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Disease resistance protein RPS2 (Resistance to Pseudomonas syringae protein 2)

 RPS2_ARATH              Reviewed;         909 AA.
Q42484; O82096; Q8L3R0; Q8L3W3; Q8L4X9; Q8L4Y0; Q8L587; Q8L5B3;
Q8LKZ8; Q8LKZ9; Q8LL00; Q8LL01; Q9ASP5;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 161.
RecName: Full=Disease resistance protein RPS2;
AltName: Full=Resistance to Pseudomonas syringae protein 2;
Name=RPS2; OrderedLocusNames=At4g26090; ORFNames=F20B18.200;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=8091210; DOI=10.1126/science.8091210;
Bent A.F., Kunkel B.N., Dahlbeck D., Brown K.L., Schmidt R.,
Giraudat J., Leung J., Staskawicz B.J.;
"RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of plant
disease resistance genes.";
Science 265:1856-1860(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
"The A. thaliana disease resistance gene RPS2 encodes a protein
containing a nucleotide-binding site and leucine-rich repeats.";
Cell 78:1089-1099(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
STRAIN=cv. Po-1;
PubMed=11333251;
Banerjee D., Zhang X., Bent A.F.;
"The leucine-rich repeat domain can determine effective interaction
between RPS2 and other host factors in Arabidopsis RPS2-mediated
disease resistance.";
Genetics 158:439-450(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
STRAIN=cv. Ab-7, cv. Ang-0, cv. BG-4, cv. Bla-2, cv. Bur-0, cv. C2-1,
cv. Co-1, cv. Ct-1, cv. Cvi-0, cv. D2-9, cv. Fm-17, cv. G2-1,
cv. Gott-20, cv. Gr-6, cv. Hs-12, cv. Kas-1, cv. KNO-2, cv. Mt-0,
cv. Po-1, cv. Pog-0, cv. Pu-8, cv. RLD, cv. Tamm-17, cv. Tsu-0,
cv. Wu-0, cv. Yo-0, and cv. Zu-0;
PubMed=12618410;
Mauricio R., Stahl E.A., Korves T., Tian D., Kreitman M.,
Bergelson J.;
"Natural selection for polymorphism in the disease resistance gene
rps2 of Arabidopsis thaliana.";
Genetics 163:735-746(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[6]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 184-352.
STRAIN=cv. Nd-1;
PubMed=9670562; DOI=10.1046/j.1365-313X.1998.00138.x;
Speulman E., Bouchez D., Holub E.B., Beynon J.L.;
"Disease resistance gene homologs correlate with disease resistance
loci of Arabidopsis thaliana.";
Plant J. 14:467-474(1998).
[10]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-353.
PubMed=8986840; DOI=10.1073/pnas.93.26.15497;
Leister R.T., Ausubel F.M., Katagiri F.;
"Molecular recognition of pathogen attack occurs inside of plant cells
in plant disease resistance specified by the Arabidopsis genes RPS2
and RPM1.";
Proc. Natl. Acad. Sci. U.S.A. 93:15497-15502(1996).
[11]
IDENTIFICATION IN A COMPLEX CONTAINING AVRRPT2 AND AVRB.
PubMed=10849351; DOI=10.1046/j.1365-313x.2000.00744.x;
Leister R.T., Katagiri F.;
"A resistance gene product of the nucleotide binding site -- leucine
rich repeats class can form a complex with bacterial avirulence
proteins in vivo.";
Plant J. 22:345-354(2000).
[12]
MUTAGENESIS OF 7-LEU--ARG-25; 38-LEU--THR-40; LYS-188; THR-189;
THR-190 AND 262-GLU-GLU-263.
PubMed=11148296; DOI=10.1105/tpc.12.12.2541;
Tao Y., Yuan F., Leister R.T., Ausubel F.M., Katagiri F.;
"Mutational analysis of the Arabidopsis nucleotide binding site-
leucine-rich repeat resistance gene RPS2.";
Plant Cell 12:2541-2554(2000).
[13]
MUTANTS 204C; 205C; 206C; 209C; 210C AND 211C.
PubMed=11204781; DOI=10.1094/MPMI.2001.14.2.181;
Axtell M.J., McNellis T.W., Mudgett M.B., Hsu C.S., Staskawicz B.J.;
"Mutational analysis of the Arabidopsis RPS2 disease resistance gene
and the corresponding pseudomonas syringae avrRpt2 avirulence gene.";
Mol. Plant Microbe Interact. 14:181-188(2001).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH AVRRPT2 AND RIN4.
