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Protein

LRR receptor-like serine/threonine-protein kinase FLS2

Gene

FLS2

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

Functioni

Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 or to the phosphatase hopD2 from Pseudomonas syringae blocks the downstream plant immune response.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481flg221 Publication
Binding sitei152 – 1521flg221 Publication
Binding sitei272 – 2721flg221 Publication
Binding sitei296 – 2961flg221 Publication
Binding sitei898 – 8981ATPPROSITE-ProRule annotation
Active sitei997 – 9971Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi876 – 8849ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • transmembrane receptor protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • defense response by callose deposition in cell wall Source: TAIR
  • defense response to bacterium Source: TAIR
  • detection of bacterium Source: TAIR
  • receptor-mediated endocytosis Source: TAIR
  • 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, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G46330-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
LRR receptor-like serine/threonine-protein kinase FLS2 (EC:2.7.11.1)
Alternative name(s):
Protein FLAGELLIN-SENSING 2
Protein FLAGELLIN-SENSITIVE 2
Gene namesi
Name:FLS2
Ordered Locus Names:At5g46330
ORF Names:MPL12.13, MPL12.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G46330.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 806783ExtracellularSequence analysisAdd
BLAST
Transmembranei807 – 82721HelicalSequence analysisAdd
BLAST
Topological domaini828 – 1173346CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endosome Source: TAIR
  • endosome membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi294 – 2941R → A: Abolishes flagellin-binding. 1 Publication
Mutagenesisi316 – 3161H → A: Abolishes flagellin-binding. 1 Publication
Mutagenesisi318 – 3181G → R in fls2-24; abolishes flagellin-binding. 2 Publications
Mutagenesisi342 – 3421T → Y: Abolishes flagellin-binding. 1 Publication
Mutagenesisi434 – 4341T → Y: No effect on flagellin-binding. 1 Publication
Mutagenesisi867 – 8671T → V: Abolishes flagellin-dependent signaling and reduces ligand-receptor internalization.
Mutagenesisi898 – 8981K → H: Loss of binding with avrPto. 1 Publication
Mutagenesisi1040 – 10401T → A: Abolishes flagellin-dependent signaling.
Mutagenesisi1064 – 10641G → R in fls2-17; abolishes kinase activity and strongly reduces flagellin-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 11731150LRR receptor-like serine/threonine-protein kinase FLS2PRO_0000323720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 ↔ 681 Publication
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi165 ↔ 1871 Publication
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi262 – 2621N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence analysis
Glycosylationi361 – 3611N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi371 – 3711N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi388 – 3881N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi406 – 4061N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi432 – 4321N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence analysis
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence analysis
Glycosylationi588 – 5881N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi631 – 6311N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi684 – 6841N-linked (GlcNAc...)Sequence analysis
Glycosylationi704 – 7041N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence analysis
Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence analysis
Glycosylationi744 – 7441N-linked (GlcNAc...)Sequence analysis
Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence analysis
Modified residuei867 – 8671Phosphothreonine1 Publication
Modified residuei984 – 9841PhosphotyrosineBy similarity
Modified residuei1035 – 10351PhosphoserineBy similarity
Modified residuei1043 – 10431PhosphotyrosineBy similarity
Modified residuei1050 – 10501PhosphotyrosineBy similarity

Post-translational modificationi

Autophosphorylated. The phosphorylated form is essential in the perception of flagellin. Dephosphorylated by KAPP. Autophosphorylation is inhibited by the binding with avrPto1.1 Publication
Polyubiquitinated at the kinase domain mediated by P.syringae AvrPtoB.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9FL28.
PRIDEiQ9FL28.

PTM databases

iPTMnetiQ9FL28.
SwissPalmiQ9FL28.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Inductioni

Repressed upon infection with the P.syringae virulent DC3000 strain, in a flg22- and avrPtoB-dependent manner (at protein level).1 Publication

Gene expression databases

ExpressionAtlasiQ9FL28. baseline and differential.
GenevisibleiQ9FL28. AT.

