FLS2_ORYSJ
ID FLS2_ORYSJ Reviewed; 1183 AA.
AC Q0JA29; A3AXG7; Q7XS37;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase FLS2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein FLAGELLIN-SENSING 2 homolog {ECO:0000305};
DE Short=OsFLS2 {ECO:0000303|PubMed:18986259};
DE AltName: Full=Protein FLAGELLIN-SENSITIVE 2 homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=FLS2 {ECO:0000303|PubMed:18986259};
GN OrderedLocusNames=Os04g0618700 {ECO:0000312|EMBL:BAF15808.1},
GN LOC_Os04g52780 {ECO:0000305};
GN ORFNames=OsJ_16186 {ECO:0000312|EMBL:EAZ32006.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION.
RX PubMed=18986259; DOI=10.1094/mpmi-21-12-1635;
RA Takai R., Isogai A., Takayama S., Che F.S.;
RT "Analysis of flagellin perception mediated by flg22 receptor OsFLS2 in
RT rice.";
RL Mol. Plant Microbe Interact. 21:1635-1642(2008).
RN [7]
RP INDUCTION BY FLAGELLIN.
RX PubMed=22968716; DOI=10.1105/tpc.112.101972;
RA Ding B., Bellizzi M.R., Ning Y., Meyers B.C., Wang G.L.;
RT "HDT701, a histone H4 deacetylase, negatively regulates plant innate
RT immunity by modulating histone H4 acetylation of defense-related genes in
RT rice.";
RL Plant Cell 24:3783-3794(2012).
RN [8]
RP INTERACTION WITH SERK2.
RX PubMed=24482436; DOI=10.1093/mp/ssu003;
RA Chen X., Zuo S., Schwessinger B., Chern M., Canlas P.E., Ruan D., Zhou X.,
RA Wang J., Daudi A., Petzold C.J., Heazlewood J.L., Ronald P.C.;
RT "An XA21-associated kinase (OsSERK2) regulates immunity mediated by the
RT XA21 and XA3 immune receptors.";
RL Mol. Plant 7:874-892(2014).
RN [9]
RP FUNCTION.
RX PubMed=25617720; DOI=10.1016/j.molp.2015.01.012;
RA Wang S., Sun Z., Wang H., Liu L., Lu F., Yang J., Zhang M., Zhang S.,
RA Guo Z., Bent A.F., Sun W.;
RT "Rice OsFLS2-mediated perception of bacterial flagellins is evaded by
RT Xanthomonas oryzae pvs. oryzae and oryzicola.";
RL Mol. Plant 8:1024-1037(2015).
CC -!- FUNCTION: Constitutes the pattern-recognition receptor (PPR) that
CC determines the specific perception of flagellin (flg22), a potent
CC elicitor of the defense response to pathogen-associated molecular
CC patterns (PAMPs). Recognizes flg22 from Pseudomonas aeruginosa and
CC Acidovorax avenae. flg22 is a peptide derived from the bacterial
CC flagellin N-terminus sequence (PubMed:18986259, PubMed:25617720). Does
CC not recognize flg22 from Xanthomonas oryzae pv. oryzae (Xoo) or
CC Xanthomonas oryzae pv. oryzicola (Xoc) (PubMed:25617720).
CC {ECO:0000269|PubMed:18986259, ECO:0000269|PubMed:25617720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with SERK2. {ECO:0000269|PubMed:24482436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced by flagellin (flg22). {ECO:0000269|PubMed:22968716}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE02151.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAZ32006.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL662970; CAE02151.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP008210; BAF15808.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91038.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ32006.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015634951.1; XM_015779465.1.
DR AlphaFoldDB; Q0JA29; -.
DR SMR; Q0JA29; -.
DR STRING; 4530.OS04T0618700-01; -.
DR PaxDb; Q0JA29; -.
DR PRIDE; Q0JA29; -.
DR EnsemblPlants; Os04t0618700-01; Os04t0618700-01; Os04g0618700.
DR GeneID; 4337016; -.
DR Gramene; Os04t0618700-01; Os04t0618700-01; Os04g0618700.
DR KEGG; osa:4337016; -.
DR eggNOG; ENOG502QTTB; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q0JA29; -.