PubMed=12581526; DOI=10.1016/S0092-8674(03)00036-9;
Axtell M.J., Staskawicz B.J.;
"Initiation of RPS2-specified disease resistance in Arabidopsis is
coupled to the AvrRpt2-directed elimination of RIN4.";
Cell 112:369-377(2003).
[15]
FUNCTION.
PubMed=12581527; DOI=10.1016/S0092-8674(03)00040-0;
Mackey D., Belkhadir Y., Alonso J.M., Ecker J.R., Dangl J.L.;
"Arabidopsis RIN4 is a target of the type III virulence effector
AvrRpt2 and modulates RPS2-mediated resistance.";
Cell 112:379-389(2003).
[16]
INTERACTION WITH NRP1, AND MUTAGENESIS OF GLY-182 AND THR-189.
DOI=10.1016/j.pmpp.2005.02.006;
Quirino B.F., Genger R., Ham J.H., Zabala G., Bent A.F.;
"Identification and functional analysis of Arabidopsis proteins that
interact with resistance gene product RPS2 in yeast.";
Physiol. Mol. Plant Pathol. 65:257-267(2004).
[17]
INTERACTION WITH MORC1/CRT1.
PubMed=18191794; DOI=10.1016/j.chom.2007.11.006;
Kang H.-G., Kuhl J.C., Kachroo P., Klessig D.F.;
"CRT1, an Arabidopsis ATPase that interacts with diverse resistance
proteins and modulates disease resistance to turnip crinkle virus.";
Cell Host Microbe 3:48-57(2008).
[18]
INTERACTION WITH TRAF1B.
PubMed=26867179; DOI=10.1016/j.chom.2016.01.005;
Huang S., Chen X., Zhong X., Li M., Ao K., Huang J., Li X.;
"Plant TRAF proteins regulate NLR immune receptor turnover.";
Cell Host Microbe 19:204-215(2016).
-!- FUNCTION: Disease resistance (R) protein that specifically
recognizes the AvrRpt2 type III effector avirulence protein from
Pseudomonas syringae. Resistance proteins guard the plant against
pathogens that contain an appropriate avirulence protein via an
indirect interaction with this avirulence protein. That triggers a
defense system including the hypersensitive response, which
restricts the pathogen growth. Acts via its interaction with RIN4,
and probably triggers the plant resistance when RIN4 is degraded
by AvrRpt2. {ECO:0000269|PubMed:12581527}.
-!- SUBUNIT: Interacts indirectly with RIN4. Found in a complex with
AvrRpt2 and AvrB (PubMed:10849351, PubMed:12581526). Interacts
with MORC1/CRT1 (PubMed:18191794). Binds to NRP1 (Ref.16).
Interacts with TRAF1B (PubMed:26867179).
{ECO:0000269|PubMed:10849351, ECO:0000269|PubMed:12581526,
ECO:0000269|PubMed:18191794, ECO:0000269|PubMed:26867179,
ECO:0000269|Ref.16}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8986840}. Cell
membrane {ECO:0000269|PubMed:12581526}. Note=Not a peripheral
membrane protein. Has the biochemical properties of an integral
membrane protein without an obvious integral membrane primary
structure. {ECO:0000269|PubMed:12581526}.
-!- DOMAIN: The LRR repeats probably act as specificity determinant of
pathogen recognition. {ECO:0000250}.
-!- DOMAIN: The coiled coil domain is essential for the resistance to
AvrRpt2; the cultivars that do not display resistance showing
specific variations in this region.
-!- POLYMORPHISM: The polymorphism between the different cultivars
influence the specificity to the pathogen recognition. In cv.
Po.1, KNO2, BG-4 and Zu-0, RPS2 does not confer resistance to
AvrRpt2. {ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
-!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative
genomics of disease resistance gene homologs;
URL="http://niblrrs.ucdavis.edu";
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EMBL; U14158; AAA21874.1; -; Genomic_DNA.
EMBL; U12860; AAA50236.1; -; mRNA.
EMBL; AF368301; AAK38117.1; -; Genomic_DNA.
EMBL; AF487797; AAM90859.1; -; Genomic_DNA.
EMBL; AF487798; AAM90860.1; -; Genomic_DNA.
EMBL; AF487799; AAM90861.1; -; Genomic_DNA.
EMBL; AF487800; AAM90862.1; -; Genomic_DNA.
EMBL; AF487801; AAM90863.1; -; Genomic_DNA.
EMBL; AF487802; AAM90864.1; -; Genomic_DNA.
EMBL; AF487803; AAM90865.1; -; Genomic_DNA.