Interactioni

Subunit structurei

Heterodimer with BAK1 (PubMed:24114786). Interacts with KAPP. Interacts with BAK1. Does not form homodimer. Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a specific ligand-induced manner. Interacts with P.syringae AvrPto1, AvrPtoB and (via the kinase and cytoplasmic domains) hopD2. Interacts with PBS1. Component of large complexes containing, at least, FLS2 and ACD6 in endoplasmic reticulum and plasma membrane (PubMed:24923602). Interacts with MORC1/CRT1 (PubMed:23250427).13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BAK1Q94F623EBI-1799448,EBI-617138
RBG7Q032504EBI-1799448,EBI-1393626

Protein-protein interaction databases

BioGridi19925. 27 interactions.
DIPiDIP-46004N.
IntActiQ9FL28. 3 interactions.
STRINGi3702.AT5G46330.1.

Structurei

Secondary structure

1
1173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3811Combined sources
Helixi50 – 556Combined sources
Helixi60 – 623Combined sources
Beta strandi66 – 683Combined sources
Beta strandi74 – 785Combined sources
Beta strandi85 – 873Combined sources
Helixi90 – 945Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi109 – 1113Combined sources
Helixi114 – 1185Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi133 – 1353Combined sources
Helixi138 – 1425Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 1665Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi181 – 1833Combined sources
Helixi188 – 1903Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi205 – 2073Combined sources
Helixi210 – 2145Combined sources
Beta strandi220 – 2223Combined sources
Helixi234 – 2385Combined sources
Beta strandi244 – 2463Combined sources
Helixi258 – 2625Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi277 – 2793Combined sources
Helixi282 – 2865Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi301 – 3033Combined sources
Helixi306 – 3105Combined sources
Beta strandi315 – 3184Combined sources
Helixi330 – 3345Combined sources
Beta strandi340 – 3423Combined sources
Helixi354 – 3585Combined sources
Beta strandi364 – 3663Combined sources
Helixi380 – 3823Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi393 – 3964Combined sources
Helixi402 – 4065Combined sources
Beta strandi412 – 4143Combined sources
Turni428 – 4314Combined sources
Beta strandi434 – 4374Combined sources
Helixi449 – 4535Combined sources
Beta strandi459 – 4613Combined sources
Helixi473 – 4775Combined sources
Beta strandi482 – 4854Combined sources
Helixi497 – 5026Combined sources
Beta strandi507 – 5093Combined sources
Beta strandi512 – 5187Combined sources
Helixi521 – 5255Combined sources
Beta strandi531 – 5333Combined sources
Beta strandi536 – 5416Combined sources
Helixi545 – 5495Combined sources
Beta strandi555 – 5573Combined sources
Beta strandi564 – 5663Combined sources
Helixi569 – 5735Combined sources
Beta strandi578 – 5814Combined sources
Beta strandi584 – 5907Combined sources
Helixi593 – 5975Combined sources
Beta strandi602 – 6054Combined sources
Helixi617 – 6226Combined sources
Beta strandi628 – 6314Combined sources
Helixi643 – 6453Combined sources
Beta strandi653 – 6553Combined sources
Beta strandi658 – 6614Combined sources
Helixi667 – 6715Combined sources
Beta strandi677 – 6793Combined sources
Helixi691 – 6966Combined sources
Beta strandi701 – 7044Combined sources
Helixi716 – 7205Combined sources
Beta strandi726 – 7283Combined sources
Helixi741 – 7444Combined sources
Beta strandi750 – 7523Combined sources
Helixi773 – 7764Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MN8X-ray3.06A25-800[»]
4MNAX-ray4.00A25-800[»]
ProteinModelPortaliQ9FL28.
SMRiQ9FL28. Positions 26-784, 854-1153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati97 – 11923LRR 1Add
BLAST
Repeati121 – 14323LRR 2Add
BLAST
Repeati145 – 16723LRR 3Add
BLAST
Repeati169 – 19224LRR 4Add
BLAST
Repeati193 – 21523LRR 5Add
BLAST
Repeati217 – 24024LRR 6Add
BLAST
Repeati241 – 26323LRR 7Add
BLAST
Repeati265 – 28824LRR 8Add
BLAST
Repeati289 – 31123LRR 9Add
BLAST
Repeati313 – 33523LRR 10Add
BLAST
Repeati337 – 35923LRR 11Add
BLAST
Repeati361 – 38323LRR 12Add
BLAST
Repeati385 – 40723LRR 13Add
BLAST
Repeati409 – 43123LRR 14Add
BLAST
Repeati432 – 45423LRR 15Add
BLAST
Repeati456 – 47823LRR 16Add
BLAST
Repeati480 – 50324LRR 17Add
BLAST
Repeati504 – 52724LRR 18Add
BLAST
Repeati528 – 55023LRR 19Add
BLAST
Repeati552 – 57423LRR 20Add
BLAST
Repeati576 – 59924LRR 21Add
BLAST
Repeati600 – 62122LRR 22Add
BLAST
Repeati627 – 64923LRR 23Add
BLAST
Repeati650 – 67324LRR 24Add
BLAST
Repeati674 – 69623LRR 25Add
BLAST
Repeati699 – 72123LRR 26Add
BLAST
Repeati723 – 74624LRR 27Add
BLAST
Repeati747 – 76923LRR 28Add
BLAST
Domaini870 – 1155286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

