FLS2_ARATH
ID FLS2_ARATH Reviewed; 1173 AA.
AC Q9FL28; Q0WVN3; Q84WF4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase FLS2;
DE EC=2.7.11.1;
DE AltName: Full=Protein FLAGELLIN-SENSING 2 {ECO:0000303|PubMed:10911994};
DE AltName: Full=Protein FLAGELLIN-SENSITIVE 2 {ECO:0000303|PubMed:10911994};
DE Flags: Precursor;
GN Name=FLS2 {ECO:0000303|PubMed:10911994};
GN OrderedLocusNames=At5g46330 {ECO:0000312|Araport:AT5G46330};
GN ORFNames=MPL12.13 {ECO:0000312|EMBL:BAB11088.1},
GN MPL12.8 {ECO:0000312|EMBL:BAB11088.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-831.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10911994; DOI=10.1016/s1097-2765(00)80265-8;
RA Gomez-Gomez L., Boller T.;
RT "FLS2: an LRR receptor-like kinase involved in the perception of the
RT bacterial elicitor flagellin in Arabidopsis.";
RL Mol. Cell 5:1003-1011(2000).
RN [6]
RP BINDING TO FLAGELLIN.
RX PubMed=11564731; DOI=10.1074/jbc.m102390200;
RA Bauer Z., Gomez-Gomez L., Boller T., Felix G.;
RT "Sensitivity of different ecotypes and mutants of Arabidopsis thaliana
RT toward the bacterial elicitor flagellin correlates with the presence of
RT receptor-binding sites.";
RL J. Biol. Chem. 276:45669-45676(2001).
RN [7]
RP FUNCTION, MUTAGENESIS OF GLY-318 AND GLY-1064, AND INTERACTION WITH KAPP.
RX PubMed=11340188; DOI=10.2307/3871370;
RA Gomez-Gomez L., Bauer Z., Boller T.;
RT "Both the extracellular leucine-rich repeat domain and the kinase activity
RT of FSL2 are required for flagellin binding and signaling in Arabidopsis.";
RL Plant Cell 13:1155-1163(2001).
RN [8]
RP FUNCTION.
RX PubMed=11875555; DOI=10.1038/415977a;
RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L.,
RA Boller T., Ausubel F.M., Sheen J.;
RT "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL Nature 415:977-983(2002).
RN [9]
RP REVIEW.
RX PubMed=12049921; DOI=10.1016/s1360-1385(02)02261-6;
RA Gomez-Gomez L., Boller T.;
RT "Flagellin perception: a paradigm for innate immunity.";
RL Trends Plant Sci. 7:251-256(2002).
RN [10]
RP FUNCTION.
RX PubMed=15085136; DOI=10.1038/nature02485;
RA Zipfel C., Robatzek S., Navarro L., Oakeley E.J., Jones J.D.G., Felix G.,
RA Boller T.;
RT "Bacterial disease resistance in Arabidopsis through flagellin
RT perception.";
RL Nature 428:764-767(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RA Robatzek S., Chinchilla D., Bauer Z., Zipfel C., Kunze G., Bittel P.,
RA Caniard A., Felix G., Boller T.;
RT "Functional analysis and expression studies of the flagellin receptor
RT FLS2.";
RL (In) Proceedings of the 15th international conference on Arabidopsis
RL research, abstract#05-086, Berlin (2004).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16510871; DOI=10.1101/gad.366506;
RA Robatzek S., Chinchilla D., Boller T.;
RT "Ligand-induced endocytosis of the pattern recognition receptor FLS2 in
RT Arabidopsis.";
RL Genes Dev. 20:537-542(2006).
RN [13]
RP FUNCTION, AND BINDING TO FLAGELLIN.
RX PubMed=16377758; DOI=10.1105/tpc.105.036574;
RA Chinchilla D., Bauer Z., Regenass M., Boller T., Felix G.;
RT "The Arabidopsis receptor kinase FLS2 binds flg22 and determines the
RT specificity of flagellin perception.";
RL Plant Cell 18:465-476(2006).
RN [14]
RP SUBUNIT.
