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Protein

Disease resistance protein RPS4

Gene

RPS4

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 AvrRps4 type III effector avirulence protein from P.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. The combined presence of both regular and alternative RPS4 transcripts with truncated open reading frames (ORFs) is necessary for function (PubMed:17951452). RPS4 function is regulated at multiple levels, including gene expression, alternative splicing, and protein stability (PubMed:17951452). When over-expressed, confers temperature-conditioned EDS1-dependent auto-immunity (PubMed:24146667). Heterodimerization with RRS1 is required to form a functional complex to recognize AvrRps4 and PopP2 (PubMed:24744375). Abscisic acid deficiency enhances nuclear accumulation of RPS4 and its cell death-inducing activity (PubMed:22454454).2 Publications5 Publications

GO - Molecular functioni

  • ADP binding Source: InterPro
  • receptor activity Source: TAIR

GO - Biological processi

  • defense response signaling pathway, resistance gene-dependent Source: TAIR
  • defense response to bacterium Source: TAIR
  • plant-type hypersensitive response Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Disease resistance protein RPS41 Publication
Alternative name(s):
Resistance to Pseudomonas syringae 41 Publication
TIR-NBS-LRR class disease resistance proteinImported
Gene namesi
Name:RPS41 Publication
Ordered Locus Names:At5g45250Imported
ORF Names:K9E15.1Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G45250.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • endomembrane system Source: TAIR
  • membrane Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Loss of resistance to P.syringae expressing AvrRps4.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26D → A: Loss of cell death. 1 Publication1
Mutagenesisi28R → E: Loss of cell death. 1 Publication1
Mutagenesisi30R → A: Increased homodimerization and stronger cell death induction. 1 Publication1
Mutagenesisi33S → A: Loss of TIR domain homodimerization. Loss of TIR domain heterodimerization; when associated with A-25 in RRS1. Loss of cell death induction. 1 Publication1
Mutagenesisi34H → A: Loss of TIR domain homodimerization. Loss of TIR domain heterodimerization with RRS1. Loss of cell death induction. 1 Publication1
Mutagenesisi49 – 50DD → AA: Decreased cell death. 1 Publication2
Mutagenesisi49D → A: Loss of cell death. 1 Publication1
Mutagenesisi50 – 53DYED → NYQN: Loss of cell death. 1 Publication4
Mutagenesisi54R → N: Loss of cell death. 1 Publication1
Mutagenesisi68S → A: Loss of cell death. 1 Publication1
Mutagenesisi79Y → A or F: Loss of cell death. 1 Publication1
Mutagenesisi84W → A: Increased cell death. 1 Publication1
Mutagenesisi85C → A: Loss of cell death. 1 Publication1
Mutagenesisi88E → A: Loss of cell death. 1 Publication1
Mutagenesisi94D → N: No effect on cell death. 1 Publication1
Mutagenesisi95C → A: No effect on cell death. 1 Publication1
Mutagenesisi97 – 98DE → KK: No effect on cell death. 1 Publication2
Mutagenesisi97 – 98DE → QN: Increased cell death. 1 Publication2
Mutagenesisi111E → K: Increased cell death. 1 Publication1
Mutagenesisi112P → A or K: Loss of cell death. 1 Publication1
Mutagenesisi113 – 114ST → EE: Loss of cell death. 1 Publication2
Mutagenesisi116R → A: Loss of cell death. 1 Publication1
Mutagenesisi129 – 130Missing : Loss of cell death. 1 Publication2
Mutagenesisi133 – 134DE → NQ: Increased cell death. 1 Publication2
Mutagenesisi134E → A or K: Increased cell death. 1 Publication1
Mutagenesisi135R → E: Loss of cell death. 1 Publication1
Mutagenesisi136 – 138Missing : Loss of cell death. 1 Publication3
Mutagenesisi137K → E: Loss of cell death. 1 Publication1
Mutagenesisi139W → A or F: Loss of cell death. 1 Publication1
Mutagenesisi140K → N: Loss of cell death. 1 Publication1
Mutagenesisi160E → A: Loss of cell death. 1 Publication1
Mutagenesisi242K → A: Loss of pathogen effectors recognition. 1 Publication1
Mutagenesisi1172 – 1173KK → AA: Loss of nuclear localization; when associated with 1172-A-A-1173. 1 Publication2
Mutagenesisi1184 – 1185KK → AA: Loss of nuclear localization; when associated with 1184-A-A-1185. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004313651 – 1217Disease resistance protein RPS4Add BLAST1217

Proteomic databases

PaxDbiQ9XGM3.
PRIDEiQ9XGM3.

PTM databases

iPTMnetiQ9XGM3.

Expressioni

Inductioni

Up-regulated by AvrRps4 in an EDS1-dependent manner.1 Publication

Gene expression databases

GenevisibleiQ9XGM3. AT.