EMBL; AF487804; AAM90866.1; -; Genomic_DNA.
EMBL; AF487805; AAM90867.1; -; Genomic_DNA.
EMBL; AF487806; AAM90868.1; -; Genomic_DNA.
EMBL; AF487807; AAM90869.1; -; Genomic_DNA.
EMBL; AF487808; AAM90870.1; -; Genomic_DNA.
EMBL; AF487809; AAM90871.1; -; Genomic_DNA.
EMBL; AF487810; AAM90872.1; -; Genomic_DNA.
EMBL; AF487811; AAM90873.1; -; Genomic_DNA.
EMBL; AF487812; AAM90874.1; -; Genomic_DNA.
EMBL; AF487813; AAM90875.1; -; Genomic_DNA.
EMBL; AF487814; AAM90876.1; -; Genomic_DNA.
EMBL; AF487815; AAM90877.1; -; Genomic_DNA.
EMBL; AF487816; AAM90878.1; -; Genomic_DNA.
EMBL; AF487817; AAM90879.1; -; Genomic_DNA.
EMBL; AF487818; AAM90880.1; -; Genomic_DNA.
EMBL; AF487819; AAM90881.1; -; Genomic_DNA.
EMBL; AF487820; AAM90882.1; -; Genomic_DNA.
EMBL; AF487821; AAM90883.1; -; Genomic_DNA.
EMBL; AF487822; AAM90884.1; -; Genomic_DNA.
EMBL; AF487823; AAM90885.1; -; Genomic_DNA.
EMBL; AL049483; CAB39674.1; -; Genomic_DNA.
EMBL; AL161564; CAB79464.1; -; Genomic_DNA.
EMBL; CP002687; AEE85156.1; -; Genomic_DNA.
EMBL; AK117214; BAC41890.1; -; mRNA.
EMBL; BT005972; AAO64907.1; -; mRNA.
EMBL; U97217; AAC50025.1; -; Genomic_DNA.
PIR; A54809; A54809.
RefSeq; NP_194339.1; NM_118742.2.
UniGene; At.46720; -.
UniGene; At.69675; -.
UniGene; At.75226; -.
PDB; 2FT5; Model; -; A=135-477.
PDBsum; 2FT5; -.
ProteinModelPortal; Q42484; -.
SMR; Q42484; -.
BioGrid; 14002; 14.
DIP; DIP-53465N; -.
IntAct; Q42484; 11.
STRING; 3702.AT4G26090.1; -.
PaxDb; Q42484; -.
PRIDE; Q42484; -.
EnsemblPlants; AT4G26090.1; AT4G26090.1; AT4G26090.
GeneID; 828715; -.
Gramene; AT4G26090.1; AT4G26090.1; AT4G26090.
KEGG; ath:AT4G26090; -.
Araport; AT4G26090; -.
TAIR; locus:2005517; AT4G26090.
eggNOG; KOG4658; Eukaryota.
eggNOG; COG4886; LUCA.
InParanoid; Q42484; -.
KO; K13459; -.
OMA; HAWELFC; -.
OrthoDB; EOG093602JL; -.
PhylomeDB; Q42484; -.
PRO; PR:Q42484; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q42484; differential.
Genevisible; Q42484; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0043531; F:ADP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0016045; P:detection of bacterium; IMP:TAIR.
GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR002182; NB-ARC.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF13855; LRR_8; 1.
Pfam; PF00931; NB-ARC; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; Hypersensitive response;
Leucine-rich repeat; Membrane; Nucleotide-binding; Plant defense;
Reference proteome; Repeat.
CHAIN 1 909 Disease resistance protein RPS2.
/FTId=PRO_0000212718.
DOMAIN 135 440 NB-ARC.
REPEAT 512 533 LRR 1.
REPEAT 534 556 LRR 2.
REPEAT 559 580 LRR 3.
REPEAT 582 604 LRR 4.
REPEAT 605 627 LRR 5.
NP_BIND 182 189 ATP.
COILED 29 58 {ECO:0000255}.
VARIANT 48 48 I -> V (in strain: cv. Po-1 and cv. Zu-
0). {ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 104 104 Y -> C (in strain: cv. BG-4, cv. KNO2,
cv. Po-1, cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 154 154 S -> Y (in strain: cv. Pog-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 419 419 S -> P (in strain: cv. BG-4, cv. KNO2,
cv. Po-1, cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 439 439 H -> N (in strain: cv. BG-4, cv. KNO2,
cv. Po-1, cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 472 472 H -> Y (in strain: cv. BG-4, cv. KNO2,
cv. Po-1 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 515 515 V -> A (in strain: cv. Yo-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 515 515 V -> L (in strain: cv. Ang-0, cv. Mt-0
and cv. RLD).