RX PubMed=17625569; DOI=10.1038/nature05999;
RA Chinchilla D., Zipfel C., Robatzek S., Kemmerling B., Nuernberger T.,
RA Jones J.D.G., Felix G., Boller T.;
RT "A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant
RT defence.";
RL Nature 448:497-500(2007).
RN [15]
RP DOMAIN.
RX PubMed=17933906; DOI=10.1105/tpc.106.048801;
RA Dunning F.M., Sun W., Jansen K.L., Helft L., Bent A.F.;
RT "Identification and mutational analysis of Arabidopsis FLS2 leucine-rich
RT repeat domain residues that contribute to flagellin perception.";
RL Plant Cell 19:3297-3313(2007).
RN [16]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17925310; DOI=10.1093/pcp/pcm132;
RA Ali G.S., Prasad K.V.S.K., Day I., Reddy A.S.N.;
RT "Ligand-dependent reduction in the membrane mobility of FLAGELLIN
RT SENSITIVE2, an arabidopsis receptor-like kinase.";
RL Plant Cell Physiol. 48:1601-1611(2007).
RN [17]
RP INTERACTION WITH BAK1.
RX PubMed=17626179; DOI=10.1073/pnas.0705306104;
RA Heese A., Hann D.R., Gimenez-Ibanez S., Jones A.M.E., He K., Li J.,
RA Schroeder J.I., Peck S.C., Rathjen J.P.;
RT "The receptor-like kinase SERK3/BAK1 is a central regulator of innate
RT immunity in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12217-12222(2007).
RN [18]
RP INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO1, MUTAGENESIS OF LYS-898, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=18158241; DOI=10.1016/j.cub.2007.12.020;
RA Xiang T., Zong N., Zou Y., Wu Y., Zhang J., Xing W., Li Y., Tang X.,
RA Zhu L., Chai J., Zhou J.-M.;
RT "Pseudomonas syringae effector AvrPto blocks innate immunity by targeting
RT receptor kinases.";
RL Curr. Biol. 18:74-80(2008).
RN [19]
RP UBIQUITINATION BY AVRPTOB, INTERACTION WITH AVRPTOB, REPRESSION BY
RP PSEUDOMONAS SYRINGAE, AND SUBCELLULAR LOCATION.
RX PubMed=19062288; DOI=10.1016/j.cub.2008.10.063;
RA Goehre V., Spallek T., Haeweker H., Mersmann S., Mentzel T., Boller T.,
RA de Torres M., Mansfield J.W., Robatzek S.;
RT "Plant pattern-recognition receptor FLS2 is directed for degradation by the
RT bacterial ubiquitin ligase AvrPtoB.";
RL Curr. Biol. 18:1824-1832(2008).
RN [20]
RP INTERACTION WITH PBS1; BIK1; PBL1 AND PBL2.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
RN [21]
RP INTERACTION WITH BAK1, AND PHOSPHORYLATION AT THR-867.
RX PubMed=20103591; DOI=10.1074/jbc.m109.096842;
RA Schulze B., Mentzel T., Jehle A.K., Mueller K., Beeler S., Boller T.,
RA Felix G., Chinchilla D.;
RT "Rapid heteromerization and phosphorylation of ligand-activated plant
RT transmembrane receptors and their associated kinase BAK1.";
RL J. Biol. Chem. 285:9444-9451(2010).
RN [22]
RP INTERACTION WITH BSK8.
RX PubMed=21726371; DOI=10.1111/j.1364-3703.2010.00704.x;
RA Qi Y., Tsuda K., Glazebrook J., Katagiri F.;
RT "Physical association of pattern-triggered immunity (PTI) and effector-
RT triggered immunity (ETI) immune receptors in Arabidopsis.";
RL Mol. Plant Pathol. 12:702-708(2011).
RN [23]
RP INTERACTION WITH SERK3/BAK1; SERK4/BKK1; SERK1 AND SERK2.
RC STRAIN=cv. Columbia;
RX PubMed=21693696; DOI=10.1105/tpc.111.084301;
RA Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N.,
RA Malinovsky F.G., Tor M., de Vries S., Zipfel C.;
RT "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and
RT BKK1/SERK4 are required for innate immunity to hemibiotrophic and
RT biotrophic pathogens.";
RL Plant Cell 23:2440-2455(2011).