Interactioni

Subunit structurei

Interacts with EDS1 (PubMed:22158818, PubMed:22158819). Interacts with SRFR1 (PubMed:21079790). Interacts with RRS1 (PubMed:24744375).4 Publications

Protein-protein interaction databases

BioGridi19810. 2 interactors.
DIPiDIP-61677N.
STRINGi3702.AT5G45250.1.

Structurei

Secondary structure

11217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 21Combined sources5
Helixi25 – 29Combined sources5
Helixi31 – 41Combined sources11
Beta strandi46 – 48Combined sources3
Helixi58 – 67Combined sources10
Beta strandi69 – 75Combined sources7
Helixi79 – 81Combined sources3
Helixi83 – 98Combined sources16
Beta strandi100 – 110Combined sources11
Helixi112 – 116Combined sources5
Helixi120 – 129Combined sources10
Turni130 – 132Combined sources3
Helixi136 – 145Combined sources10
Helixi146 – 148Combined sources3
Beta strandi152 – 154Combined sources3
Helixi160 – 175Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C6RX-ray2.05A/B/C/D11-178[»]
4C6TX-ray2.65B/D11-178[»]
ProteinModelPortaliQ9XGM3.
SMRiQ9XGM3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 149TIRPROSITE-ProRule annotationAdd BLAST136
Domaini211 – 472NB-ARCSequence analysisAdd BLAST262
Repeati260 – 285LRR 1Sequence analysisAdd BLAST26
Repeati436 – 459LRR 2Sequence analysisAdd BLAST24
Repeati614 – 636LRR 3Sequence analysisAdd BLAST23
Repeati637 – 659LRR 4Sequence analysisAdd BLAST23
Repeati682 – 706LRR 5Sequence analysisAdd BLAST25
Repeati708 – 728LRR 6Sequence analysisAdd BLAST21
Repeati729 – 749LRR 7Sequence analysisAdd BLAST21
Repeati750 – 774LRR 8Sequence analysisAdd BLAST25
Repeati796 – 818LRR 9Sequence analysisAdd BLAST23
Repeati819 – 842LRR 10Sequence analysisAdd BLAST24
Repeati861 – 887LRR 11Sequence analysisAdd BLAST27

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 34Important for interaction with RRS11 Publication2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1170 – 1177Nuclear localization signalPROSITE-ProRule annotation8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1171 – 1174Poly-LysSequence analysis4

Domaini

The TIR domain is a signaling domain involved in cell death induction (PubMed:19132868). It is involved in homo- and heterodimerization, but other domains also contribute to the interaction (PubMed:24744375). The LRR domain may interact directly with pathogen-derived elicitors (PubMed:10571887).1 Publication2 Publications

