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		<id>http://192.168.164.12:81/ricewiki/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Duweili13</id>
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	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175586</id>
		<title>OsCERK1</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175586"/>
				<updated>2014-06-01T10:31:40Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
*Rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown ofOsCERK1resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice.&lt;br /&gt;
*The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1.&lt;br /&gt;
*Our studies show that chitin, chitin oligomers, and chitosan rapidly induce in vivophosphorylation &lt;br /&gt;
of CERK1 at multiple residues in the juxtamembrane and kinase domain. Functional analyses with a kinase dead variant provide evidence that kinase activity of CERK1 is required for its chitin-dependent in vivophosphorylation, as well as for early defense responses and downstream signaling.&lt;br /&gt;
*The CERK1 ectodomain binds chitin and partially deacetylated chitosan directly without any&lt;br /&gt;
requirement for interacting proteins and that all three LysM domains are necessary for chitin binding.&lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
*OsLysM-RLK9(designated OsCERK1hereafter) encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain. Motif analysis indicated the presence of one LysM motif in the OsCERK1 extracellular domain, while CERK1 contained three LysM motifs in its extracellular domain (Miya et al., 2007). &lt;br /&gt;
*In the LysM motif of OsCERK1, 54.8% of the amino acid residues were identical to those of the third LysM motif (LysM3, 42 amino acids) of CERK1 . Interestingly, the corresponding regions of the amino acid sequence of the OsCERK1 extracellular domain also showed significant similarity with the other two LysM motifs of CERK1; 24.5% identity with LysM1 and 43% with LysM2 . However, these regions in OsCERK1 were not identified as LysM motifs by the motif database analysis. The amino acid sequence of the intracellular Ser/Thr kinase domain of OsCERK1 showed a very high similarity with that of CERK1,with 64% identical residues.&lt;br /&gt;
*OsCERK1was expressed in all tissues tested, with weak expression in the flowers . Interestingly, the expression pattern ofOsCERK1in plants was very similar to that of CEBiP, except for the weak expression &lt;br /&gt;
in the flowers (Kakuet al., 2006).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
===Expression===&lt;br /&gt;
*Three RNAiOsCERK1knockdown cell lines were generated to investigate the function of OsCERK1. Transcriptional analyses of the knockdown cell lines showed that expression ofOsCERK1was markedly &lt;br /&gt;
reduced but expression of the otherOsLysM-RLKgenes and theCEBiPgene was not affected in these cell &lt;br /&gt;
lines.&lt;br /&gt;
*Chitin oligosaccharide elicitor is known to induce biphasic generation of reactive oxygen species &lt;br /&gt;
(ROS) in rice suspension cell cultures. The first peak of ROS at approximately 30 min after elicitor treatment does not require protein synthesis, but the latter peak at approximately 2 h does require protein synthesis (Yamaguchi et al., 2005). &lt;br /&gt;
*Both peaks of chitin oligosaccharide-induced ROS generation were markedly decreased in allOsCERK1-RNAi cell lines compared to vector control (VC) cells. On the other hand, ROS generation induced by a bacterial lipopolysaccharide (LPS) (Desakiet al., 2006) was not affected in these OsCERK1-RNAi cell lines , although the amount of ROS accumulated varied between the cell lines.&lt;br /&gt;
*These results indicate that knockdown ofOsCERK1specifically affected the chitin-induced ROS generation of rice cells.&lt;br /&gt;
*Here, we identified a receptor-like kinase, designated CERK1, which is essential for chitin elicitor signaling in Arabidopsis. The KO mutants for CERK1 completely lost the ability to respond to the chitin elicitor, including MAPK activation, reactive oxygen species generation, and gene expression. Disease resistance of the KO mutant against an incompatible fungus, Alternaria brassicicola, was partly impaired. Complementation with the WT CERK1 gene showed cerk1 mutations were responsible for the mutant phenotypes.&lt;br /&gt;
&lt;br /&gt;
===Catalytic activity===&lt;br /&gt;
ATP + a protein = ADP + a phosphoprotein.&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Life Sciences; 1-1-1 Higashi-Mita, Tama-ku, Kawasaki,Kanagawa 214-8571, Japan&lt;br /&gt;
*The Sainsbury Laboratory, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom&lt;br /&gt;