Both extracellular leucine-rich repeats and protein kinase domains are required for flg22-binding. The LRR 9 to LRR 15 domains are involved in flg22-binding.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 28 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

eggNOGiENOG410IH3G. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiQ9FL28.
KOiK13420.
OMAiPENIIGA.
PhylomeDBiQ9FL28.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 3 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
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]
SMARTiSM00369. LRR_TYP. 13 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. 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.

Q9FL28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLSKTFLI LTLTFFFFGI ALAKQSFEPE IEALKSFKNG ISNDPLGVLS
60 70 80 90 100
DWTIIGSLRH CNWTGITCDS TGHVVSVSLL EKQLEGVLSP AIANLTYLQV
110 120 130 140 150
LDLTSNSFTG KIPAEIGKLT ELNQLILYLN YFSGSIPSGI WELKNIFYLD
160 170 180 190 200
LRNNLLSGDV PEEICKTSSL VLIGFDYNNL TGKIPECLGD LVHLQMFVAA
210 220 230 240 250
GNHLTGSIPV SIGTLANLTD LDLSGNQLTG KIPRDFGNLL NLQSLVLTEN
260 270 280 290 300
LLEGDIPAEI GNCSSLVQLE LYDNQLTGKI PAELGNLVQL QALRIYKNKL
310 320 330 340 350
TSSIPSSLFR LTQLTHLGLS ENHLVGPISE EIGFLESLEV LTLHSNNFTG
360 370 380 390 400
EFPQSITNLR NLTVLTVGFN NISGELPADL GLLTNLRNLS AHDNLLTGPI
410 420 430 440 450
PSSISNCTGL KLLDLSHNQM TGEIPRGFGR MNLTFISIGR NHFTGEIPDD
460 470 480 490 500
IFNCSNLETL SVADNNLTGT LKPLIGKLQK LRILQVSYNS LTGPIPREIG
510 520 530 540 550
NLKDLNILYL HSNGFTGRIP REMSNLTLLQ GLRMYSNDLE GPIPEEMFDM
560 570 580 590 600
KLLSVLDLSN NKFSGQIPAL FSKLESLTYL SLQGNKFNGS IPASLKSLSL
610 620 630 640 650
LNTFDISDNL LTGTIPGELL ASLKNMQLYL NFSNNLLTGT IPKELGKLEM
660 670 680 690 700
VQEIDLSNNL FSGSIPRSLQ ACKNVFTLDF SQNNLSGHIP DEVFQGMDMI
710 720 730 740 750
ISLNLSRNSF SGEIPQSFGN MTHLVSLDLS SNNLTGEIPE SLANLSTLKH
760 770 780 790 800
LKLASNNLKG HVPESGVFKN INASDLMGNT DLCGSKKPLK PCTIKQKSSH
810 820 830 840 850
FSKRTRVILI ILGSAAALLL VLLLVLILTC CKKKEKKIEN SSESSLPDLD
860 870 880 890 900
SALKLKRFEP KELEQATDSF NSANIIGSSS LSTVYKGQLE DGTVIAVKVL
910 920 930 940 950
NLKEFSAESD KWFYTEAKTL SQLKHRNLVK ILGFAWESGK TKALVLPFME
960 970 980 990 1000
NGNLEDTIHG SAAPIGSLLE KIDLCVHIAS GIDYLHSGYG FPIVHCDLKP
1010 1020 1030 1040 1050
ANILLDSDRV AHVSDFGTAR ILGFREDGST TASTSAFEGT IGYLAPEFAY
1060 1070 1080 1090 1100
MRKVTTKADV FSFGIIMMEL MTKQRPTSLN DEDSQDMTLR QLVEKSIGNG
1110 1120 1130 1140 1150
RKGMVRVLDM ELGDSIVSLK QEEAIEDFLK LCLFCTSSRP EDRPDMNEIL
1160 1170
THLMKLRGKA NSFREDRNED REV
Length:1,173
Mass (Da):128,824
Last modified:March 1, 2001 - v1
Checksum:i6AF93B467A339359
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti652 – 6521Q → K in AAO41929 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010698 Genomic DNA. Translation: BAB11088.1.
CP002688 Genomic DNA. Translation: AED95370.1.
BT003880 mRNA. Translation: AAO41929.1.
AK226709 mRNA. Translation: BAE98815.1.
RefSeqiNP_199445.1. NM_124003.3.
UniGeneiAt.29960.

