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Protein

Disease resistance protein RPM1

Gene

RPM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Disease resistance (R) protein that specifically recognizes the AvrRpm1 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 phosphorylated by AvrRpm1. It is then degraded at the onset of the hypersensitive response.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi200 – 2078ATPSequence analysis

GO - Molecular functioni

  • ADP binding Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • nucleotide binding Source: TAIR

GO - Biological processi

  • plant-type hypersensitive response Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Hypersensitive response, Plant defense

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Disease resistance protein RPM1
Alternative name(s):
Resistance to Pseudomonas syringae protein 3
Gene namesi
Name:RPM1
Synonyms:RPS3
Ordered Locus Names:At3g07040
ORF Names:F17A9.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G07040.

Subcellular locationi

GO - Cellular componenti

  • endomembrane system Source: UniProtKB-SubCell
  • extrinsic component of plasma membrane Source: CACAO
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431S → F: Loss of function. 1 Publication
Mutagenesisi105 – 1051P → S: Loss of function. 1 Publication
Mutagenesisi174 – 1741G → R: Loss of function. 1 Publication
Mutagenesisi186 – 1861L → F: Loss of function. 1 Publication
Mutagenesisi203 – 2031G → D or S: Loss of function. 1 Publication
Mutagenesisi205 – 2051G → R or E: Loss of function. 1 Publication
Mutagenesisi211 – 2111A → V: Loss of function. 1 Publication
Mutagenesisi219 – 2191V → M: Loss of function. 1 Publication
Mutagenesisi247 – 2471E → K: Loss of function. 1 Publication
Mutagenesisi269 – 2691V → M: Loss of function. 1 Publication
Mutagenesisi272 – 2721L → F: Loss of function. 1 Publication
Mutagenesisi290 – 2901T → I: Loss of function. 1 Publication
Mutagenesisi301 – 3011L → F in rps3-2; loss of function. 1 Publication
Mutagenesisi307 – 3071G → E: Loss of function. 1 Publication
Mutagenesisi313 – 3131T → I: Loss of function. 1 Publication
Mutagenesisi325 – 3251G → E: Loss of function. 1 Publication
Mutagenesisi340 – 3401E → K: Loss of function. 1 Publication
Mutagenesisi341 – 3411A → V: Loss of function.
Mutagenesisi344 – 3441L → F: Loss of function. 1 Publication
Mutagenesisi379 – 3791A → V: Loss of function. 1 Publication
Mutagenesisi384 – 3841G → R: Loss of function. 1 Publication
Mutagenesisi395 – 3951E → K: Loss of function. 1 Publication
Mutagenesisi439 – 4391S → F: Loss of function. 1 Publication
Mutagenesisi442 – 4421P → L: Loss of function. 1 Publication
Mutagenesisi464 – 4641P → L: Loss of function. 1 Publication
Mutagenesisi467 – 4671G → R: Loss of function. 1 Publication
Mutagenesisi471 – 4711E → K: Loss of function. 1 Publication
Mutagenesisi474 – 4741A → T: Loss of function. 1 Publication
Mutagenesisi494 – 4941P → L: Loss of function. 1 Publication
Mutagenesisi497 – 4971R → Q: Loss of function. 1 Publication
Mutagenesisi498 – 4981P → L or S: Loss of function. 1 Publication
Mutagenesisi515 – 5151S → F: Loss of function. 1 Publication
Mutagenesisi620 – 6201P → S or L: Loss of function. 1 Publication
Mutagenesisi738 – 7381S → F: Loss of function. 1 Publication
Mutagenesisi766 – 7661G → E in rps3-4; loss of function. 1 Publication
Mutagenesisi778 – 7781L → F: Loss of function. 1 Publication
Mutagenesisi781 – 7811L → F: Loss of function. 1 Publication
Mutagenesisi787 – 7871R → H: Loss of function. 1 Publication
Mutagenesisi812 – 8121N → I: Loss of function. 1 Publication
Mutagenesisi852 – 8521L → F: Loss of function. 1 Publication
Mutagenesisi924 – 9241L → F: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 926926Disease resistance protein RPM1PRO_0000212717Add
BLAST

Proteomic databases

PaxDbiQ39214.
PRIDEiQ39214.

PTM databases

iPTMnetiQ39214.

Expressioni

Gene expression databases

GenevisibleiQ39214. AT.