RN [24]
RP INTERACTION WITH MORC1/CRT1.
RC STRAIN=cv. Columbia;
RX PubMed=23250427; DOI=10.1038/ncomms2279;
RA Kang H.-G., Hyong W.C., von Einem S., Manosalva P., Ehlers K., Liu P.-P.,
RA Buxa S.V., Moreau M., Mang H.-G., Kachroo P., Kogel K.-H., Klessig D.F.;
RT "CRT1 is a nuclear-translocated MORC endonuclease that participates in
RT multiple levels of plant immunity.";
RL Nat. Commun. 3:1297-1297(2012).
RN [25]
RP INTERACTION WITH BSK1.
RX PubMed=23532072; DOI=10.1105/tpc.112.107904;
RA Shi H., Shen Q., Qi Y., Yan H., Nie H., Chen Y., Zhao T., Katagiri F.,
RA Tang D.;
RT "BR-SIGNALING KINASE1 physically associates with FLAGELLIN SENSING2 and
RT regulates plant innate immunity in Arabidopsis.";
RL Plant Cell 25:1143-1157(2013).
RN [26]
RP PHOSPHORYLATION AT SER-869; SER-906; SER-938; THR-941; SER-961; SER-1084
RP AND SER-1115.
RX PubMed=24104392; DOI=10.1007/s13238-013-3053-6;
RA Xu J., Wei X., Yan L., Liu D., Ma Y., Guo Y., Peng C., Zhou H., Yang C.,
RA Lou Z., Shui W.;
RT "Identification and functional analysis of phosphorylation residues of the
RT Arabidopsis BOTRYTIS-INDUCED KINASE1.";
RL Protein Cell 4:771-781(2013).
RN [27]
RP INTERACTION WITH RBOHD.
RX PubMed=24629339; DOI=10.1016/j.chom.2014.02.009;
RA Li L., Li M., Yu L., Zhou Z., Liang X., Liu Z., Cai G., Gao L., Zhang X.,
RA Wang Y., Chen S., Zhou J.M.;
RT "The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase
RT RbohD to control plant immunity.";
RL Cell Host Microbe 15:329-338(2014).
RN [28]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=24923602; DOI=10.1093/mp/ssu072;
RA Zhang Z., Shrestha J., Tateda C., Greenberg J.T.;
RT "Salicylic acid signaling controls the maturation and localization of the
RT arabidopsis defense protein ACCELERATED CELL DEATH6.";
RL Mol. Plant 7:1365-1383(2014).
RN [29]
RP FUNCTION, AND INTERACTION WITH HOPD2.
RX PubMed=24625928; DOI=10.1126/science.1248849;
RA Macho A.P., Schwessinger B., Ntoukakis V., Brutus A., Segonzac C., Roy S.,
RA Kadota Y., Oh M.H., Sklenar J., Derbyshire P., Lozano-Duran R.,
RA Malinovsky F.G., Monaghan J., Menke F.L., Huber S.C., He S.Y., Zipfel C.;
RT "A bacterial tyrosine phosphatase inhibits plant pattern recognition
RT receptor activation.";
RL Science 343:1509-1512(2014).
RN [30]
RP INTERACTION WITH IOS1.
RX PubMed=27317676; DOI=10.1105/tpc.16.00313;
RA Yeh Y.-H., Panzeri D., Kadota Y., Huang Y.-C., Huang P.-Y., Tao C.-N.,
RA Roux M., Chien H.-C., Chin T.-C., Chu P.-W., Zipfel C., Zimmerli L.;
RT "The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent
RT and BAK1-independent pattern-triggered immunity.";
RL Plant Cell 28:1701-1721(2016).
RN [31]
RP INTERACTION WITH PCRK1 AND PCRK2.
RX PubMed=27208222; DOI=10.1104/pp.15.01954;
RA Kong Q., Sun T., Qu N., Ma J., Li M., Cheng Y.T., Zhang Q., Wu D.,
RA Zhang Z., Zhang Y.;
RT "Two redundant receptor-like cytoplasmic kinases function downstream of
RT pattern recognition receptors to regulate activation of SA biosynthesis.";
RL Plant Physiol. 171:1344-1354(2016).
RN [32]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SERK3/BAK1.
