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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)DescriptionActionsGraphical viewLength
Binding sitei148flg221 Publication1
Binding sitei152flg221 Publication1
Binding sitei272flg221 Publication1
Binding sitei296flg221 Publication1
Binding sitei898ATPPROSITE-ProRule annotation1
Active sitei997Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi876 – 884ATPPROSITE-ProRule annotation9

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

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)DescriptionActionsGraphical viewLength
Topological domaini24 – 806ExtracellularSequence analysisAdd BLAST783
Transmembranei807 – 827HelicalSequence analysisAdd BLAST21
Topological domaini828 – 1173CytoplasmicSequence analysisAdd BLAST346

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)DescriptionActionsGraphical viewLength
Mutagenesisi294R → A: Abolishes flagellin-binding. 1 Publication1
Mutagenesisi316H → A: Abolishes flagellin-binding. 1 Publication1
Mutagenesisi318G → R in fls2-24; abolishes flagellin-binding. 2 Publications1
Mutagenesisi342T → Y: Abolishes flagellin-binding. 1 Publication1
Mutagenesisi434T → Y: No effect on flagellin-binding. 1 Publication1
Mutagenesisi867T → V: Abolishes flagellin-dependent signaling and reduces ligand-receptor internalization. 1
Mutagenesisi898K → H: Loss of binding with avrPto. 1 Publication1
Mutagenesisi1040T → A: Abolishes flagellin-dependent signaling. 1
Mutagenesisi1064G → R in fls2-17; abolishes kinase activity and strongly reduces flagellin-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000032372024 – 1173LRR receptor-like serine/threonine-protein kinase FLS2Add BLAST1150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi61 ↔ 681 Publication
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Glycosylationi94N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi165 ↔ 1871 Publication
Glycosylationi179N-linked (GlcNAc...)Sequence analysis1
Glycosylationi217N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi262N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi347N-linked (GlcNAc...)Sequence analysis1
Glycosylationi361N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi371N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi388N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi406N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi432N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi453N-linked (GlcNAc...)Sequence analysis1
Glycosylationi466N-linked (GlcNAc...)Sequence analysis1
Glycosylationi525N-linked (GlcNAc...)Sequence analysis1
Glycosylationi588N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi631N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi684N-linked (GlcNAc...)Sequence analysis1
Glycosylationi704N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi720N-linked (GlcNAc...)Sequence analysis1
Glycosylationi733N-linked (GlcNAc...)Sequence analysis1
Glycosylationi744N-linked (GlcNAc...)Sequence analysis1
Glycosylationi772N-linked (GlcNAc...)Sequence analysis1
Modified residuei867Phosphothreonine1 Publication1
Modified residuei869Phosphoserine; by BAK11 Publication1
Modified residuei906Phosphoserine; by BAK11 Publication1
Modified residuei938Phosphoserine1 Publication1
Modified residuei941Phosphothreonine1 Publication1
Modified residuei961Phosphoserine; by BAK11 Publication1
Modified residuei984PhosphotyrosineBy similarity1
Modified residuei1035PhosphoserineBy similarity1
Modified residuei1043PhosphotyrosineBy similarity1
Modified residuei1050PhosphotyrosineBy similarity1
Modified residuei1084Phosphoserine1 Publication1
Modified residuei1115Phosphoserine; by BAK11 Publication1

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.

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. Component of large complexes containing, at least, FLS2 and ACD6 in endoplasmic reticulum and plasma membrane (PubMed:24923602). Interacts with MORC1/CRT1 (PubMed:23250427). Interacts with PBS1, BIK1, PBL1 and PBL2 (PubMed:20413097). Interacts with RBOHD (PubMed:24629339).14 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