Interactioni

Subunit structurei

Interacts directly with RIN4 via its N-terminal region. Interacts (via N-terminus) with RIN2 and RIN3 (via C-terminus). Interacts with TIP49A, a protein known to interact with the TATA binding protein complex (TBP) (PubMed:11955429, PubMed:12062092, PubMed:16212605). Binds to MORC1/CRT1 (PubMed:20332379).4 Publications

Protein-protein interaction databases

BioGridi5224. 7 interactions.
MINTiMINT-8060368.
STRINGi3702.AT3G07040.1.

Structurei

3D structure databases

ProteinModelPortaliQ39214.
SMRiQ39214. Positions 559-881.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 467315NB-ARCAdd
BLAST
Repeati560 – 58122LRR 1Add
BLAST
Repeati582 – 60322LRR 2Add
BLAST
Repeati605 – 62622LRR 3Add
BLAST
Repeati628 – 65023LRR 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 4536Leucine-zipperAdd
BLAST

Domaini

The LRR repeats probably act as specificity determinant of pathogen recognition.

Sequence similaritiesi

Belongs to the disease resistance NB-LRR family.Curated
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 NB-ARC domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4658. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000237754.
InParanoidiQ39214.
KOiK13457.
OMAiKEDEAWV.
PhylomeDBiQ39214.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR002182. NB-ARC.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00931. NB-ARC. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q39214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASATVDFGI GRILSVLENE TLLLSGVHGE IDKMKKELLI MKSFLEDTHK
60 70 80 90 100
HGGNGSTTTT TQLFQTFVAN TRDLAYQIED ILDEFGYHIH GYRSCAKIWR
110 120 130 140 150
AFHFPRYMWA RHSIAQKLGM VNVMIQSISD SMKRYYHSEN YQAALLPPID
160 170 180 190 200
DGDAKWVNNI SESSLFFSEN SLVGIDAPKG KLIGRLLSPE PQRIVVAVVG
210 220 230 240 250
MGGSGKTTLS ANIFKSQSVR RHFESYAWVT ISKSYVIEDV FRTMIKEFYK
260 270 280 290 300
EADTQIPAEL YSLGYRELVE KLVEYLQSKR YIVVLDDVWT TGLWREISIA
310 320 330 340 350
LPDGIYGSRV MMTTRDMNVA SFPYGIGSTK HEIELLKEDE AWVLFSNKAF
360 370 380 390 400
PASLEQCRTQ NLEPIARKLV ERCQGLPLAI ASLGSMMSTK KFESEWKKVY
410 420 430 440 450
STLNWELNNN HELKIVRSIM FLSFNDLPYP LKRCFLYCSL FPVNYRMKRK
460 470 480 490 500
RLIRMWMAQR FVEPIRGVKA EEVADSYLNE LVYRNMLQVI LWNPFGRPKA
510 520 530 540 550
FKMHDVIWEI ALSVSKLERF CDVYNDDSDG DDAAETMENY GSRHLCIQKE
560 570 580 590 600
MTPDSIRATN LHSLLVCSSA KHKMELLPSL NLLRALDLED SSISKLPDCL
610 620 630 640 650
VTMFNLKYLN LSKTQVKELP KNFHKLVNLE TLNTKHSKIE ELPLGMWKLK
660 670 680 690 700
KLRYLITFRR NEGHDSNWNY VLGTRVVPKI WQLKDLQVMD CFNAEDELIK
710 720 730 740 750
NLGCMTQLTR ISLVMVRREH GRDLCDSLNK IKRIRFLSLT SIDEEEPLEI
760 770 780 790 800
DDLIATASIE KLFLAGKLER VPSWFNTLQN LTYLGLRGSQ LQENAILSIQ
810 820 830 840 850
TLPRLVWLSF YNAYMGPRLR FAQGFQNLKI LEIVQMKHLT EVVIEDGAMF
860 870 880 890 900
ELQKLYVRAC RGLEYVPRGI ENLINLQELH LIHVSNQLVE RIRGEGSVDR
910 920
SRVKHIPAIK HYFRTDNGSF YVSLSS
Length:926
Mass (Da):106,883
Last modified:November 1, 1996 - v1
Checksum:iE2B2D6613CB0FA0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87851 Genomic DNA. Translation: CAA61131.1.
AC016827 Genomic DNA. Translation: AAF27008.1.
CP002686 Genomic DNA. Translation: AEE74492.1.
PIRiA57072.
RefSeqiNP_187360.1. NM_111584.2.
UniGeneiAt.40415.

