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C0LGT6

- EFR_ARATH

UniProt

C0LGT6 - EFR_ARATH

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Protein

LRR receptor-like serine/threonine-protein kinase EFR

Gene
EFR, At5g20480, F7C8.70
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Reduces transformation by Rhizobium radiobacter probably by inducing plant defense during the interaction. Binding to the effector AvrPto1 from P.syringae blocks the downstream plant immune response while interaction with hopD2 decreases the phosphorylation level of EFR upon elf18 treatment. Specific endoplasmic reticulum quality control components (ERD2B, CRT3, UGGT and STT3A) are required for the biogenesis of EFR.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei741 – 7411ATP By similarity
Active sitei849 – 8491Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi718 – 7269ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB-KW
  4. transmembrane receptor protein kinase activity Source: TAIR

GO - Biological processi

  1. defense response signaling pathway, resistance gene-independent Source: TAIR
  2. detection of bacterium Source: TAIR
  3. immune response-regulating signaling pathway Source: TAIR
  4. plant-type hypersensitive response Source: TAIR
  5. regulation of anion channel activity Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Plant defense

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G20480-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
LRR receptor-like serine/threonine-protein kinase EFR (EC:2.7.11.1)
Alternative name(s):
Elongation factor Tu receptor
Short name:
EF-Tu receptor
Gene namesi
Name:EFR
Ordered Locus Names:At5g20480
ORF Names:F7C8.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G20480.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 653629Extracellular Reviewed predictionAdd
BLAST
Transmembranei654 – 67421Helical; Reviewed predictionAdd
BLAST
Topological domaini675 – 1031357Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endomembrane system Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Enhanced susceptibility to R.radiobacter.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 772IS → AA: No effect on elf18 sensitivity.
Mutagenesisi81 – 822GG → AA: No effect on elf18 sensitivity.
Mutagenesisi103 – 1064NLAD → ALAA: Insensitive to elf18.
Mutagenesisi274 – 2752GT → AA: No effect on elf18 sensitivity.
Mutagenesisi293 – 2942ER → AA: No effect on elf18 sensitivity.
Mutagenesisi298 – 2992SS → AA: No effect on elf18 sensitivity.
Mutagenesisi317 – 3182WW → AA: Decreased elf18 sensitivity.
Mutagenesisi347 – 3482EY → AA: Decreased elf18 sensitivity.
Mutagenesisi373 – 3753SLF → ALA: No effect on elf18 sensitivity.
Mutagenesisi397 – 3993ELS → ALA: Decreased elf18 sensitivity.
Mutagenesisi447 – 4493HLN → ALA: Insensitive to elf18.
Mutagenesisi469 – 4735DLWMD → ALWMA: Insensitive to elf18.
Mutagenesisi564 – 5685NVDFS → AVDFA: Decreased elf18 sensitivity. 1 Publication
Mutagenesisi588 – 5903NLN → ALA: Insensitive to elf18. 1 Publication
Mutagenesisi702 – 7021Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi791 – 7911Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi836 – 8361Y → F: Loss of elf18-triggered immunity, but no effect on the kinase activity. 1 Publication
Mutagenesisi849 – 8491D → N: Loss of kinase activity. 1 Publication
Mutagenesisi875 – 8751Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi877 – 8771Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi897 – 8971Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi902 – 9021Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi915 – 9151Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi939 – 9391Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi944 – 9441Y → F: No effect on elf18-triggered immunity. 1 Publication
Mutagenesisi979 – 9791Y → F: No effect on elf18-triggered immunity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Chaini25 – 10311007LRR receptor-like serine/threonine-protein kinase EFRPRO_0000387508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...) Reviewed prediction
Glycosylationi55 – 551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi95 – 951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi143 – 1431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi180 – 1801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi191 – 1911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi239 – 2391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi288 – 2881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi323 – 3231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi329 – 3291N-linked (GlcNAc...) Reviewed prediction
Glycosylationi342 – 3421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi366 – 3661N-linked (GlcNAc...) Reviewed prediction
Glycosylationi439 – 4391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi478 – 4781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi571 – 5711N-linked (GlcNAc...) Reviewed prediction
Glycosylationi590 – 5901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi608 – 6081N-linked (GlcNAc...) Reviewed prediction
Modified residuei709 – 7091Phosphothreonine By similarity
Modified residuei791 – 7911Phosphotyrosine By similarity
Modified residuei836 – 8361Phosphotyrosine1 Publication
Modified residuei897 – 8971Phosphotyrosine1 Publication

Post-translational modificationi

Autophosphorylated after elicitation with elfl18. Autophosphorylation is inhibited by the binding with avrPto1. Phosphorylation at T-836 is required for immune signaling.2 Publications
Polyubiquitinated at the kinase domain mediated by P.syringae AvrPtoB.

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiC0LGT6.
PRIDEiC0LGT6.