{ECO:0000269|PubMed:12618410}.
VARIANT 527 527 P -> H (in strain: cv. Ab-7, cv. Fm-17,
cv. Gr-6 and cv. Hs-12).
{ECO:0000269|PubMed:12618410}.
VARIANT 544 544 S -> R (in strain: cv. Wu-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 545 545 S -> Y (in strain: cv. BG-4, cv. KNO2,
cv. Po-1, cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 644 644 E -> G (in strain: cv. BG-4, KNO2, cv.
Po-1, cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 649 649 G -> E (in strain: cv. Wu-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 649 649 G -> Q (in strain: cv. BG-4, cv. KNO2,
cv. Po-1 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 653 653 A -> V (in strain: cv. BG-4, cv. KNO2,
cv. Po-1, cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 699 699 E -> D (in strain: cv. Yo-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 703 703 E -> D (in strain: cv. Ang-0, cv. BG-4,
cv. Bur-0, cv. Co-1, cv. Ct-1, cv. D2-9,
cv. G2-1, cv. Kas-1, cv. KNO2, cv. Mt-0,
cv. Po-1, cv. Pog-0, cv. Pu-8, cv. RLD,
cv. Tamm-17, cv. Tsu-0, cv. Wu-0, cv. Yo-
0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
VARIANT 778 778 N -> K (in strain: cv. D2-9, cv. G2-1 and
cv. Tsu-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 785 785 L -> V (in strain: cv. Wu-0).
{ECO:0000269|PubMed:12618410}.
VARIANT 833 833 R -> T (in strain: cv. BG-4, cv. Ct-1,
cv. Cvi-0, cv. D2-9, cv. G2-1, cv. Kas-1,
cv. KNO2, cv. Po-1, cv. Pu-8, cv. Tsu-0,
cv. Wu-0 and cv. Zu-0).
{ECO:0000269|PubMed:11333251,
ECO:0000269|PubMed:12618410}.
MUTAGEN 7 25 Missing: In R2M1; abolishes disease
resistance to AvrRpt2. Induces dominant
negative effect.
{ECO:0000269|PubMed:11148296}.
MUTAGEN 38 40 LET->TEL: In R2M2; abolishes disease
resistance to AvrRpt2. Induces dominant
negative effect.
{ECO:0000269|PubMed:11148296}.
MUTAGEN 182 182 G->A: Reduced interaction with NRP1.
{ECO:0000269|Ref.16}.
MUTAGEN 188 188 K->L: In R2M4; abolishes disease
resistance to AvrRpt2. Does not display a
dominant negative effect.
{ECO:0000269|PubMed:11148296}.
MUTAGEN 189 189 T->A: Reduced interaction with NRP1.
{ECO:0000269|Ref.16}.
MUTAGEN 189 189 T->S: In R2M4a; no effect. In R2M4c;
abolishes disease resistance to AvrRpt2;
when associated with S-190. Does not
display a dominant negative effect.
{ECO:0000269|PubMed:11148296}.
MUTAGEN 190 190 T->S: In R2M4b; no effect. In R2M4c;
abolishes disease resistance to AvrRpt2;
when associated with S-189. Does not
display a dominant negative effect.
{ECO:0000269|PubMed:11148296}.
MUTAGEN 262 263 DD->TA: In R2M5; abolishes disease
resistance to AvrRpt2. Does not display a
dominant negative effect.
{ECO:0000269|PubMed:11148296}.
MUTAGEN 276 276 P->L: In 204C; abolishes disease
resistance to AvrRpt2.
MUTAGEN 353 353 I->K: No effect.
{ECO:0000269|PubMed:8986840}.
MUTAGEN 412 412 A->V: In 205C; abolishes disease
resistance to AvrRpt2.
MUTAGEN 456 456 A->T: In 209C; abolishes disease
resistance to AvrRpt2.
MUTAGEN 558 558 P->L: In 210C; abolishes disease
resistance to AvrRpt2.
MUTAGEN 566 566 S->L: In 206C; abolishes disease
resistance to AvrRpt2.
MUTAGEN 597 597 P->S: In 211C; abolishes disease
resistance to AvrRpt2.
CONFLICT 195 195 I -> V (in Ref. 9; AAC50025).
{ECO:0000305}.
CONFLICT 267 267 E -> G (in Ref. 9; AAC50025).
{ECO:0000305}.
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


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