90862.1; -; Genomic_DNA.
DR EMBL; AF487801; AAM90863.1; -; Genomic_DNA.
DR EMBL; AF487802; AAM90864.1; -; Genomic_DNA.
DR EMBL; AF487803; AAM90865.1; -; Genomic_DNA.
DR EMBL; AF487804; AAM90866.1; -; Genomic_DNA.
DR EMBL; AF487805; AAM90867.1; -; Genomic_DNA.
DR EMBL; AF487806; AAM90868.1; -; Genomic_DNA.
DR EMBL; AF487807; AAM90869.1; -; Genomic_DNA.
DR EMBL; AF487808; AAM90870.1; -; Genomic_DNA.
DR EMBL; AF487809; AAM90871.1; -; Genomic_DNA.
DR EMBL; AF487810; AAM90872.1; -; Genomic_DNA.
DR EMBL; AF487811; AAM90873.1; -; Genomic_DNA.
DR EMBL; AF487812; AAM90874.1; -; Genomic_DNA.
DR EMBL; AF487813; AAM90875.1; -; Genomic_DNA.
DR EMBL; AF487814; AAM90876.1; -; Genomic_DNA.
DR EMBL; AF487815; AAM90877.1; -; Genomic_DNA.
DR EMBL; AF487816; AAM90878.1; -; Genomic_DNA.
DR EMBL; AF487817; AAM90879.1; -; Genomic_DNA.
DR EMBL; AF487818; AAM90880.1; -; Genomic_DNA.
DR EMBL; AF487819; AAM90881.1; -; Genomic_DNA.
DR EMBL; AF487820; AAM90882.1; -; Genomic_DNA.
DR EMBL; AF487821; AAM90883.1; -; Genomic_DNA.
DR EMBL; AF487822; AAM90884.1; -; Genomic_DNA.
DR EMBL; AF487823; AAM90885.1; -; Genomic_DNA.
DR EMBL; AL049483; CAB39674.1; -; Genomic_DNA.
DR EMBL; AL161564; CAB79464.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85156.1; -; Genomic_DNA.
DR EMBL; AK117214; BAC41890.1; -; mRNA.
DR EMBL; BT005972; AAO64907.1; -; mRNA.
DR EMBL; U97217; AAC50025.1; -; Genomic_DNA.
DR PIR; A54809; A54809.
DR RefSeq; NP_194339.1; NM_118742.2.
DR AlphaFoldDB; Q42484; -.
DR SMR; Q42484; -.
DR BioGRID; 14002; 14.
DR DIP; DIP-53465N; -.
DR IntAct; Q42484; 11.
DR STRING; 3702.AT4G26090.1; -.
DR PaxDb; Q42484; -.
DR PRIDE; Q42484; -.
DR ProteomicsDB; 226542; -.
DR EnsemblPlants; AT4G26090.1; AT4G26090.1; AT4G26090.
DR GeneID; 828715; -.
DR Gramene; AT4G26090.1; AT4G26090.1; AT4G26090.
DR KEGG; ath:AT4G26090; -.
DR Araport; AT4G26090; -.
DR TAIR; locus:2005517; AT4G26090.
DR eggNOG; KOG4658; Eukaryota.
DR HOGENOM; CLU_000427_4_0_1; -.
DR InParanoid; Q42484; -.
DR OMA; LEEGEWK; -.
DR OrthoDB; 183010at2759; -.
DR PhylomeDB; Q42484; -.
DR PRO; PR:Q42484; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42484; differential.
DR Genevisible; Q42484; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0016045; P:detection of bacterium; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23155; PTHR23155; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Coiled coil; Cytoplasm;
KW Hypersensitive response; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..909
FT /note="Disease resistance protein RPS2"
FT /id="PRO_0000212718"
FT DOMAIN 135..440
FT /note="NB-ARC"
FT REPEAT 512..533
FT /note="LRR 1"
FT REPEAT 534..556
FT /note="LRR 2"
FT REPEAT 559..580
FT /note="LRR 3"
FT REPEAT 582..604
FT /note="LRR 4"
FT REPEAT 605..627
FT /note="LRR 5"
FT COILED 29..58
FT /evidence="ECO:0000255"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VARIANT 48
FT /note="I -> V (in strain: cv. Po-1 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 104
FT /note="Y -> C (in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv.