RX DOI=10.1038/s41586-020-2210-3;
RA Xiyu M., Lucas A.N.C., Michelle E.L., Kai T., Zhiping W., Jun L., Xiao Y.,
RA Bo L., Jinggeng Z., Daniel V.S., Junmin P., Brett M.T., Antje H.,
RA Eugenia R., Ping H., Libo S.;
RT "Ligand-induced monoubiquitination of BIK1 regulates plant immunity.";
RL Nature 0:0-0(2020).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 25-800 IN COMPLEX WITH BAK1 AND
RP FLG22, DISULFIDE BONDS, GLYCOSYLATION AT ASN-94; ASN-217; ASN-262; ASN-361;
RP ASN-371; ASN-388; ASN-406; ASN-432; ASN-588; ASN-631 AND ASN-704, SUBUNIT,
RP AND MUTAGENESIS OF ARG-294; HIS-316; GLY-318; THR-342 AND THR-434.
RX PubMed=24114786; DOI=10.1126/science.1243825;
RA Sun Y., Li L., Macho A.P., Han Z., Hu Z., Zipfel C., Zhou J.M., Chai J.;
RT "Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1
RT immune complex.";
RL Science 342:624-628(2013).
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). Flagellin-binding to the receptor is the first step
CC to initiate the innate immune MAP kinase signaling cascade (MEKK1,
CC MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against
CC pathogens. Binding to the effector AvrPto1 or to the phosphatase hopD2
CC from Pseudomonas syringae blocks the downstream plant immune response.
CC {ECO:0000269|PubMed:10911994, ECO:0000269|PubMed:11340188,
CC ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:15085136,
CC ECO:0000269|PubMed:16377758, ECO:0000269|PubMed:24625928,
CC ECO:0000269|Ref.11}.
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: Heterodimer with SERK3/BAK1 (PubMed:24114786, PubMed:17626179,
CC PubMed:20103591, PubMed:21693696, Ref.32). The activation by flagellin
CC (flg22) induces the dissociation of the complex with SERK3/BAK1
CC (Ref.32, PubMed:20413097). Interacts with KAPP. Does not form
CC homodimer. Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a
CC specific ligand-induced manner. Interacts with P.syringae AvrPto1,
CC AvrPtoB and (via the kinase and cytoplasmic domains) hopD2. Component
CC of large complexes containing, at least, FLS2 and ACD6 in endoplasmic
CC reticulum and plasma membrane (PubMed:24923602). Interacts with
CC MORC1/CRT1 (PubMed:23250427). Interacts with PBS1, BIK1, PBL1 and PBL2
CC (PubMed:20413097). Interacts with RBOHD (PubMed:24629339). Binds to
CC IOS1 which triggers FLS2-BAK1 complex formation upon microbe-associated
CC molecular patterns (MAMPs) treatment (PubMed:27317676). Interacts with
CC PCRK1 AND PCRK2 (PubMed:27208222). Interacts with BSK1
CC (PubMed:23532072). Interaction with BSK8 (PubMed:21726371).
CC {ECO:0000269|PubMed:11340188, ECO:0000269|PubMed:17625569,
CC ECO:0000269|PubMed:17626179, ECO:0000269|PubMed:17925310,
CC ECO:0000269|PubMed:18158241, ECO:0000269|PubMed:19062288,
CC ECO:0000269|PubMed:20103591, ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:21693696, ECO:0000269|PubMed:21726371,
CC ECO:0000269|PubMed:23250427, ECO:0000269|PubMed:23532072,
CC ECO:0000269|PubMed:24114786, ECO:0000269|PubMed:24625928,
CC ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:24923602,
CC ECO:0000269|PubMed:27208222, ECO:0000269|PubMed:27317676,
CC ECO:0000269|Ref.32}.