*Department of Plant Cell Biology, Albrecht-von-Haller-Institute of Plant Sciences, Georg-August-University Goettingen, Untere Karspuele 2, D-37073 Goettingen, Germany&lt;br /&gt;
*Department of Life Sciences, Faculty of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa214-8571, Japan,&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
*Nürnberger T., Kemmerling B. (2006) Trends Plant Sci. 11, 519–522 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Boller T., Felix G. (2009) Annu. Rev. Plant Biol. 60, 379–406 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Kim, T.W. and Wang, Z.Y.(2010) Brassinosteroid signal transduction from receptor kinases to transcription factors.Annu. Rev. Plant Biol.61, 681–704.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = OsCERK1|&lt;br /&gt;
Description =LysM receptor-like kinase |&lt;br /&gt;
Version = |&lt;br /&gt;
Length =  bp|&lt;br /&gt;
Definition = chitin elicitor receptor kinase|&lt;br /&gt;
Chromosome = Chromosome |&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Japonica Group&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175585</id>
		<title>OsCERK1</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175585"/>
				<updated>2014-06-01T10:30:26Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
*Rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown ofOsCERK1resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice.&lt;br /&gt;
*The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1.&lt;br /&gt;
*Our studies show that chitin, chitin oligomers, and chitosan rapidly induce in vivophosphorylation &lt;br /&gt;
of CERK1 at multiple residues in the juxtamembrane and kinase domain. Functional analyses with a kinase dead variant provide evidence that kinase activity of CERK1 is required for its chitin-dependent in vivophosphorylation, as well as for early defense responses and downstream signaling.&lt;br /&gt;
*The CERK1 ectodomain binds chitin and partially deacetylated chitosan directly without any&lt;br /&gt;
requirement for interacting proteins and that all three LysM domains are necessary for chitin binding.&lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
*OsLysM-RLK9(designated OsCERK1hereafter) encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain. Motif analysis indicated the presence of one LysM motif in the OsCERK1 extracellular domain, while CERK1 contained three LysM motifs in its extracellular domain (Miya et al., 2007). &lt;br /&gt;
*In the LysM motif of OsCERK1, 54.8% of the amino acid residues were identical to those of the third LysM motif (LysM3, 42 amino acids) of CERK1 . Interestingly, the corresponding regions of the amino acid sequence of the OsCERK1 extracellular domain also showed significant similarity with the other two LysM motifs of CERK1; 24.5% identity with LysM1 and 43% with LysM2 . However, these regions in OsCERK1 were not identified as LysM motifs by the motif database analysis. The amino acid sequence of the intracellular Ser/Thr kinase domain of OsCERK1 showed a very high similarity with that of CERK1,with 64% identical residues.&lt;br /&gt;
*OsCERK1was expressed in all tissues tested, with weak expression in the flowers . Interestingly, the expression pattern ofOsCERK1in plants was very similar to that of CEBiP, except for the weak expression &lt;br /&gt;
in the flowers (Kakuet al., 2006).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
===Expression===&lt;br /&gt;
*Three RNAiOsCERK1knockdown cell lines were generated to investigate the function of OsCERK1. Transcriptional analyses of the knockdown cell lines showed that expression ofOsCERK1was markedly &lt;br /&gt;
reduced but expression of the otherOsLysM-RLKgenes and theCEBiPgene was not affected in these cell &lt;br /&gt;
lines.&lt;br /&gt;
*Chitin oligosaccharide elicitor is known to induce biphasic generation of reactive oxygen species &lt;br /&gt;
(ROS) in rice suspension cell cultures. The first peak of ROS at approximately 30 min after elicitor treatment does not require protein synthesis, but the latter peak at approximately 2 h does&lt;br /&gt;
require protein synthesis (Yamaguchi et al., 2005). &lt;br /&gt;
*Both peaks of chitin oligosaccharide-induced ROS generation were markedly decreased in allOsCERK1-RNAi cell lines compared to vector control (VC) cells. On the other hand, ROS generation induced&lt;br /&gt;
 by a bacterial lipopolysaccharide (LPS) (Desakiet al., 2006) was not affected in these OsCERK1-RNAi cell lines , although the amount of ROS accumulated varied between the cell lines.&lt;br /&gt;
*These results indicate that knockdown ofOsCERK1specifically affected the chitin-induced ROS generation &lt;br /&gt;
of rice cells.&lt;br /&gt;