Sequence similaritiesi

Contains 11 LRR (leucine-rich) repeats.Sequence analysis
Contains 1 NB-ARC domain.Sequence analysis
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiENOG410JS6A. Eukaryota.
COG4886. LUCA.
InParanoidiQ9XGM3.
KOiK16226.
OMAiHYHAFID.
OrthoDBiEOG093601ZB.
PhylomeDBiQ9XGM3.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.40.50.300. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR011713. Leu-rich_rpt_3.
IPR002182. NB-ARC.
IPR027417. P-loop_NTPase.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF07725. LRR_3. 1 hit.
PF00931. NB-ARC. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52200. SSF52200. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced.2 Publications
Isoform 1 (identifier: Q9XGM3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METSSISTVE DKPPQHQVFI NFRGADLRRR FVSHLVTALK LNNINVFIDD
60 70 80 90 100
YEDRGQPLDV LLKRIEESKI VLAIFSGNYT ESVWCVRELE KIKDCTDEGT
110 120 130 140 150
LVAIPIFYKL EPSTVRDLKG KFGDRFRSMA KGDERKKKWK EAFNLIPNIM
160 170 180 190 200
GIIIDKKSVE SEKVNEIVKA VKTALTGIPP EGSHNAVVGA LGNSNAGTSS
210 220 230 240 250
GDKKHETFGN EQRLKDLEEK LDRDKYKGTR IIGVVGMPGI GKTTLLKELY
260 270 280 290 300
KTWQGKFSRH ALIDQIRVKS KHLELDRLPQ MLLGELSKLN HPHVDNLKDP
310 320 330 340 350
YSQLHERKVL VVLDDVSKRE QIDALREILD WIKEGKEGSR VVIATSDMSL
360 370 380 390 400
TNGLVDDTYM VQNLNHRDSL QLFHYHAFID DQANPQKKDF MKLSEGFVHY
410 420 430 440 450
ARGHPLALKV LGGELNKKSM DHWNSKMKKL AQSPSPNIVS VFQVSYDELT
460 470 480 490 500
TAQKDAFLDI ACFRSQDKDY VESLLASSDL GSAEAMSAVK SLTDKFLINT
510 520 530 540 550
CDGRVEMHDL LYKFSREVDL KASNQDGSRQ RRLWLHQHII KGGIINVLQN
560 570 580 590 600
KMKAANVRGI FLDLSEVEDE TSLDRDHFIN MGNLRYLKFY NSHCPQECKT
610 620 630 640 650
NNKINIPDKL KLPLKEVRCL HWLKFPLETL PNDFNPINLV DLKLPYSEME
660 670 680 690 700
QLWEGDKDTP CLRWVDLNHS SKLCSLSGLS KAEKLQRLNL EGCTTLKAFP
710 720 730 740 750
HDMKKMKMLA FLNLKGCTSL ESLPEMNLIS LKTLTLSGCS TFKEFPLISD
760 770 780 790 800
NIETLYLDGT AISQLPMNME KLQRLVVLNM KDCKMLEEIP GRVGELKALQ
810 820 830 840 850
ELILSDCLNL KIFPEIDISF LNILLLDGTA IEVMPQLPSV QYLCLSRNAK
860 870 880 890 900
ISCLPVGISQ LSQLKWLDLK YCTSLTSVPE FPPNLQCLDA HGCSSLKTVS
910 920 930 940 950
KPLARIMPTE QNHSTFIFTN CENLEQAAKE EITSYAQRKC QLLSYARKRY
960 970 980 990 1000
NGGLVSESLF STCFPGCEVP SWFCHETVGS ELEVKLLPHW HDKKLAGIAL
1010 1020 1030 1040 1050
CAVVSCLDPQ DQVSRLSVTC TFKVKDEDKS WVAYTCPVGS WTRHGGGKDK
1060 1070 1080 1090 1100
IELDHVFIGY TSCPHTIKCH EEGNSDECNP TEASLKFTVT GGTSENGKYK
1110 1120 1130 1140 1150
VLKCGLSLVY AKDKDKNSAL ETKYDMLIGK SFQETSEGVD GRVKKTKGKY
1160 1170 1180 1190 1200
VMPVEKNFQE TTEGVDGRVN KKKKTRMDNG RPKKKQRSGR DDNQTRMQVE
1210
LQEGNINSVI MHTVKNF
Length:1,217
Mass (Da):137,726
Last modified:November 1, 1999 - v1
Checksum:iB69B959ADA976E25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243468 Genomic DNA. Translation: CAB50708.1.
AB020744 Genomic DNA. Translation: BAB10246.1.
CP002688 Genomic DNA. Translation: AED95221.1.
PIRiT51140.
RefSeqiNP_199338.1. NM_123893.2. [Q9XGM3-1]
UniGeneiAt.55387.

Genome annotation databases

EnsemblPlantsiAT5G45250.1; AT5G45250.1; AT5G45250. [Q9XGM3-1]
GeneIDi834561.
GrameneiAT5G45250.1; AT5G45250.1; AT5G45250.
KEGGiath:AT5G45250.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243468 Genomic DNA. Translation: CAB50708.1.
AB020744 Genomic DNA. Translation: BAB10246.1.
CP002688 Genomic DNA. Translation: AED95221.1.
PIRiT51140.
RefSeqiNP_199338.1. NM_123893.2. [Q9XGM3-1]
UniGeneiAt.55387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C6RX-ray2.05A/B/C/D11-178[»]
4C6TX-ray2.65B/D11-178[»]
ProteinModelPortaliQ9XGM3.
SMRiQ9XGM3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19810. 2 interactors.
DIPiDIP-61677N.
STRINGi3702.AT5G45250.1.

PTM databases

iPTMnetiQ9XGM3.

Proteomic databases

PaxDbiQ9XGM3.
PRIDEiQ9XGM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G45250.1; AT5G45250.1; AT5G45250. [Q9XGM3-1]
GeneIDi834561.
GrameneiAT5G45250.1; AT5G45250.1; AT5G45250.
KEGGiath:AT5G45250.

Organism-specific databases

TAIRiAT5G45250.

Phylogenomic databases

eggNOGiENOG410JS6A. Eukaryota.
COG4886. LUCA.
InParanoidiQ9XGM3.
KOiK16226.
OMAiHYHAFID.
OrthoDBiEOG093601ZB.
PhylomeDBiQ9XGM3.

Miscellaneous databases

PROiQ9XGM3.

Gene expression databases

GenevisibleiQ9XGM3. AT.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.40.50.300. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR011713. Leu-rich_rpt_3.
IPR002182. NB-ARC.
IPR027417. P-loop_NTPase.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF07725. LRR_3. 1 hit.
PF00931. NB-ARC. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52200. SSF52200. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPS4C_ARATH
AccessioniPrimary (citable) accession number: Q9XGM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 26, 2014
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

MOS12 and the MOS4-associated complex (MAC) are required for the proper splicing of R genes and contribute in the alternative splicing of RPS4.1 Publication
Only two amino-acid changes (N195D and Y950H) are linked to a change from a resistant strain (cv. Columbia or cv. Landsberg erecta) to a susceptible one (cv. RLD).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.