FT Wu-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 154
FT /note="S -> Y (in strain: cv. Pog-0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 419
FT /note="S -> P (in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv.
FT Wu-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 439
FT /note="H -> N (in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv.
FT Wu-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 472
FT /note="H -> Y (in strain: cv. BG-4, cv. KNO2, cv. Po-1 and
FT cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 515
FT /note="V -> A (in strain: cv. Yo-0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 515
FT /note="V -> L (in strain: cv. Ang-0, cv. Mt-0 and cv. RLD)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 527
FT /note="P -> H (in strain: cv. Ab-7, cv. Fm-17, cv. Gr-6 and
FT cv. Hs-12)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 544
FT /note="S -> R (in strain: cv. Wu-0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 545
FT /note="S -> Y (in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv.
FT Wu-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 644
FT /note="E -> G (in strain: cv. BG-4, KNO2, cv. Po-1, cv. Wu-
FT 0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 649
FT /note="G -> E (in strain: cv. Wu-0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 649
FT /note="G -> Q (in strain: cv. BG-4, cv. KNO2, cv. Po-1 and
FT cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 653
FT /note="A -> V (in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv.
FT Wu-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 699
FT /note="E -> D (in strain: cv. Yo-0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 703
FT /note="E -> D (in strain: cv. Ang-0, cv. BG-4, cv. Bur-0,
FT cv. Co-1, cv. Ct-1, cv. D2-9, cv. G2-1, cv. Kas-1, cv.
FT KNO2, cv. Mt-0, cv. Po-1, cv. Pog-0, cv. Pu-8, cv. RLD, cv.
FT Tamm-17, cv. Tsu-0, cv. Wu-0, cv. Yo-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT VARIANT 778
FT /note="N -> K (in strain: cv. D2-9, cv. G2-1 and cv. Tsu-
FT 0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 785
FT /note="L -> V (in strain: cv. Wu-0)"
FT /evidence="ECO:0000269|PubMed:12618410"
FT VARIANT 833
FT /note="R -> T (in strain: cv. BG-4, cv. Ct-1, cv. Cvi-0,
FT cv. D2-9, cv. G2-1, cv. Kas-1, cv. KNO2, cv. Po-1, cv. Pu-
FT 8, cv. Tsu-0, cv. Wu-0 and cv. Zu-0)"
FT /evidence="ECO:0000269|PubMed:11333251,
FT ECO:0000269|PubMed:12618410"
FT MUTAGEN 7..25
FT /note="Missing: In R2M1; abolishes disease resistance to
FT AvrRpt2. Induces dominant negative effect."
FT /evidence="ECO:0000269|PubMed:11148296"
FT MUTAGEN 38..40
FT /note="LET->TEL: In R2M2; abolishes disease resistance to
FT AvrRpt2. Induces dominant negative effect."
FT /evidence="ECO:0000269|PubMed:11148296"
FT MUTAGEN 182
FT /note="G->A: Reduced interaction with NRP1."
FT /evidence="ECO:0000269|Ref.16"
FT MUTAGEN 188
FT /note="K->L: In R2M4; abolishes disease resistance to
FT AvrRpt2. Does not display a dominant negative effect."
FT /evidence="ECO:0000269|PubMed:11148296"
FT MUTAGEN 189
FT /note="T->A: Reduced interaction with NRP1."
FT /evidence="ECO:0000269|Ref.16"
FT MUTAGEN 189
FT /note="T->S: In R2M4a; no effect. In R2M4c; abolishes
FT disease resistance to AvrRpt2; when associated with S-190.