CC -!- INTERACTION:
CC Q9FL28; Q9LFG1: At3g53590; NbExp=3; IntAct=EBI-1799448, EBI-20664191;
CC Q9FL28; Q94F62: BAK1; NbExp=19; IntAct=EBI-1799448, EBI-617138;
CC Q9FL28; O65440-2: BAM3; NbExp=2; IntAct=EBI-1799448, EBI-20653325;
CC Q9FL28; O48814: BIK1; NbExp=5; IntAct=EBI-1799448, EBI-1238176;
CC Q9FL28; Q42371: ERECTA; NbExp=2; IntAct=EBI-1799448, EBI-16940407;
CC Q9FL28; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-1799448, EBI-16895926;
CC Q9FL28; Q9FL28: FLS2; NbExp=3; IntAct=EBI-1799448, EBI-1799448;
CC Q9FL28; Q9C8I6: IOS1; NbExp=2; IntAct=EBI-1799448, EBI-16924837;
CC Q9FL28; Q8GX94: LRR-RLK; NbExp=2; IntAct=EBI-1799448, EBI-16955556;
CC Q9FL28; Q9M0G7: MIK1; NbExp=3; IntAct=EBI-1799448, EBI-16196224;
CC Q9FL28; Q03250: RBG7; NbExp=4; IntAct=EBI-1799448, EBI-1393626;
CC Q9FL28; Q9S7I6: RPK2; NbExp=2; IntAct=EBI-1799448, EBI-16940204;
CC Q9FL28; P21184: fliC; Xeno; NbExp=5; IntAct=EBI-1799448, EBI-16077660;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24923602,
CC ECO:0000269|Ref.32}; Single-pass type I membrane protein {ECO:0000255}.
CC Endosome membrane {ECO:0000269|PubMed:24923602, ECO:0000269|Ref.32};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Internalization
CC by endocytosis, especially in response to pathogen-associated molecular
CC patterns (PAMPs e.g. flg22) recognition (PubMed:24923602, Ref.32).
CC Accumulates at the plasma membrane, in an ACD6-dependent manner, in
CC response to salicylic acid (SA) signaling, thus priming defenses
CC (PubMed:24923602). {ECO:0000269|PubMed:24923602, ECO:0000269|Ref.32}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10911994}.
CC -!- INDUCTION: Repressed upon infection with the P.syringae virulent DC3000
CC strain, in a flg22- and avrPtoB-dependent manner (at protein level).
CC {ECO:0000269|PubMed:19062288}.
CC -!- DOMAIN: Both extracellular leucine-rich repeats and protein kinase
CC domains are required for flg22-binding. The LRR 9 to LRR 15 domains are
CC involved in flg22-binding. {ECO:0000269|PubMed:17933906}.
CC -!- PTM: Autophosphorylated. The phosphorylated form is essential in the
CC perception of flagellin. Dephosphorylated by KAPP. Autophosphorylation
CC is inhibited by the binding with avrPto1.
CC {ECO:0000269|PubMed:20103591}.
CC -!- PTM: Polyubiquitinated at the kinase domain mediated by P.syringae
CC AvrPtoB. {ECO:0000269|PubMed:19062288}.
CC -!- DISRUPTION PHENOTYPE: Impaired BIK1 pathogen-associated molecular
CC patterns (PAMPs e.g. flg22)-induced ubiquitination.
CC {ECO:0000269|Ref.32}.
CC -!- MISCELLANEOUS: After flg22-binding, forms instantaneously a heteromeric
CC complex with BAK1 and is transphosphorylated within 15 seconds. After
CC activation, the receptor is internalized by endocytosis and subject to
CC degradation.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB010698; BAB11088.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95370.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68238.1; -; Genomic_DNA.
DR EMBL; BT003880; AAO41929.1; -; mRNA.
DR EMBL; AK226709; BAE98815.1; -; mRNA.
DR RefSeq; NP_001330009.1; NM_001344672.1.
DR RefSeq; NP_199445.1; NM_124003.4.
DR PDB; 4MN8; X-ray; 3.06 A; A=25-800.
DR PDB; 4MNA; X-ray; 4.00 A; A=25-800.
DR PDBsum; 4MN8; -.
DR PDBsum; 4MNA; -.
DR AlphaFoldDB; Q9FL28; -.
DR SMR; Q9FL28; -.
DR BioGRID; 19925; 54.
DR DIP; DIP-46004N; -.
DR IntAct; Q9FL28; 45.
DR MINT; Q9FL28; -.
DR STRING; 3702.AT5G46330.1; -.
DR iPTMnet; Q9FL28; -.
DR SwissPalm; Q9FL28; -.