*Here, we identified a receptor-like kinase, designated CERK1, which is essential for chitin elicitor signaling in Arabidopsis. The KO mutants for CERK1 completely lost the ability to respond to the chitin elicitor, including MAPK activation, reactive oxygen species generation, and gene expression. Disease resistance of the KO mutant against an incompatible fungus, Alternaria brassicicola, was partly impaired. Complementation with the WT CERK1 gene showed cerk1 mutations were responsible for the mutant phenotypes.&lt;br /&gt;
&lt;br /&gt;
===Catalytic activity===&lt;br /&gt;
ATP + a protein = ADP + a phosphoprotein.&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Life Sciences; 1-1-1 Higashi-Mita, Tama-ku, Kawasaki,Kanagawa 214-8571, Japan&lt;br /&gt;
*The Sainsbury Laboratory, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom&lt;br /&gt;
*Department of Plant Cell Biology, Albrecht-von-Haller-Institute of Plant Sciences, Georg-August-University Goettingen, Untere Karspuele 2, D-37073 Goettingen, Germany&lt;br /&gt;
*Department of Life Sciences, Faculty of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa214-8571, Japan,&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
*Nürnberger T., Kemmerling B. (2006) Trends Plant Sci. 11, 519–522 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Boller T., Felix G. (2009) Annu. Rev. Plant Biol. 60, 379–406 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Kim, T.W. and Wang, Z.Y.(2010) Brassinosteroid signal transduction from receptor kinases to transcription factors.Annu. Rev. Plant Biol.61, 681–704.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = OsCERK1|&lt;br /&gt;
Description =LysM receptor-like kinase |&lt;br /&gt;
Version = |&lt;br /&gt;
Length =  bp|&lt;br /&gt;
Definition = chitin elicitor receptor kinase|&lt;br /&gt;
Chromosome = Chromosome |&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Japonica Group&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175383</id>
		<title>OsCERK1</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175383"/>
				<updated>2014-06-01T06:33:09Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
*Rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown ofOsCERK1resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice.&lt;br /&gt;
*The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to &lt;br /&gt;
form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells &lt;br /&gt;
treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1.&lt;br /&gt;
*Our studies show that chitin, chitin oligomers, and chitosan rapidly induce in vivophosphorylation &lt;br /&gt;
of CERK1 at multiple residues in the juxtamembrane and kinase domain. Functional analyses with a kinase dead variant provide evidence that kinase activity of CERK1 is required for its chitin-dependent in vivophosphorylation, as well as for early defense responses and downstream signaling.&lt;br /&gt;
*The CERK1 ectodomain binds chitin and partially deacetylated chitosan directly without any&lt;br /&gt;
requirement for interacting proteins and that all three LysM domains are necessary for chitin binding.&lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
*OsLysM-RLK9(designated OsCERK1hereafter) encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain. Motif analysis indicated the presence of one LysM motif in the OsCERK1 extracellular domain, while CERK1 contained three LysM motifs in its extracellular domain &lt;br /&gt;
(Miya et al., 2007). &lt;br /&gt;
*In the LysM motif of OsCERK1, 54.8% of the amino acid residues were identical to those of the third&lt;br /&gt;
 LysM motif (LysM3, 42 amino acids) of CERK1 . Interestingly, the corresponding regions of the amino &lt;br /&gt;
acid sequence of the OsCERK1 extracellular domain also showed significant similarity with the other &lt;br /&gt;
two LysM motifs of CERK1; 24.5% identity with LysM1 and 43% with LysM2 . However, these regions in &lt;br /&gt;
OsCERK1 were not identified as LysM motifs by the motif database analysis. The amino acid sequence of&lt;br /&gt;
 the intracellular Ser/Thr kinase domain of OsCERK1 showed a very high similarity with that of CERK1,&lt;br /&gt;
 with 64% identical residues.&lt;br /&gt;
*OsCERK1was expressed in all tissues tested, with weak expression in the flowers . Interestingly, the expression pattern ofOsCERK1in plants was very similar to that of CEBiP, except for the weak expression &lt;br /&gt;
in the flowers (Kakuet al., 2006).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
===Expression===&lt;br /&gt;
*Three RNAiOsCERK1knockdown cell lines were generated to investigate the function of OsCERK1. Transcriptional analyses of the knockdown cell lines showed that expression ofOsCERK1was markedly &lt;br /&gt;
reduced but expression of the otherOsLysM-RLKgenes and theCEBiPgene was not affected in these cell &lt;br /&gt;