Genome annotation databases

EnsemblPlantsiAT3G07040.1; AT3G07040.1; AT3G07040.
GeneIDi819889.
GrameneiAT3G07040.1; AT3G07040.1; AT3G07040.
KEGGiath:AT3G07040.

Cross-referencesi

Web resourcesi

NIB-LRRS

Functional and comparative genomics of disease resistance gene homologs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87851 Genomic DNA. Translation: CAA61131.1.
AC016827 Genomic DNA. Translation: AAF27008.1.
CP002686 Genomic DNA. Translation: AEE74492.1.
PIRiA57072.
RefSeqiNP_187360.1. NM_111584.2.
UniGeneiAt.40415.

3D structure databases

ProteinModelPortaliQ39214.
SMRiQ39214. Positions 559-881.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5224. 7 interactions.
MINTiMINT-8060368.
STRINGi3702.AT3G07040.1.

PTM databases

iPTMnetiQ39214.

Proteomic databases

PaxDbiQ39214.
PRIDEiQ39214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G07040.1; AT3G07040.1; AT3G07040.
GeneIDi819889.
GrameneiAT3G07040.1; AT3G07040.1; AT3G07040.
KEGGiath:AT3G07040.

Organism-specific databases

TAIRiAT3G07040.

Phylogenomic databases

eggNOGiKOG4658. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000237754.
InParanoidiQ39214.
KOiK13457.
OMAiKEDEAWV.
PhylomeDBiQ39214.

Miscellaneous databases

PROiQ39214.

Gene expression databases

GenevisibleiQ39214. AT.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR002182. NB-ARC.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00931. NB-ARC. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Arabidopsis RPM1 gene enabling dual specificity disease resistance."
    Grant M.R., Godiard L., Straube E., Ashfield T., Lewald J., Stattler A., Innes R.W., Dangl J.L.
    Science 269:843-846(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS RPS3-2 AND RPS3-4.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "The Arabidopsis thaliana RPM1 disease resistance gene product is a peripheral plasma membrane protein that is degraded coincident with the hypersensitive response."
    Boyes D.C., Nam J., Dangl J.L.
    Proc. Natl. Acad. Sci. U.S.A. 95:15849-15854(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEGRADATION.
  5. "Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein."
    Tornero P., Chao R.A., Luthin W.N., Goff S.A., Dangl J.L.
    Plant Cell 14:435-450(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-43; PRO-105; GLY-174; LEU-186; GLY-203; GLY-205; ALA-211; VAL-219; GLU-247; VAL-269; LEU-272; THR-290; LEU-301; GLY-307; THR-313; GLY-325; GLU-340; LEU-344; ALA-379; GLY-384; GLU-395; SER-439; PRO-442; PRO-464; GLY-467; GLU-471; ALA-474; PRO-494; ARG-497; PRO-498; SER-515; PRO-620; SER-738; GLY-766; LEU-778; LEU-781; ARG-787; ASN-812; LEU-852 AND LEU-924.
  6. "An evolutionarily conserved mediator of plant disease resistance gene function is required for normal Arabidopsis development."
    Holt B.F. III, Boyes D.C., Ellerstroem M., Siefers N., Wiig A., Kauffman S., Grant M.R., Dangl J.L.
    Dev. Cell 2:807-817(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIP49A.
  7. "RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis."
    Mackey D., Holt B.F. III, Wiig A., Dangl J.L.
    Cell 108:743-754(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIN4.
  8. "A duplicated pair of Arabidopsis RING-finger E3 ligases contribute to the RPM1- and RPS2-mediated hypersensitive response."
    Kawasaki T., Nam J., Boyes D.C., Holt B.F. III, Hubert D.A., Wiig A., Dangl J.L.
    Plant J. 44:258-270(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIN2 AND RIN3.
  9. "Endosome-associated CRT1 functions early in resistance gene-mediated defense signaling in Arabidopsis and tobacco."
    Kang H.-G., Oh C.-S., Sato M., Katagiri F., Glazebrook J., Takahashi H., Kachroo P., Martin G.B., Klessig D.F.
    Plant Cell 22:918-936(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MORC1/CRT1.

Entry informationi

Entry nameiRPM1_ARATH
AccessioniPrimary (citable) accession number: Q39214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.