Genome annotation databases

EnsemblPlantsiAT5G46330.1; AT5G46330.1; AT5G46330.
GeneIDi834676.
GrameneiAT5G46330.1; AT5G46330.1; AT5G46330.
KEGGiath:AT5G46330.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010698 Genomic DNA. Translation: BAB11088.1.
CP002688 Genomic DNA. Translation: AED95370.1.
BT003880 mRNA. Translation: AAO41929.1.
AK226709 mRNA. Translation: BAE98815.1.
RefSeqiNP_199445.1. NM_124003.3.
UniGeneiAt.29960.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MN8X-ray3.06A25-800[»]
4MNAX-ray4.00A25-800[»]
ProteinModelPortaliQ9FL28.
SMRiQ9FL28. Positions 26-784, 854-1153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19925. 27 interactions.
DIPiDIP-46004N.
IntActiQ9FL28. 3 interactions.
STRINGi3702.AT5G46330.1.

PTM databases

iPTMnetiQ9FL28.
SwissPalmiQ9FL28.

Proteomic databases

PaxDbiQ9FL28.
PRIDEiQ9FL28.

Protocols and materials databases

DNASUi834676.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G46330.1; AT5G46330.1; AT5G46330.
GeneIDi834676.
GrameneiAT5G46330.1; AT5G46330.1; AT5G46330.
KEGGiath:AT5G46330.

Organism-specific databases

TAIRiAT5G46330.

Phylogenomic databases

eggNOGiENOG410IH3G. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiQ9FL28.
KOiK13420.
OMAiPENIIGA.
PhylomeDBiQ9FL28.

Enzyme and pathway databases

BioCyciARA:AT5G46330-MONOMER.

Miscellaneous databases

PROiQ9FL28.