DR PaxDb; Q9FL28; -.
DR PRIDE; Q9FL28; -.
DR ProteomicsDB; 230627; -.
DR DNASU; 834676; -.
DR EnsemblPlants; AT5G46330.1; AT5G46330.1; AT5G46330.
DR EnsemblPlants; AT5G46330.2; AT5G46330.2; AT5G46330.
DR GeneID; 834676; -.
DR Gramene; AT5G46330.1; AT5G46330.1; AT5G46330.
DR Gramene; AT5G46330.2; AT5G46330.2; AT5G46330.
DR KEGG; ath:AT5G46330; -.
DR Araport; AT5G46330; -.
DR TAIR; locus:2170483; AT5G46330.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9FL28; -.
DR OMA; ALPRHCN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9FL28; -.
DR PRO; PR:Q9FL28; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL28; baseline and differential.
DR Genevisible; Q9FL28; AT.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0016045; P:detection of bacterium; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:TAIR.
DR GO; GO:0010359; P:regulation of anion channel activity; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 6.
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; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 13.
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 3D-structure; ATP-binding; Cell membrane; Disulfide bond; Endosome;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1173
FT /note="LRR receptor-like serine/threonine-protein kinase
FT FLS2"
FT /id="PRO_0000323720"
FT TOPO_DOM 24..806
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 828..1173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 97..119
FT /note="LRR 1"
FT REPEAT 121..143
FT /note="LRR 2"
FT REPEAT 145..167
FT /note="LRR 3"
FT REPEAT 169..192
FT /note="LRR 4"
FT REPEAT 193..215
FT /note="LRR 5"
FT REPEAT 217..240
FT /note="LRR 6"
FT REPEAT 241..263
FT /note="LRR 7"
FT REPEAT 265..288
FT /note="LRR 8"
FT REPEAT 289..311
FT /note="LRR 9"
FT REPEAT 313..335
FT /note="LRR 10"
FT REPEAT 337..359
FT /note="LRR 11"
FT REPEAT 361..383
FT /note="LRR 12"
FT REPEAT 385..407
FT /note="LRR 13"
FT REPEAT 409..431
FT /note="LRR 14"
FT REPEAT 432..454
FT /note="LRR 15"
FT REPEAT 456..478
FT /note="LRR 16"
FT REPEAT 480..503
FT /note="LRR 17"
FT REPEAT 504..527
FT /note="LRR 18"
FT REPEAT 528..550
FT /note="LRR 19"
FT REPEAT 552..574
FT /note="LRR 20"
FT REPEAT 576..599
FT /note="LRR 21"
FT REPEAT 600..621
FT /note="LRR 22"
FT REPEAT 627..649
FT /note="LRR 23"
FT REPEAT 650..673
FT /note="LRR 24"
FT REPEAT 674..696
FT /note="LRR 25"
FT REPEAT 699..721
FT /note="LRR 26"
FT REPEAT 723..746
FT /note="LRR 27"
FT REPEAT 747..769
FT /note="LRR 28"
FT DOMAIN 870..1155
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 997
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 876..884
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 898
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 148
FT /note="Interacts with flagellin flg22"
FT /evidence="ECO:0000269|PubMed:24114786"
FT SITE 152
FT /note="Interacts with flagellin flg22"
FT /evidence="ECO:0000269|PubMed:24114786"
FT SITE 272
FT /note="Interacts with flagellin flg22"
FT /evidence="ECO:0000269|PubMed:24114786"
FT SITE 296
FT /note="Interacts with flagellin flg22"
FT /evidence="ECO:0000269|PubMed:24114786"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:20103591"
FT MOD_RES 869
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 906
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 941
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 961
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 984
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1043
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1050
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 1115
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24104392"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MNA"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8, ECO:0007744|PDB:4MNA"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MNA"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MNA"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24114786,
FT ECO:0007744|PDB:4MN8, ECO:0007744|PDB:4MNA"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..68
FT /evidence="ECO:0000269|PubMed:24114786"
FT DISULFID 165..187
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 294
FT /note="R->A: Abolishes flagellin-binding."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 316
FT /note="H->A: Abolishes flagellin-binding."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 318
FT /note="G->R: In fls2-24; abolishes flagellin-binding."