lines.&lt;br /&gt;
*Chitin oligosaccharide elicitor is known to induce biphasic generation of reactive oxygen species &lt;br /&gt;
(ROS) in rice suspension cell cultures. The first peak of ROS at approximately 30 min after elicitor treatment does not require protein synthesis, but the latter peak at approximately 2 h does&lt;br /&gt;
require protein synthesis (Yamaguchi et al., 2005). &lt;br /&gt;
*Both peaks of chitin oligosaccharide-induced ROS generation were markedly decreased in allOsCERK1-RNAi cell lines compared to vector control (VC) cells. On the other hand, ROS generation induced&lt;br /&gt;
 by a bacterial lipopolysaccharide (LPS) (Desakiet al., 2006) was not affected in these OsCERK1-RNAi cell lines , although the amount of ROS accumulated varied between the cell lines.&lt;br /&gt;
*These results indicate that knockdown ofOsCERK1specifically affected the chitin-induced ROS generation &lt;br /&gt;
of rice cells.&lt;br /&gt;
*Here, we identified a receptor-like kinase, designated CERK1, which is essential for chitin elicitor signaling in Arabidopsis. The KO mutants for CERK1 completely lost the ability to respond to the chitin elicitor, including MAPK activation, reactive oxygen species generation, and gene expression. Disease resistance of the KO mutant against an incompatible fungus, Alternaria brassicicola, was partly impaired. Complementation with the WT CERK1 gene showed cerk1 mutations were responsible for the mutant phenotypes.&lt;br /&gt;
&lt;br /&gt;
===Catalytic activity===&lt;br /&gt;
ATP + a protein = ADP + a phosphoprotein.&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Life Sciences; 1-1-1 Higashi-Mita, Tama-ku, Kawasaki,Kanagawa 214-8571, Japan&lt;br /&gt;
*The Sainsbury Laboratory, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom&lt;br /&gt;
*Department of Plant Cell Biology, Albrecht-von-Haller-Institute of Plant Sciences, Georg-August-University Goettingen, Untere Karspuele 2, D-37073 Goettingen, Germany&lt;br /&gt;
*Department of Life Sciences, Faculty of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa214-8571, Japan,&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
*Nürnberger T., Kemmerling B. (2006) Trends Plant Sci. 11, 519–522 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Boller T., Felix G. (2009) Annu. Rev. Plant Biol. 60, 379–406 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Kim, T.W. and Wang, Z.Y.(2010) Brassinosteroid signal transduction from receptor kinases to transcription factors.Annu. Rev. Plant Biol.61, 681–704.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = OsCERK1|&lt;br /&gt;
Description =LysM receptor-like kinase |&lt;br /&gt;
Version = |&lt;br /&gt;
Length =  bp|&lt;br /&gt;
Definition = chitin elicitor receptor kinase|&lt;br /&gt;
Chromosome = Chromosome |&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Japonica Group&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175382</id>
		<title>OsCERK1</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175382"/>
				<updated>2014-06-01T06:32:08Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
*Rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown ofOsCERK1resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice.&lt;br /&gt;
*The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to &lt;br /&gt;
form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells &lt;br /&gt;
treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1.&lt;br /&gt;
*Our studies show that chitin, chitin oligomers, and chitosan rapidly induce in vivophosphorylation &lt;br /&gt;
of CERK1 at multiple residues in the juxtamembrane and kinase domain. Functional analyses with a kinase dead variant provide evidence that kinase activity of CERK1 is required for its chitin-dependent in vivophosphorylation, as well as for early defense responses and downstream signaling.&lt;br /&gt;
*The CERK1 ectodomain binds chitin and partially deacetylated chitosan directly without any&lt;br /&gt;
requirement for interacting proteins and that all three LysM domains are necessary for chitin binding.&lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
*OsLysM-RLK9(designated OsCERK1hereafter) encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain. Motif analysis indicated the presence of one LysM motif in the OsCERK1 extracellular domain, while CERK1 contained three LysM motifs in its extracellular domain &lt;br /&gt;
(Miya et al., 2007). &lt;br /&gt;
*In the LysM motif of OsCERK1, 54.8% of the amino acid residues were identical to those of the third&lt;br /&gt;
 LysM motif (LysM3, 42 amino acids) of CERK1 . Interestingly, the corresponding regions of the amino &lt;br /&gt;