11173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 38Combined sources11
Helixi50 – 55Combined sources6
Helixi60 – 62Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi74 – 78Combined sources5
Beta strandi85 – 87Combined sources3
Helixi90 – 94Combined sources5
Beta strandi100 – 102Combined sources3
Beta strandi109 – 111Combined sources3
Helixi114 – 118Combined sources5
Beta strandi124 – 126Combined sources3
Beta strandi133 – 135Combined sources3
Helixi138 – 142Combined sources5
Beta strandi148 – 150Combined sources3
Beta strandi157 – 159Combined sources3
Helixi162 – 166Combined sources5
Beta strandi172 – 174Combined sources3
Beta strandi181 – 183Combined sources3
Helixi188 – 190Combined sources3
Beta strandi195 – 198Combined sources4
Beta strandi205 – 207Combined sources3
Helixi210 – 214Combined sources5
Beta strandi220 – 222Combined sources3
Helixi234 – 238Combined sources5
Beta strandi244 – 246Combined sources3
Helixi258 – 262Combined sources5
Beta strandi267 – 270Combined sources4
Beta strandi277 – 279Combined sources3
Helixi282 – 286Combined sources5
Beta strandi292 – 294Combined sources3
Beta strandi301 – 303Combined sources3
Helixi306 – 310Combined sources5
Beta strandi315 – 318Combined sources4
Helixi330 – 334Combined sources5
Beta strandi340 – 342Combined sources3
Helixi354 – 358Combined sources5
Beta strandi364 – 366Combined sources3
Helixi380 – 382Combined sources3
Beta strandi388 – 390Combined sources3
Beta strandi393 – 396Combined sources4
Helixi402 – 406Combined sources5
Beta strandi412 – 414Combined sources3
Turni428 – 431Combined sources4
Beta strandi434 – 437Combined sources4
Helixi449 – 453Combined sources5
Beta strandi459 – 461Combined sources3
Helixi473 – 477Combined sources5
Beta strandi482 – 485Combined sources4
Helixi497 – 502Combined sources6
Beta strandi507 – 509Combined sources3
Beta strandi512 – 518Combined sources7
Helixi521 – 525Combined sources5
Beta strandi531 – 533Combined sources3
Beta strandi536 – 541Combined sources6
Helixi545 – 549Combined sources5
Beta strandi555 – 557Combined sources3
Beta strandi564 – 566Combined sources3
Helixi569 – 573Combined sources5
Beta strandi578 – 581Combined sources4
Beta strandi584 – 590Combined sources7
Helixi593 – 597Combined sources5
Beta strandi602 – 605Combined sources4
Helixi617 – 622Combined sources6
Beta strandi628 – 631Combined sources4
Helixi643 – 645Combined sources3
Beta strandi653 – 655Combined sources3
Beta strandi658 – 661Combined sources4
Helixi667 – 671Combined sources5
Beta strandi677 – 679Combined sources3
Helixi691 – 696Combined sources6
Beta strandi701 – 704Combined sources4
Helixi716 – 720Combined sources5
Beta strandi726 – 728Combined sources3
Helixi741 – 744Combined sources4
Beta strandi750 – 752Combined sources3
Helixi773 – 776Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MN8X-ray3.06A25-800[»]
4MNAX-ray4.00A25-800[»]
ProteinModelPortaliQ9FL28.
SMRiQ9FL28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati97 – 119LRR 1Add BLAST23
Repeati121 – 143LRR 2Add BLAST23
Repeati145 – 167LRR 3Add BLAST23
Repeati169 – 192LRR 4Add BLAST24
Repeati193 – 215LRR 5Add BLAST23
Repeati217 – 240LRR 6Add BLAST24
Repeati241 – 263LRR 7Add BLAST23
Repeati265 – 288LRR 8Add BLAST24
Repeati289 – 311LRR 9Add BLAST23
Repeati313 – 335LRR 10Add BLAST23
Repeati337 – 359LRR 11Add BLAST23
Repeati361 – 383LRR 12Add BLAST23
Repeati385 – 407LRR 13Add BLAST23
Repeati409 – 431LRR 14Add BLAST23
Repeati432 – 454LRR 15Add BLAST23
Repeati456 – 478LRR 16Add BLAST23
Repeati480 – 503LRR 17Add BLAST24
Repeati504 – 527LRR 18Add BLAST24
Repeati528 – 550LRR 19Add BLAST23
Repeati552 – 574LRR 20Add BLAST23
Repeati576 – 599LRR 21Add BLAST24
Repeati600 – 621LRR 22Add BLAST22
Repeati627 – 649LRR 23Add BLAST23
Repeati650 – 673LRR 24Add BLAST24
Repeati674 – 696LRR 25Add BLAST23
Repeati699 – 721LRR 26Add BLAST23
Repeati723 – 746LRR 27Add BLAST24
Repeati747 – 769LRR 28Add BLAST23
Domaini870 – 1155Protein kinasePROSITE-ProRule annotationAdd BLAST286

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.
OrthoDBiEOG093601F8.
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. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti652Q → K in AAO41929 (PubMed:14593172).Curated1

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_124003.4.
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_124003.4.
UniGeneiAt.29960.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MN8X-ray3.06A25-800[»]
4MNAX-ray4.00A25-800[»]
ProteinModelPortaliQ9FL28.
SMRiQ9FL28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9FL28.
SwissPalmiQ9FL28.

Proteomic databases

PaxDbiQ9FL28.

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.
OrthoDBiEOG093601F8.
PhylomeDBiQ9FL28.

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. 1 hit.
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...

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: November 30, 2016
This is version 131 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.