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C0LGT6

- EFR_ARATH

UniProt

C0LGT6 - EFR_ARATH

Protein

LRR receptor-like serine/threonine-protein kinase EFR

Gene

EFR

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (05 May 2009)
      Previous versions | rss
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    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 – 7411ATPPROSITE-ProRule annotation
    Active sitei849 – 8491Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi718 – 7269ATPPROSITE-ProRule annotation

    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

    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

    GO - Cellular componenti

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

    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. 1 Publication
    Mutagenesisi81 – 822GG → AA: No effect on elf18 sensitivity. 1 Publication
    Mutagenesisi103 – 1064NLAD → ALAA: Insensitive to elf18. 1 Publication
    Mutagenesisi274 – 2752GT → AA: No effect on elf18 sensitivity. 1 Publication
    Mutagenesisi293 – 2942ER → AA: No effect on elf18 sensitivity. 1 Publication
    Mutagenesisi298 – 2992SS → AA: No effect on elf18 sensitivity. 1 Publication
    Mutagenesisi317 – 3182WW → AA: Decreased elf18 sensitivity. 1 Publication
    Mutagenesisi347 – 3482EY → AA: Decreased elf18 sensitivity. 1 Publication
    Mutagenesisi373 – 3753SLF → ALA: No effect on elf18 sensitivity. 1 Publication
    Mutagenesisi397 – 3993ELS → ALA: Decreased elf18 sensitivity. 1 Publication
    Mutagenesisi447 – 4493HLN → ALA: Insensitive to elf18. 1 Publication
    Mutagenesisi469 – 4735DLWMD → ALWMA: Insensitive to elf18. 1 Publication
    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. 2 Publications
    Mutagenesisi791 – 7911Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi836 – 8361Y → F: Loss of elf18-triggered immunity, but no effect on the kinase activity. 2 Publications
    Mutagenesisi849 – 8491D → N: Loss of kinase activity. 2 Publications
    Mutagenesisi875 – 8751Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi877 – 8771Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi897 – 8971Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi902 – 9021Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi915 – 9151Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi939 – 9391Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi944 – 9441Y → F: No effect on elf18-triggered immunity. 2 Publications
    Mutagenesisi979 – 9791Y → F: No effect on elf18-triggered immunity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    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...)Sequence Analysis
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi590 – 5901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Modified residuei709 – 7091PhosphothreonineBy similarity
    Modified residuei791 – 7911PhosphotyrosineBy 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.1 Publication
    Polyubiquitinated at the kinase domain mediated by P.syringae AvrPtoB.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 653629ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini675 – 1031357CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei654 – 67421HelicalSequence AnalysisAdd
    BLAST

    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 kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 21 LRR (leucine-rich) repeats.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti893 – 8931G → L in BAE98400. 1 PublicationCurated
    Sequence conflicti929 – 9291K → E in AAL77697. (PubMed:14593172)Curated
    Sequence conflicti929 – 9291K → E in AAO64755. (PubMed:14593172)Curated

    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

    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: October 1, 2014
    This is version 46 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