acid sequence of the OsCERK1 extracellular domain also showed significant similarity with the other &lt;br /&gt;
two LysM motifs of CERK1; 24.5% identity with LysM1 and 43% with LysM2 . However, these regions in &lt;br /&gt;
OsCERK1 were not identified as LysM motifs by the motif database analysis. The amino acid sequence of&lt;br /&gt;
 the intracellular Ser/Thr kinase domain of OsCERK1 showed a very high similarity with that of CERK1,&lt;br /&gt;
 with 64% identical residues.&lt;br /&gt;
*OsCERK1was expressed in all tissues tested, with weak expression in the flowers . Interestingly, the expression pattern ofOsCERK1in plants was very similar to that of CEBiP, except for the weak expression &lt;br /&gt;
in the flowers (Kakuet al., 2006).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
===Expression===&lt;br /&gt;
*Three RNAiOsCERK1knockdown cell lines were generated to investigate the function of OsCERK1. Transcriptional analyses of the knockdown cell lines showed that expression ofOsCERK1was markedly &lt;br /&gt;
reduced but expression of the otherOsLysM-RLKgenes and theCEBiPgene was not affected in these cell &lt;br /&gt;
lines.&lt;br /&gt;
*Chitin oligosaccharide elicitor is known to induce biphasic generation of reactive oxygen species &lt;br /&gt;
(ROS) in rice suspension cell cultures. The first peak of ROS at approximately 30 min after elicitor treatment does not require protein synthesis, but the latter peak at approximately 2 h does&lt;br /&gt;
require protein synthesis (Yamaguchi et al., 2005). &lt;br /&gt;
*Both peaks of chitin oligosaccharide-induced ROS generation were markedly decreased in allOsCERK1-RNAi cell lines compared to vector control (VC) cells (Figure 2c). On the other hand, ROS generation induced&lt;br /&gt;
 by a bacterial lipopolysaccharide (LPS) (Desakiet al., 2006) was not affected in these OsCERK1-RNAi cell lines (Figure 2d), although the amount of ROS accumulated varied between the cell lines.&lt;br /&gt;
*These results indicate that knockdown ofOsCERK1specifically affected the chitin-induced ROS generation &lt;br /&gt;
of rice cells.&lt;br /&gt;
*Here, we identified a receptor-like kinase, designated CERK1, which is essential for chitin elicitor signaling in Arabidopsis. The KO mutants for CERK1 completely lost the ability to respond to the chitin elicitor, including MAPK activation, reactive oxygen species generation, and gene expression. Disease resistance of the KO mutant against an incompatible fungus, Alternaria brassicicola, was partly impaired. Complementation with the WT CERK1 gene showed cerk1 mutations were responsible for the mutant phenotypes.&lt;br /&gt;
&lt;br /&gt;
===Catalytic activity===&lt;br /&gt;
ATP + a protein = ADP + a phosphoprotein.&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Life Sciences; 1-1-1 Higashi-Mita, Tama-ku, Kawasaki,Kanagawa 214-8571, Japan&lt;br /&gt;
*The Sainsbury Laboratory, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom&lt;br /&gt;
*Department of Plant Cell Biology, Albrecht-von-Haller-Institute of Plant Sciences, Georg-August-University Goettingen, Untere Karspuele 2, D-37073 Goettingen, Germany&lt;br /&gt;
*Department of Life Sciences, Faculty of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa214-8571, Japan,&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
*Nürnberger T., Kemmerling B. (2006) Trends Plant Sci. 11, 519–522 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Boller T., Felix G. (2009) Annu. Rev. Plant Biol. 60, 379–406 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Kim, T.W. and Wang, Z.Y.(2010) Brassinosteroid signal transduction from receptor kinases to transcription factors.Annu. Rev. Plant Biol.61, 681–704.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = OsCERK1|&lt;br /&gt;
Description =LysM receptor-like kinase |&lt;br /&gt;
Version = |&lt;br /&gt;
Length =  bp|&lt;br /&gt;
Definition = chitin elicitor receptor kinase|&lt;br /&gt;
Chromosome = Chromosome |&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Japonica Group&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175377</id>
		<title>OsCERK1</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=OsCERK1&amp;diff=175377"/>
				<updated>2014-06-01T06:29:33Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: Created page with &amp;quot;==Annotated Information== ===Function=== Rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown ofOsCERK1resulted in ma...&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
Rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown ofOsCERK1resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice.&lt;br /&gt;
The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1.&lt;br /&gt;
