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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261D → A: Loss of cell death. 1 Publication
Mutagenesisi28 – 281R → E: Loss of cell death. 1 Publication
Mutagenesisi30 – 301R → A: Increased homodimerization and stronger cell death induction. 1 Publication
Mutagenesisi33 – 331S → A: Loss of TIR domain homodimerization. Loss of TIR domain heterodimerization; when associated with A-25 in RRS1. Loss of cell death induction. 1 Publication
Mutagenesisi34 – 341H → A: Loss of TIR domain homodimerization. Loss of TIR domain heterodimerization with RRS1. Loss of cell death induction. 1 Publication
Mutagenesisi49 – 502DD → AA: Decreased cell death. 1 Publication
Mutagenesisi49 – 491D → A: Loss of cell death. 1 Publication
Mutagenesisi50 – 534DYED → NYQN: Loss of cell death. 1 Publication
Mutagenesisi54 – 541R → N: Loss of cell death. 1 Publication
Mutagenesisi68 – 681S → A: Loss of cell death. 1 Publication
Mutagenesisi79 – 791Y → A or F: Loss of cell death. 1 Publication
Mutagenesisi84 – 841W → A: Increased cell death. 1 Publication
Mutagenesisi85 – 851C → A: Loss of cell death. 1 Publication
Mutagenesisi88 – 881E → A: Loss of cell death. 1 Publication
Mutagenesisi94 – 941D → N: No effect on cell death. 1 Publication
Mutagenesisi95 – 951C → A: No effect on cell death. 1 Publication
Mutagenesisi97 – 982DE → KK: No effect on cell death. 1 Publication
Mutagenesisi97 – 982DE → QN: Increased cell death. 1 Publication
Mutagenesisi111 – 1111E → K: Increased cell death. 1 Publication
Mutagenesisi112 – 1121P → A or K: Loss of cell death. 1 Publication
Mutagenesisi113 – 1142ST → EE: Loss of cell death. 1 Publication
Mutagenesisi116 – 1161R → A: Loss of cell death. 1 Publication
Mutagenesisi129 – 1302Missing : Loss of cell death. 1 Publication
Mutagenesisi133 – 1342DE → NQ: Increased cell death. 1 Publication
Mutagenesisi134 – 1341E → A or K: Increased cell death. 1 Publication
Mutagenesisi135 – 1351R → E: Loss of cell death. 1 Publication
Mutagenesisi136 – 1383Missing : Loss of cell death. 1 Publication
Mutagenesisi137 – 1371K → E: Loss of cell death. 1 Publication
Mutagenesisi139 – 1391W → A or F: Loss of cell death. 1 Publication
Mutagenesisi140 – 1401K → N: Loss of cell death. 1 Publication
Mutagenesisi160 – 1601E → A: Loss of cell death. 1 Publication
Mutagenesisi242 – 2421K → A: Loss of pathogen effectors recognition. 1 Publication
Mutagenesisi1172 – 11732KK → AA: Loss of nuclear localization; when associated with 1172-A-A-1173. 1 Publication
Mutagenesisi1184 – 11852KK → AA: Loss of nuclear localization; when associated with 1184-A-A-1185. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12171217Disease resistance protein RPS4PRO_0000431365Add
BLAST

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 interactions.
DIPiDIP-61677N.
STRINGi3702.AT5G45250.1.

Structurei

Secondary structure

1
1217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 215Combined sources
Helixi25 – 295Combined sources
Helixi31 – 4111Combined sources
Beta strandi46 – 483Combined sources
Helixi58 – 6710Combined sources
Beta strandi69 – 757Combined sources
Helixi79 – 813Combined sources
Helixi83 – 9816Combined sources
Beta strandi100 – 11011Combined sources
Helixi112 – 1165Combined sources
Helixi120 – 12910Combined sources
Turni130 – 1323Combined sources
Helixi136 – 14510Combined sources
Helixi146 – 1483Combined sources
Beta strandi152 – 1543Combined sources
Helixi160 – 17516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C6RX-ray2.05A/B/C/D11-178[»]
4C6TX-ray2.65B/D11-178[»]
ProteinModelPortaliQ9XGM3.
SMRiQ9XGM3. Positions 13-178, 232-258, 605-911.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 149136TIRPROSITE-ProRule annotationAdd
BLAST
Domaini211 – 472262NB-ARCSequence analysisAdd
BLAST
Repeati260 – 28526LRR 1Sequence analysisAdd
BLAST
Repeati436 – 45924LRR 2Sequence analysisAdd
BLAST
Repeati614 – 63623LRR 3Sequence analysisAdd
BLAST
Repeati637 – 65923LRR 4Sequence analysisAdd
BLAST
Repeati682 – 70625LRR 5Sequence analysisAdd
BLAST
Repeati708 – 72821LRR 6Sequence analysisAdd
BLAST
Repeati729 – 74921LRR 7Sequence analysisAdd
BLAST
Repeati750 – 77425LRR 8Sequence analysisAdd
BLAST
Repeati796 – 81823LRR 9Sequence analysisAdd
BLAST
Repeati819 – 84224LRR 10Sequence analysisAdd
BLAST
Repeati861 – 88727LRR 11Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 342Important for interaction with RRS11 Publication

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1170 – 11778Nuclear localization signalPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1171 – 11744Poly-LysSequence analysis

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.
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_123893.1. [Q9XGM3-1]
UniGeneiAt.55387.