DR OMA; ALPRHCN; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005768; C:endosome; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IEA:EnsemblPlants.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0016045; P:detection of bacterium; IEA:EnsemblPlants.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:EnsemblPlants.
DR GO; GO:0010359; P:regulation of anion channel activity; IEA:EnsemblPlants.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 15.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1183
FT /note="LRR receptor-like serine/threonine-protein kinase
FT FLS2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441258"
FT TOPO_DOM 42..809
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 831..1183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 97..120
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 121..145
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 147..169
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 171..193
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 194..217
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 218..241
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 242..265
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 267..289
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 290..313
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 315..337
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 338..361
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 363..385
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 386..409
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 433..457
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 459..480
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 481..505
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 507..529
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 530..553
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 555..577
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 578..600
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 601..625
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 627..651
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 652..675
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 676..699
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 701..724
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 725..748
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 749..773
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT DOMAIN 876..1179
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1013
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 882..890
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 87..94
FT /evidence="ECO:0000250|UniProtKB:Q9FL28"
FT DISULFID 167..189
FT /evidence="ECO:0000250|UniProtKB:Q9FL28"
FT CONFLICT 1168
FT /note="A -> P (in Ref. 5; EAZ32006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1183 AA; 124752 MW; C1843DC53A8869FE CRC64;
MERNKFASKM SQHYTKTICI AVVLVAVLFS LSSAAAAGSG AAVSVQLEAL LEFKNGVADD
PLGVLAGWRV GKSGDGAVRG GALPRHCNWT GVACDGAGQV TSIQLPESKL RGALSPFLGN
ISTLQVIDLT SNAFAGGIPP QLGRLGELEQ LVVSSNYFAG GIPSSLCNCS AMWALALNVN
NLTGAIPSCI GDLSNLEIFE AYLNNLDGEL PPSMAKLKGI MVVDLSCNQL SGSIPPEIGD
LSNLQILQLY ENRFSGHIPR ELGRCKNLTL LNIFSNGFTG EIPGELGELT NLEVMRLYKN
ALTSEIPRSL RRCVSLLNLD LSMNQLAGPI PPELGELPSL QRLSLHANRL AGTVPASLTN
LVNLTILELS ENHLSGPLPA SIGSLRNLRR LIVQNNSLSG QIPASISNCT QLANASMSFN
LFSGPLPAGL GRLQSLMFLS LGQNSLAGDI PDDLFDCGQL QKLDLSENSF TGGLSRLVGQ
LGNLTVLQLQ GNALSGEIPE EIGNMTKLIS LKLGRNRFAG HVPASISNMS SLQLLDLGHN
RLDGVFPAEV FELRQLTILG AGSNRFAGPI PDAVANLRSL SFLDLSSNML NGTVPAALGR
LDQLLTLDLS HNRLAGAIPG AVIASMSNVQ MYLNLSNNAF TGAIPAEIGG LVMVQTIDLS
NNQLSGGVPA TLAGCKNLYS LDLSGNSLTG ELPANLFPQL DLLTTLNISG NDLDGEIPAD
IAALKHIQTL DVSRNAFAGA IPPALANLTA LRSLNLSSNT FEGPVPDGGV FRNLTMSSLQ
GNAGLCGGKL LAPCHGHAAG KKRVFSRTGL VILVVLIALS TLLLLMVATI LLVSYRRYRR
KRRAADIAGD SPEAAVVVPE LRRFSYGQLA AATNSFDQGN VIGSSNLSTV YKGVLAGDAD
GGMVVAVKRL NLEQFPSKSD KCFLTELATL SRLRHKNLAR VVGYAWEAGK IKALVLDYMV
NGDLDGAIHG GAAAPPPAPS RWTVRERLRV CVSVAHGLVY LHSGYDFPVV HCDVKPSNVL
LDGDWEARVS DFGTARMLGV HLPAAANAAA QSTATSSAFR GTVGYMAPEF AYMRTVSTKV
DVFSFGVLAM ELFTGRRPTG TIEEDGVPLT LQQLVDNAVS RGLDGVHAVL DPRMKVATEA
DLSTAADVLA VALSCAAFEP ADRPDMGAVL SSLLKMSKLV GED