Our studies show that chitin, chitin oligomers, and chitosan rapidly induce in vivophosphorylation of CERK1 at multiple residues in the juxtamembrane and kinase domain. Functional analyses with a kinase dead variant provide evidence that kinase activity of CERK1 is required for its chitin-dependent in vivophosphorylation, as well as for early defense responses and downstream signaling.&lt;br /&gt;
The CERK1 ectodomain binds chitin and partially deacetylated chitosan directly without any&lt;br /&gt;
requirement for interacting proteins and that all three LysM domains are necessary for chitin binding.&lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
OsLysM-RLK9(designated OsCERK1hereafter) encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain. Motif analysis indicated the presence of one LysM motif in the OsCERK1 extracellular domain, while CERK1 contained three LysM motifs in its extracellular domain (Miya et al., 2007). &lt;br /&gt;
In the LysM motif of OsCERK1, 54.8% of the amino acid residues were identical to those of the third LysM motif (LysM3, 42 amino acids) of CERK1 . Interestingly, the corresponding regions of the amino acid sequence of the OsCERK1 extracellular domain also showed significant similarity with the other two LysM motifs of CERK1; 24.5% identity with LysM1 and 43% with LysM2 . However, these regions in OsCERK1 were not identified as LysM motifs by the motif database analysis. The amino acid sequence of the intracellular Ser/Thr kinase domain of OsCERK1 showed a very high similarity with that of CERK1, with 64% identical residues.&lt;br /&gt;
OsCERK1was expressed in all tissues tested, with weak expression in the flowers . Interestingly, the expression pattern ofOsCERK1in plants was very similar to that of CEBiP, except for the weak expression in the flowers (Kakuet al., 2006).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
===Expression===&lt;br /&gt;
Three RNAiOsCERK1knockdown cell lines were generated to investigate the function of OsCERK1. Transcriptional analyses of the knockdown cell lines showed that expression ofOsCERK1was markedly reduced but expression of the otherOsLysM-RLKgenes and theCEBiPgene was not affected in these cell lines.&lt;br /&gt;
Chitin oligosaccharide elicitor is known to induce biphasic generation of reactive oxygen species (ROS) in rice suspension cell cultures. The first peak of ROS at approximately 30 min after elicitor treatment does not require protein synthesis, but the latter peak at approximately 2 h does&lt;br /&gt;
require protein synthesis (Yamaguchi et al., 2005). &lt;br /&gt;
Both peaks of chitin oligosaccharide-induced ROS generation were markedly decreased in allOsCERK1-RNAi cell lines compared to vector control (VC) cells (Figure 2c). On the other hand, ROS generation induced by a bacterial lipopolysaccharide (LPS) (Desakiet al., 2006) was not affected in these OsCERK1-RNAi cell lines (Figure 2d), although the amount of ROS accumulated varied between the cell lines.&lt;br /&gt;
These results indicate that knockdown ofOsCERK1specifically affected the chitin-induced ROS generation of rice cells.&lt;br /&gt;
Here, we identified a receptor-like kinase, designated CERK1, which is essential for chitin elicitor signaling in Arabidopsis. The KO mutants for CERK1 completely lost the ability to respond to the chitin elicitor, including MAPK activation, reactive oxygen species generation, and gene expression. Disease resistance of the KO mutant against an incompatible fungus, Alternaria brassicicola, was partly impaired. Complementation with the WT CERK1 gene showed cerk1 mutations were responsible for the mutant phenotypes.&lt;br /&gt;
&lt;br /&gt;
===Catalytic activity===&lt;br /&gt;
ATP + a protein = ADP + a phosphoprotein.&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Life Sciences; 1-1-1 Higashi-Mita, Tama-ku, Kawasaki,Kanagawa 214-8571, Japan&lt;br /&gt;
*The Sainsbury Laboratory, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom&lt;br /&gt;
*Department of Plant Cell Biology, Albrecht-von-Haller-Institute of Plant Sciences, Georg-August-University Goettingen, Untere Karspuele 2, D-37073 Goettingen, Germany&lt;br /&gt;
*Department of Life Sciences, Faculty of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa214-8571, Japan,&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
*Nürnberger T., Kemmerling B. (2006) Trends Plant Sci. 11, 519–522 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Boller T., Felix G. (2009) Annu. Rev. Plant Biol. 60, 379–406 CrossRefMedlineSearch Google Scholar&lt;br /&gt;
*Kim, T.W. and Wang, Z.Y.(2010) Brassinosteroid signal transduction from receptor kinases to transcription factors.Annu. Rev. Plant Biol.61, 681–704.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = OsCERK1|&lt;br /&gt;