Genome annotation databases

EnsemblPlantsiAT5G45250.1; AT5G45250.1; AT5G45250. [Q9XGM3-1]
GeneIDi834561.
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_123893.1. [Q9XGM3-1]
UniGeneiAt.55387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C6RX-ray2.05A/B/C/D11-178[»]
4C6TX-ray2.65B/D11-178[»]
ProteinModelPortaliQ9XGM3.
SMRiQ9XGM3. Positions 13-178, 232-258, 605-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19810. 2 interactions.
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.
KEGGiath:AT5G45250.

Organism-specific databases

TAIRiAT5G45250.

Phylogenomic databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-LRR family of disease-resistance genes."
    Gassmann W., Hinsch M.E., Staskawicz B.J.
    Plant J. 20:265-277(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE SPLICING.
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(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. "Two Arabidopsis srfr (suppressor of rps4-RLD) mutants exhibit avrRps4-specific disease resistance independent of RPS4."
    Kwon S.I., Koczan J.M., Gassmann W.
    Plant J. 40:366-375(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Nuclear accumulation of the Arabidopsis immune receptor RPS4 is necessary for triggering EDS1-dependent defense."
    Wirthmueller L., Zhang Y., Jones J.D., Parker J.E.
    Curr. Biol. 17:2023-2029(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 1172-LYS-LYS-1173 AND 1184-LYS-LYS-1185.
  6. "Alternative splicing and mRNA levels of the disease resistance gene RPS4 are induced during defense responses."
    Zhang X.C., Gassmann W.
    Plant Physiol. 145:1577-1587(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, INDUCTION BY AVRRPS4.
    Strain: cv. Columbia, cv. Landsberg erecta and cv. Wassilewskija.
  7. "RRS1 and RPS4 provide a dual Resistance-gene system against fungal and bacterial pathogens."
    Narusaka M., Shirasu K., Noutoshi Y., Kubo Y., Shiraishi T., Iwabuchi M., Narusaka Y.
    Plant J. 60:218-226(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Columbia, cv. RLD and cv. Wassilewskija.
  8. "The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction."
    Swiderski M.R., Birker D., Jones J.D.
    Mol. Plant Microbe Interact. 22:157-165(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF ASP-26; ARG-28; 49-ASP--ASP-53; ARG-54; SER-68; TYR-79; TRP-84; CYS-85; GLU-88; ASP-94; CYS-95; 97-ASP-GLU-98; GLU-111; PRO-112; 113-SER-THR-114; ARG-116; 129-MET-ALA-130; 133-ASP-GLU-134; ARG-135; 136-LYS--LYS-138; TRP-139; LYS-140 AND GLU-160.
  9. "The Arabidopsis resistance-like gene SNC1 is activated by mutations in SRFR1 and contributes to resistance to the bacterial effector AvrRps4."
    Kim S.H., Gao F., Bhattacharjee S., Adiasor J.A., Nam J.C., Gassmann W.
    PLoS Pathog. 6:E1001172-E1001172(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRFR1, SUBCELLULAR LOCATION.
  10. "Arabidopsis EDS1 connects pathogen effector recognition to cell compartment-specific immune responses."
    Heidrich K., Wirthmueller L., Tasset C., Pouzet C., Deslandes L., Parker J.E.
    Science 334:1401-1404(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDS1, SUBCELLULAR LOCATION.
  11. "Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators."
    Bhattacharjee S., Halane M.K., Kim S.H., Gassmann W.
    Science 334:1405-1408(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDS1.
  12. "Abscisic acid deficiency antagonizes high-temperature inhibition of disease resistance through enhancing nuclear accumulation of resistance proteins SNC1 and RPS4 in Arabidopsis."
    Mang H.G., Qian W., Zhu Y., Qian J., Kang H.G., Klessig D.F., Hua J.
    Plant Cell 24:1271-1284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "The cyclin L homolog MOS12 and the MOS4-associated complex are required for the proper splicing of plant resistance genes."
    Xu F., Xu S., Wiermer M., Zhang Y., Li X.
    Plant J. 70:916-928(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: MISCELLANEOUS.
  14. "Arabidopsis TNL-WRKY domain receptor RRS1 contributes to temperature-conditioned RPS4 auto-immunity."
    Heidrich K., Tsuda K., Blanvillain-Baufume S., Wirthmueller L., Bautor J., Parker J.E.
    Front. Plant Sci. 4:403-403(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Columbia and cv. Wassilewskija.
  15. "Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana."
    Wan L., Zhang X., Williams S.J., Ve T., Bernoux M., Sohn K.H., Jones J.D., Dodds P.N., Kobe B.
    Acta Crystallogr. F 69:1275-1280(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION OF 11-178.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 11-178 IN COMPLEX WITH RRS1, DOMAIN, FUNCTION, MUTAGENESIS OF ARG-30; SER-33; HIS-34 AND LYS-242.
    Strain: cv. Columbia.

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: June 8, 2016
This is version 123 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.