Interactioni

Subunit structurei

Binds to Pseudomonas syringae AvrPto1 and (via the kinase and cytoplasmic domains) to hopD2. Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a specific ligand-induced manner.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RBG7Q032504EBI-8801168,EBI-1393626

Protein-protein interaction databases

BioGridi17446. 1 interaction.
IntActiC0LGT6. 1 interaction.
STRINGi3702.AT5G20480.1-P.

Structurei

3D structure databases

ProteinModelPortaliC0LGT6.
SMRiC0LGT6. Positions 27-622, 698-993.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati98 – 12023LRR 1Add
BLAST
Repeati122 – 14423LRR 2Add
BLAST
Repeati146 – 16823LRR 3Add
BLAST
Repeati170 – 19324LRR 4Add
BLAST
Repeati194 – 21623LRR 5Add
BLAST
Repeati218 – 24023LRR 6Add
BLAST
Repeati242 – 26423LRR 7Add
BLAST
Repeati267 – 28923LRR 8Add
BLAST
Repeati291 – 31222LRR 9Add
BLAST
Repeati315 – 33521LRR 10Add
BLAST
Repeati345 – 36824LRR 11Add
BLAST
Repeati370 – 39223LRR 12Add
BLAST
Repeati394 – 41623LRR 13Add
BLAST
Repeati418 – 44023LRR 14Add
BLAST
Repeati442 – 46423LRR 15Add
BLAST
Repeati466 – 48722LRR 16Add
BLAST
Repeati490 – 51223LRR 17Add
BLAST
Repeati514 – 53623LRR 18Add
BLAST
Repeati538 – 56023LRR 19Add
BLAST
Repeati561 – 58424LRR 20Add
BLAST
Repeati585 – 59713LRR 21Add
BLAST
Domaini712 – 1001290Protein kinaseAdd
BLAST

Domaini

The last two LRR (561-597) are necessary for elf18 binding and functionality.1 Publication

Sequence similaritiesi

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000116551.
InParanoidiQ8S9I3.
KOiK13428.
OMAiSGRIPRY.
PhylomeDBiC0LGT6.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_subgrp.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

C0LGT6-1 [UniParc]FASTAAdd to Basket

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MKLSFSLVFN ALTLLLQVCI FAQARFSNET DMQALLEFKS QVSENNKREV     50
LASWNHSSPF CNWIGVTCGR RRERVISLNL GGFKLTGVIS PSIGNLSFLR 100
LLNLADNSFG STIPQKVGRL FRLQYLNMSY NLLEGRIPSS LSNCSRLSTV 150
DLSSNHLGHG VPSELGSLSK LAILDLSKNN LTGNFPASLG NLTSLQKLDF 200
AYNQMRGEIP DEVARLTQMV FFQIALNSFS GGFPPALYNI SSLESLSLAD 250
NSFSGNLRAD FGYLLPNLRR LLLGTNQFTG AIPKTLANIS SLERFDISSN 300
YLSGSIPLSF GKLRNLWWLG IRNNSLGNNS SSGLEFIGAV ANCTQLEYLD 350
VGYNRLGGEL PASIANLSTT LTSLFLGQNL ISGTIPHDIG NLVSLQELSL 400
ETNMLSGELP VSFGKLLNLQ VVDLYSNAIS GEIPSYFGNM TRLQKLHLNS 450
NSFHGRIPQS LGRCRYLLDL WMDTNRLNGT IPQEILQIPS LAYIDLSNNF 500
LTGHFPEEVG KLELLVGLGA SYNKLSGKMP QAIGGCLSME FLFMQGNSFD 550
GAIPDISRLV SLKNVDFSNN NLSGRIPRYL ASLPSLRNLN LSMNKFEGRV 600
PTTGVFRNAT AVSVFGNTNI CGGVREMQLK PCIVQASPRK RKPLSVRKKV 650
VSGICIGIAS LLLIIIVASL CWFMKRKKKN NASDGNPSDS TTLGMFHEKV 700
SYEELHSATS RFSSTNLIGS GNFGNVFKGL LGPENKLVAV KVLNLLKHGA 750
TKSFMAECET FKGIRHRNLV KLITVCSSLD SEGNDFRALV YEFMPKGSLD 800
MWLQLEDLER VNDHSRSLTP AEKLNIAIDV ASALEYLHVH CHDPVAHCDI 850
KPSNILLDDD LTAHVSDFGL AQLLYKYDRE SFLNQFSSAG VRGTIGYAAP 900
EYGMGGQPSI QGDVYSFGIL LLEMFSGKKP TDESFAGDYN LHSYTKSILS 950
GCTSSGGSNA IDEGLRLVLQ VGIKCSEEYP RDRMRTDEAV RELISIRSKF 1000
FSSKTTITES PRDAPQSSPQ EWMLNTDMHT M 1031
Length:1,031
Mass (Da):113,353
Last modified:May 5, 2009 - v1
Checksum:iE0E0AE671DA9124D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti893 – 8931G → L in BAE98400. 1 Publication
Sequence conflicti929 – 9291K → E in AAL77697. 1 Publication
Sequence conflicti929 – 9291K → E in AAO64755. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF296833 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92850.1.
AY075690 mRNA. Translation: AAL77697.1.
BT005820 mRNA. Translation: AAO64755.1.
FJ708780 mRNA. Translation: ACN59371.1.
AK226237 mRNA. Translation: BAE98400.1.
RefSeqiNP_197548.1. NM_122055.4.
UniGeneiAt.31176.