Gene expression databases

ExpressionAtlasiQ9FL28. baseline and differential.
GenevisibleiQ9FL28. AT.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 3 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
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]
SMARTiSM00369. LRR_TYP. 13 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
    Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:131-145(1998) [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. "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 1-831.
    Strain: cv. Columbia.
  5. "FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis."
    Gomez-Gomez L., Boller T.
    Mol. Cell 5:1003-1011(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "Sensitivity of different ecotypes and mutants of Arabidopsis thaliana toward the bacterial elicitor flagellin correlates with the presence of receptor-binding sites."
    Bauer Z., Gomez-Gomez L., Boller T., Felix G.
    J. Biol. Chem. 276:45669-45676(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO FLAGELLIN.
  7. "Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis."
    Gomez-Gomez L., Bauer Z., Boller T.
    Plant Cell 13:1155-1163(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-318 AND GLY-1064, INTERACTION WITH KAPP.
  8. Cited for: FUNCTION.
  9. "Flagellin perception: a paradigm for innate immunity."
    Gomez-Gomez L., Boller T.
    Trends Plant Sci. 7:251-256(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Bacterial disease resistance in Arabidopsis through flagellin perception."
    Zipfel C., Robatzek S., Navarro L., Oakeley E.J., Jones J.D.G., Felix G., Boller T.
    Nature 428:764-767(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Functional analysis and expression studies of the flagellin receptor FLS2."
    Robatzek S., Chinchilla D., Bauer Z., Zipfel C., Kunze G., Bittel P., Caniard A., Felix G., Boller T.
    (In) Proceedings of the 15th international conference on Arabidopsis research, abstract#05-086, Berlin (2004)
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis."
    Robatzek S., Chinchilla D., Boller T.
    Genes Dev. 20:537-542(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "The Arabidopsis receptor kinase FLS2 binds flg22 and determines the specificity of flagellin perception."
    Chinchilla D., Bauer Z., Regenass M., Boller T., Felix G.
    Plant Cell 18:465-476(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING TO FLAGELLIN.
  14. "A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence."
    Chinchilla D., Zipfel C., Robatzek S., Kemmerling B., Nuernberger T., Jones J.D.G., Felix G., Boller T.
    Nature 448:497-500(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  15. "Identification and mutational analysis of Arabidopsis FLS2 leucine-rich repeat domain residues that contribute to flagellin perception."
    Dunning F.M., Sun W., Jansen K.L., Helft L., Bent A.F.
    Plant Cell 19:3297-3313(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  16. "Ligand-dependent reduction in the membrane mobility of FLAGELLIN SENSITIVE2, an arabidopsis receptor-like kinase."
    Ali G.S., Prasad K.V.S.K., Day I., Reddy A.S.N.
    Plant Cell Physiol. 48:1601-1611(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  17. "The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants."
    Heese A., Hann D.R., Gimenez-Ibanez S., Jones A.M.E., He K., Li J., Schroeder J.I., Peck S.C., Rathjen J.P.
    Proc. Natl. Acad. Sci. U.S.A. 104:12217-12222(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAK1.
  18. "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, MUTAGENESIS OF LYS-898, AUTOPHOSPHORYLATION.
  19. "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, INTERACTION WITH AVRPTOB, REPRESSION BY PSEUDOMONAS SYRINGAE, SUBCELLULAR LOCATION.
  20. "Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector."
    Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M., Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.
    Cell Host Microbe 7:290-301(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PBS1.
  21. "Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1."
    Schulze B., Mentzel T., Jehle A.K., Mueller K., Beeler S., Boller T., Felix G., Chinchilla D.
    J. Biol. Chem. 285:9444-9451(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAK1, PHOSPHORYLATION.
  22. "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: INTERACTION WITH SERK3/BAK1; SERK4/BKK1; SERK1 AND SERK2.
    Strain: cv. Columbia.
  23. "CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity."
    Kang H.-G., Hyong W.C., von Einem S., Manosalva P., Ehlers K., Liu P.-P., Buxa S.V., Moreau M., Mang H.-G., Kachroo P., Kogel K.-H., Klessig D.F.
    Nat. Commun. 3:1297-1297(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MORC1/CRT1.
    Strain: cv. Columbia.
  24. "Salicylic acid signaling controls the maturation and localization of the arabidopsis defense protein ACCELERATED CELL DEATH6."
    Zhang Z., Shrestha J., Tateda C., Greenberg J.T.
    Mol. Plant 7:1365-1383(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    Strain: cv. Columbia.
  25. Cited for: FUNCTION, INTERACTION WITH HOPD2.
  26. "Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex."
    Sun Y., Li L., Macho A.P., Han Z., Hu Z., Zipfel C., Zhou J.M., Chai J.
    Science 342:624-628(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 25-800 IN COMPLEX WITH BAK1 AND FLG22, DISULFIDE BONDS, GLYCOSYLATION AT ASN-94; ASN-217; ASN-262; ASN-361; ASN-371; ASN-388; ASN-406; ASN-432; ASN-588; ASN-631 AND ASN-704, SUBUNIT, MUTAGENESIS OF ARG-294; HIS-316; GLY-318; THR-342 AND THR-434.

Entry informationi

Entry nameiFLS2_ARATH
AccessioniPrimary (citable) accession number: Q9FL28
Secondary accession number(s): Q0WVN3, Q84WF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2001
Last modified: July 6, 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

After flg22-binding, forms instantaneously a heteromeric complex with BAK1 and is transphosphorylated within 15 seconds. After activation, the receptor is internalized by endocytosis and subject to degradation.

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.