FT Does not display a dominant negative effect."
FT /evidence="ECO:0000269|PubMed:11148296"
FT MUTAGEN 190
FT /note="T->S: In R2M4b; no effect. In R2M4c; abolishes
FT disease resistance to AvrRpt2; when associated with S-189.
FT Does not display a dominant negative effect."
FT /evidence="ECO:0000269|PubMed:11148296"
FT MUTAGEN 262..263
FT /note="DD->TA: In R2M5; abolishes disease resistance to
FT AvrRpt2. Does not display a dominant negative effect."
FT /evidence="ECO:0000269|PubMed:11148296"
FT MUTAGEN 276
FT /note="P->L: In 204C; abolishes disease resistance to
FT AvrRpt2."
FT MUTAGEN 353
FT /note="I->K: No effect."
FT /evidence="ECO:0000269|PubMed:8986840"
FT MUTAGEN 412
FT /note="A->V: In 205C; abolishes disease resistance to
FT AvrRpt2."
FT MUTAGEN 456
FT /note="A->T: In 209C; abolishes disease resistance to
FT AvrRpt2."
FT MUTAGEN 558
FT /note="P->L: In 210C; abolishes disease resistance to
FT AvrRpt2."
FT MUTAGEN 566
FT /note="S->L: In 206C; abolishes disease resistance to
FT AvrRpt2."
FT MUTAGEN 597
FT /note="P->S: In 211C; abolishes disease resistance to
FT AvrRpt2."
FT CONFLICT 195
FT /note="I -> V (in Ref. 9; AAC50025)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="E -> G (in Ref. 9; AAC50025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 909 AA; 104641 MW; D279B6E30E49D640 CRC64;
MDFISSLIVG CAQVLCESMN MAERRGHKTD LRQAITDLET AIGDLKAIRD DLTLRIQQDG
LEGRSCSNRA REWLSAVQVT ETKTALLLVR FRRREQRTRM RRRYLSCFGC ADYKLCKKVS
AILKSIGELR ERSEAIKTDG GSIQVTCREI PIKSVVGNTT MMEQVLEFLS EEEERGIIGV
YGPGGVGKTT LMQSINNELI TKGHQYDVLI WVQMSREFGE CTIQQAVGAR LGLSWDEKET
GENRALKIYR ALRQKRFLLL LDDVWEEIDL EKTGVPRPDR ENKCKVMFTT RSIALCNNMG
AEYKLRVEFL EKKHAWELFC SKVWRKDLLE SSSIRRLAEI IVSKCGGLPL ALITLGGAMA
HRETEEEWIH ASEVLTRFPA EMKGMNYVFA LLKFSYDNLE SDLLRSCFLY CALFPEEHSI
EIEQLVEYWV GEGFLTSSHG VNTIYKGYFL IGDLKAACLL ETGDEKTQVK MHNVVRSFAL
WMASEQGTYK ELILVEPSMG HTEAPKAENW RQALVISLLD NRIQTLPEKL ICPKLTTLML
QQNSSLKKIP TGFFMHMPVL RVLDLSFTSI TEIPLSIKYL VELYHLSMSG TKISVLPQEL
GNLRKLKHLD LQRTQFLQTI PRDAICWLSK LEVLNLYYSY AGWELQSFGE DEAEELGFAD
LEYLENLTTL GITVLSLETL KTLFEFGALH KHIQHLHVEE CNELLYFNLP SLTNHGRNLR
RLSIKSCHDL EYLVTPADFE NDWLPSLEVL TLHSLHNLTR VWGNSVSQDC LRNIRCINIS
HCNKLKNVSW VQKLPKLEVI ELFDCREIEE LISEHESPSV EDPTLFPSLK TLRTRDLPEL
NSILPSRFSF QKVETLVITN CPRVKKLPFQ ERRTQMNLPT VYCEEKWWKA LEKDQPNEEL
CYLPRFVPN