FT /evidence="ECO:0000269|PubMed:11340188,
FT ECO:0000269|PubMed:24114786"
FT MUTAGEN 342
FT /note="T->Y: Abolishes flagellin-binding."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 434
FT /note="T->Y: No effect on flagellin-binding."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 867
FT /note="T->V: Abolishes flagellin-dependent signaling and
FT reduces ligand-receptor internalization."
FT MUTAGEN 898
FT /note="K->H: Loss of binding with avrPto."
FT /evidence="ECO:0000269|PubMed:18158241"
FT MUTAGEN 1040
FT /note="T->A: Abolishes flagellin-dependent signaling."
FT MUTAGEN 1064
FT /note="G->R: In fls2-17; abolishes kinase activity and
FT strongly reduces flagellin-binding."
FT /evidence="ECO:0000269|PubMed:11340188"
FT CONFLICT 652
FT /note="Q -> K (in Ref. 3; AAO41929)"
FT /evidence="ECO:0000305"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:4MN8"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 449..453
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 473..477
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 545..549
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 569..573
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 617..622
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 667..671
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 691..696
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 701..704
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 716..720
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 773..776
FT /evidence="ECO:0007829|PDB:4MN8"
SQ SEQUENCE 1173 AA; 128824 MW; 6AF93B467A339359 CRC64;
MKLLSKTFLI LTLTFFFFGI ALAKQSFEPE IEALKSFKNG ISNDPLGVLS DWTIIGSLRH
CNWTGITCDS TGHVVSVSLL EKQLEGVLSP AIANLTYLQV LDLTSNSFTG KIPAEIGKLT
ELNQLILYLN YFSGSIPSGI WELKNIFYLD LRNNLLSGDV PEEICKTSSL VLIGFDYNNL
TGKIPECLGD LVHLQMFVAA GNHLTGSIPV SIGTLANLTD LDLSGNQLTG KIPRDFGNLL
NLQSLVLTEN LLEGDIPAEI GNCSSLVQLE LYDNQLTGKI PAELGNLVQL QALRIYKNKL
TSSIPSSLFR LTQLTHLGLS ENHLVGPISE EIGFLESLEV LTLHSNNFTG EFPQSITNLR
NLTVLTVGFN NISGELPADL GLLTNLRNLS AHDNLLTGPI PSSISNCTGL KLLDLSHNQM
TGEIPRGFGR MNLTFISIGR NHFTGEIPDD IFNCSNLETL SVADNNLTGT LKPLIGKLQK
LRILQVSYNS LTGPIPREIG NLKDLNILYL HSNGFTGRIP REMSNLTLLQ GLRMYSNDLE
GPIPEEMFDM KLLSVLDLSN NKFSGQIPAL FSKLESLTYL SLQGNKFNGS IPASLKSLSL
LNTFDISDNL LTGTIPGELL ASLKNMQLYL NFSNNLLTGT IPKELGKLEM VQEIDLSNNL
FSGSIPRSLQ ACKNVFTLDF SQNNLSGHIP DEVFQGMDMI ISLNLSRNSF SGEIPQSFGN
MTHLVSLDLS SNNLTGEIPE SLANLSTLKH LKLASNNLKG HVPESGVFKN INASDLMGNT
DLCGSKKPLK PCTIKQKSSH FSKRTRVILI ILGSAAALLL VLLLVLILTC CKKKEKKIEN
SSESSLPDLD SALKLKRFEP KELEQATDSF NSANIIGSSS LSTVYKGQLE DGTVIAVKVL
NLKEFSAESD KWFYTEAKTL SQLKHRNLVK ILGFAWESGK TKALVLPFME NGNLEDTIHG
SAAPIGSLLE KIDLCVHIAS GIDYLHSGYG FPIVHCDLKP ANILLDSDRV AHVSDFGTAR
ILGFREDGST TASTSAFEGT IGYLAPEFAY MRKVTTKADV FSFGIIMMEL MTKQRPTSLN
DEDSQDMTLR QLVEKSIGNG RKGMVRVLDM ELGDSIVSLK QEEAIEDFLK LCLFCTSSRP
EDRPDMNEIL THLMKLRGKA NSFREDRNED REV