Description =LysM receptor-like kinase |&lt;br /&gt;
Version = |&lt;br /&gt;
Length =  bp|&lt;br /&gt;
Definition = chitin elicitor receptor kinase|&lt;br /&gt;
Chromosome = Chromosome |&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Japonica Group&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=User_talk:Duweili13&amp;diff=173777</id>
		<title>User talk:Duweili13</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=User_talk:Duweili13&amp;diff=173777"/>
				<updated>2014-05-29T01:21:36Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
  Xa21 encodes a receptor kinase carrying extracellular leucine-rich repeats (LRRs), as well as transmembrane (TM), juxtamembrane (JM) &lt;br /&gt;
  and intracellular non-RD (arginine - aspartate) kinase domains. XA21-mediated immunity is activated upon recognition of a &lt;br /&gt;
  194-amino acid protein designated Ax21 (activator of XA21-mediated innate immunity). Non-RD kinases usually carry a cysteine or &lt;br /&gt;
  glycine in place of the arginine and can induces inflammatory responses by both NLRs and TLRs. XA21 biogenesis occurs in the &lt;br /&gt;
  endoplasmic reticulum (ER) and the phosphorylation state of XA21 is critical for XA21-mediated signaling. &lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
 XA21 is a kind of transmembrane protein. &lt;br /&gt;
&lt;br /&gt;
===Evolution===&lt;br /&gt;
 Genome analyses have revealed an approximately 10-fold greater number of non-RD receptor kinases &lt;br /&gt;
 in rice (328) than inArabidopsis (35). These results suggest that rice has a vastly expanded capacity to &lt;br /&gt;
 recognize conserved microbial signature molecules.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Ecology and Evolution, University of Chicago, 1101 E. 57th Street, Chicago, IL 60637, USA&lt;br /&gt;
*Department of Plant Pathology, University of California, Davis, CA 95616, USA&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
*Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
* Song, W.Y.et al.(1995) A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21.Science270, 1804–1806&lt;br /&gt;
* Dardick, C. and Ronald, P. (2006) Plant and animal pathogen recognition receptors signal through non-RD kinases.PLoS Pathog. 2, e2&lt;br /&gt;
* Towb, P.et al.(2009) Tube Is an IRAK-4 homolog in a Toll pathway adapted for development and immunity.J. Innate Immun.1, 309–321&lt;br /&gt;
* Park, C.J. et al. (2010) Elucidation of XA21-mediated innate immunity. Cell. Microbiol.12, 1017–1025&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = xa21|&lt;br /&gt;
Description =receptor kinase-like protein |&lt;br /&gt;
Version = AY885788.1   GI: 63098480|&lt;br /&gt;
Length = 1091 bp|&lt;br /&gt;
Definition = Oryza sativa (indica cultivar-group) isolate Xa21 receptor kinase-like protein(Xa21) gene, partial cds.|&lt;br /&gt;
Chromosome = Chromosome 11|&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;TTGATAAGATCACAGGAAGCATTCCAAAGGATATTGGCAATCTTATTGGCTTACAACATCTCTATCTCTGCAACAACAATTTCAGAGGGTCTCTTCCATCATCGTTGGGCAGGCTTAGAAACTTAGGCATTCTAGTCGCCTACGAAAACAACTTGAGCGGTTCGATCCCATTGGCCATAGGAAATCTTACTGAACTTAATATCTTACTGCTCGGCACCAACAAATTCAGTGGTTGGATACCATACACACTCTCAAACCTCACAAACTTGTTGTCATTAGGCCTTTCAACTAATAACCTTAGTGGTCCAATACCCAGTGAATTATTCAATATTCAAACACTATCAATAATGATCAATGTATCAAAAAATAACTTGGAGGGATCAATACCACAAGAAATAGGGCATCTCAAAAATCTAGTAGAATTTCATGCAGAATCGAATAGATTATCAGGTAAAATCCCTAACACGCTTGGTGATTGCCAGCTCTTACGGTATCTTTATCTGCAAAATAATTTGTTATCTGGTAGCATCCCATCAGCCTTGGGTCAGCTGAAAGGTCTCGAAACTCTTGATCTCTCAAGCAACAATTTGTCAGGCCAGATACCCACATCCTTAGCAGATATTACTATGCTTCATTCCTTGAACCTTTCTTTCAACAGCTTTATGGGGGAAGTGCCAACCATTGGTGCTTTCGCAGATGCATCCGGGATCTCAATCCAAGGCAATGCCAAACTCTGTGGTGGAATACCTGATCTACATCTGCCTCGATGTTGTCCATTACTAGAGAATAGAAAACATTTCCCAGTTCTACCTATTTCTGTTTCTCTGGTCGCAGCACTGGCCATCCTCTCATCACTCTACTTGCTTATAACCTGGCACAAGAGAACTAAAAAGGGAGCCCCTTCAAGAACTTCCATGAAAGGCCACCCATTGGTCTCTTATTCGCAGTTGGTAAAAGCAACAGATGGTTTCGCGCCGACTAATTTGTTGGGTTCTGGATCATTTGGCTCAGTATACAAAGGAAAGCTTAATATCCAAGATCATTTGCAGTGAAGGTACTAAAGCTTGAAAATCCTAAGGCACTCAAGAGT&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;DKITGSIPKDIGNLIGLQHLYLCNNNFRGSLPSSLGRLRNLGILVAYENNLSGSIPLAIGNLTELNILLL&lt;br /&gt;
GTNKFSGWIPYTLSNLTNLLSLGLSTNNLSGPIPSELFNIQTLSIMINVSKNNLEGSIPQEIGHLKNLVE&lt;br /&gt;
FHAESNRLSGKIPNTLGDCQLLRYLYLQNNLLSGSIPSALGQLKGLETLDLSSNNLSGQIPTSLADITML&lt;br /&gt;
HSLNLSFNSFMGEVPTIGAFADASGISIQGNAKLCGGIPDLHLPRCCPLLENRKHFPVLPISVSLVAALA&lt;br /&gt;
ILSSLYLLITWHKRTKKGAPSRTSMKGHPLVSYSQLVKATDGFAPTNLLGSGSFGSVYKGKLNIQDHVAVKVLKLENPKALKS&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Indica Group  (long-grained rice)&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	<entry>
		<id>https://ngdc.cncb.ac.cn/ricewiki/index.php?title=User_talk:Duweili13&amp;diff=173773</id>
		<title>User talk:Duweili13</title>