Genome annotation databases

EnsemblPlantsiAT5G20480.1; AT5G20480.1; AT5G20480.
GeneIDi832170.
KEGGiath:AT5G20480.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF296833 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92850.1 .
AY075690 mRNA. Translation: AAL77697.1 .
BT005820 mRNA. Translation: AAO64755.1 .
FJ708780 mRNA. Translation: ACN59371.1 .
AK226237 mRNA. Translation: BAE98400.1 .
RefSeqi NP_197548.1. NM_122055.4.
UniGenei At.31176.

3D structure databases

ProteinModelPortali C0LGT6.
SMRi C0LGT6. Positions 27-622, 698-993.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 17446. 1 interaction.
IntActi C0LGT6. 1 interaction.
STRINGi 3702.AT5G20480.1-P.

Proteomic databases

PaxDbi C0LGT6.
PRIDEi C0LGT6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G20480.1 ; AT5G20480.1 ; AT5G20480 .
GeneIDi 832170.
KEGGi ath:AT5G20480.

Organism-specific databases

GeneFarmi 2543. 56.
TAIRi AT5G20480.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000116551.
InParanoidi Q8S9I3.
KOi K13428.
OMAi SGRIPRY.
PhylomeDBi C0LGT6.

Enzyme and pathway databases

BioCyci ARA:AT5G20480-MONOMER.

Miscellaneous databases

PROi C0LGT6.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_subgrp.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
    Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
    BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 893-1031.
    Strain: cv. Columbia.
  6. "Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation."
    Zipfel C., Kunze G., Chinchilla D., Caniard A., Jones J.D.G., Boller T., Felix G.
    Cell 125:749-760(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases."
    Xiang T., Zong N., Zou Y., Wu Y., Zhang J., Xing W., Li Y., Tang X., Zhu L., Chai J., Zhou J.-M.
    Curr. Biol. 18:74-80(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO1, AUTOPHOSPHORYLATION.
  8. "Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB."
    Goehre V., Spallek T., Haeweker H., Mersmann S., Mentzel T., Boller T., de Torres M., Mansfield J.W., Robatzek S.
    Curr. Biol. 18:1824-1832(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY AVRPTOB.
  9. "Receptor quality control in the endoplasmic reticulum for plant innate immunity."
    Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H., Dong X., Robatzek S., Schulze-Lefert P.
    EMBO J. 28:3439-3449(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR."
    Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D., Zipfel C., Jones J.D.
    Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Arabidopsis thaliana pattern recognition receptors for bacterial elongation factor Tu and flagellin can be combined to form functional chimeric receptors."
    Albert M., Jehle A.K., Mueller K., Eisele C., Lipschis M., Felix G.
    J. Biol. Chem. 285:19035-19042(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
  12. "LRR conservation mapping to predict functional sites within protein leucine-rich repeat domains."
    Helft L., Reddy V., Chen X., Koller T., Federici L., Fernandez-Recio J., Gupta R., Bent A.
    PLoS ONE 6:E21614-E21614(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, MUTAGENESIS OF 76-ILE-SER-77; 81-GLY-GLY-82; 103-ASN--ASP-106; 274-GLY-THR-275; 293-GLU-ARG-294; 298-SER-SER-299; 317-TRP-TRP-318; 347-GLU-TYR-348; 373-SER--PHE-375; 397-GLU--SER-399; 447-HIS--ASN-449; 469-ASP--ASP-473; 564-ASN--SER-568 AND 588-ASN--ASN-590.
  13. "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens."
    Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N., Malinovsky F.G., Tor M., de Vries S., Zipfel C.
    Plant Cell 23:2440-2455(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SERK3/BAK1; SERK4/BKK1; SERK1 AND SERK2.
    Strain: cv. Columbia.
  14. Cited for: FUNCTION, PHOSPHORYLATION AT TYR-836 AND TYR-897, MUTAGENESIS OF TYR-702; TYR-791; TYR-836; ASP-849; TYR-875; TYR-877; TYR-897; TYR-902; TYR-915; TYR-939; TYR-944 AND TYR-979, SUBCELLULAR LOCATION, INTERACTION WITH HOPD2.

Entry informationi

Entry nameiEFR_ARATH
AccessioniPrimary (citable) accession number: C0LGT6
Secondary accession number(s): Q0WWU8, Q8S9I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 45 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

External Data

Dasty 3

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