		<link rel="alternate" type="text/html" href="https://ngdc.cncb.ac.cn/ricewiki/index.php?title=User_talk:Duweili13&amp;diff=173773"/>
				<updated>2014-05-29T00:53:29Z</updated>
		
		<summary type="html">&lt;p&gt;Duweili13: Created page with &amp;quot;==Annotated Information== ===Function===  Xa21 encodes a receptor kinase carrying extracellular leucine-rich repeats (LRRs), as well as transmembrane (TM), juxtamembrane (JM) ...&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;==Annotated Information==&lt;br /&gt;
===Function===&lt;br /&gt;
 Xa21 encodes a receptor kinase carrying extracellular leucine-rich repeats (LRRs), as well as transmembrane (TM), juxtamembrane (JM) and intracellular non-RD (arginine - aspartate) kinase domains. XA21-mediated immunity is activated upon recognition of a 194-amino acid protein designated Ax21 (activator of XA21-mediated innate immunity). Non-RD kinases usually carry a cysteine or glycine in place of the arginine and can induces inflammatory responses by both NLRs and TLRs. XA21 biogenesis occurs in the endoplasmic reticulum (ER) and the phosphorylation state of XA21 is critical for XA21-mediated signaling. &lt;br /&gt;
&lt;br /&gt;
===Localization===&lt;br /&gt;
 XA21 is a kind of transmembrane protein. &lt;br /&gt;
&lt;br /&gt;
===Evolution===&lt;br /&gt;
 Genome analyses have revealed an approximately 10-fold greater number of non-RD receptor kinases in rice (328) than inArabidopsis (35). These results suggest that rice has a vastly expanded capacity to recognize conserved microbial signature molecules.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Labs working on this gene==&lt;br /&gt;
*Department of Ecology and Evolution, University of Chicago, 1101 E. 57th Street, Chicago, IL 60637, USA&lt;br /&gt;
*Department of Plant Pathology, University of California, Davis, CA 95616, USA&lt;br /&gt;
*Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602,Japan&lt;br /&gt;
*Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
* Song, W.Y.et al.(1995) A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21.Science270, 1804–1806&lt;br /&gt;
* Dardick, C. and Ronald, P. (2006) Plant and animal pathogen recognition receptors signal through non-RD kinases.PLoS Pathog. 2, e2&lt;br /&gt;
* Towb, P.et al.(2009) Tube Is an IRAK-4 homolog in a Toll pathway adapted for development and immunity.J. Innate Immun.1, 309–321&lt;br /&gt;
* Park, C.J. et al. (2010) Elucidation of XA21-mediated innate immunity. Cell. Microbiol.12, 1017–1025&lt;br /&gt;
&lt;br /&gt;
==Structured information==&lt;br /&gt;
{{JaponicaGene|&lt;br /&gt;
GeneName = xa21|&lt;br /&gt;
Description =receptor kinase-like protein |&lt;br /&gt;
Version = AY885788.1   GI: 63098480|&lt;br /&gt;
Length = 1091 bp|&lt;br /&gt;
Definition = Oryza sativa (indica cultivar-group) isolate Xa21 receptor kinase-like protein(Xa21) gene, partial cds.|&lt;br /&gt;
Chromosome = Chromosome 11|&lt;br /&gt;
CDNA=&lt;br /&gt;
&amp;lt;cdnaseq&amp;gt;TTGATAAGATCACAGGAAGCATTCCAAAGGATATTGGCAATCTTATTGGCTTACAACATCTCTATCTCTGCAACAACAATTTCAGAGGGTCTCTTCCATCATCGTTGGGCAGGCTTAGAAACTTAGGCATTCTAGTCGCCTACGAAAACAACTTGAGCGGTTCGATCCCATTGGCCATAGGAAATCTTACTGAACTTAATATCTTACTGCTCGGCACCAACAAATTCAGTGGTTGGATACCATACACACTCTCAAACCTCACAAACTTGTTGTCATTAGGCCTTTCAACTAATAACCTTAGTGGTCCAATACCCAGTGAATTATTCAATATTCAAACACTATCAATAATGATCAATGTATCAAAAAATAACTTGGAGGGATCAATACCACAAGAAATAGGGCATCTCAAAAATCTAGTAGAATTTCATGCAGAATCGAATAGATTATCAGGTAAAATCCCTAACACGCTTGGTGATTGCCAGCTCTTACGGTATCTTTATCTGCAAAATAATTTGTTATCTGGTAGCATCCCATCAGCCTTGGGTCAGCTGAAAGGTCTCGAAACTCTTGATCTCTCAAGCAACAATTTGTCAGGCCAGATACCCACATCCTTAGCAGATATTACTATGCTTCATTCCTTGAACCTTTCTTTCAACAGCTTTATGGGGGAAGTGCCAACCATTGGTGCTTTCGCAGATGCATCCGGGATCTCAATCCAAGGCAATGCCAAACTCTGTGGTGGAATACCTGATCTACATCTGCCTCGATGTTGTCCATTACTAGAGAATAGAAAACATTTCCCAGTTCTACCTATTTCTGTTTCTCTGGTCGCAGCACTGGCCATCCTCTCATCACTCTACTTGCTTATAACCTGGCACAAGAGAACTAAAAAGGGAGCCCCTTCAAGAACTTCCATGAAAGGCCACCCATTGGTCTCTTATTCGCAGTTGGTAAAAGCAACAGATGGTTTCGCGCCGACTAATTTGTTGGGTTCTGGATCATTTGGCTCAGTATACAAAGGAAAGCTTAATATCCAAGATCATTTGCAGTGAAGGTACTAAAGCTTGAAAATCCTAAGGCACTCAAGAGT&amp;lt;/cdnaseq&amp;gt;|&lt;br /&gt;
AA=&lt;br /&gt;
&amp;lt;aaseq&amp;gt;DKITGSIPKDIGNLIGLQHLYLCNNNFRGSLPSSLGRLRNLGILVAYENNLSGSIPLAIGNLTELNILLL&lt;br /&gt;
GTNKFSGWIPYTLSNLTNLLSLGLSTNNLSGPIPSELFNIQTLSIMINVSKNNLEGSIPQEIGHLKNLVE&lt;br /&gt;
FHAESNRLSGKIPNTLGDCQLLRYLYLQNNLLSGSIPSALGQLKGLETLDLSSNNLSGQIPTSLADITML&lt;br /&gt;
HSLNLSFNSFMGEVPTIGAFADASGISIQGNAKLCGGIPDLHLPRCCPLLENRKHFPVLPISVSLVAALA&lt;br /&gt;
ILSSLYLLITWHKRTKKGAPSRTSMKGHPLVSYSQLVKATDGFAPTNLLGSGSFGSVYKGKLNIQDHVAVKVLKLENPKALKS&amp;lt;/aaseq&amp;gt;|&lt;br /&gt;
Source = Oryza sativa Indica Group  (long-grained rice)&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>Duweili13</name></author>	</entry>

	</feed>