CERK1_ORYSJ
ID CERK1_ORYSJ Reviewed; 624 AA.
AC A0A0P0XII1; B7F461; Q0J431; Q6ZD33;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Chitin elicitor receptor kinase 1 {ECO:0000303|PubMed:21070404};
DE Short=OsCERK1 {ECO:0000303|PubMed:21070404};
DE EC=2.7.11.1 {ECO:0000269|PubMed:23498959};
DE AltName: Full=LysM domain receptor-like kinase 1 {ECO:0000305};
DE Short=LysM RLK1 {ECO:0000305};
DE Short=LysM-containing receptor-like kinase 1 {ECO:0000305};
DE AltName: Full=LysM domain receptor-like kinase 9 {ECO:0000303|PubMed:21070404};
DE Short=OsLysM-RLK9 {ECO:0000303|PubMed:21070404};
DE Flags: Precursor;
GN Name=CERK1 {ECO:0000303|PubMed:21070404};
GN Synonyms=RLK9 {ECO:0000303|PubMed:21070404};
GN OrderedLocusNames=Os08g0538300 {ECO:0000312|EMBL:BAT06465.1},
GN LOC_Os08g42580 {ECO:0000305};
GN ORFNames=P0665C04.34 {ECO:0000312|EMBL:BAD01244.1},
GN P0666G10.101 {ECO:0000312|EMBL:BAD33138.1};
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=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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, HOMOOLIGOMERS, INTERACTION WITH CEBIP, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=21070404; DOI=10.1111/j.1365-313x.2010.04324.x;
RA Shimizu T., Nakano T., Takamizawa D., Desaki Y., Ishii-Minami N.,
RA Nishizawa Y., Minami E., Okada K., Yamane H., Kaku H., Shibuya N.;
RT "Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate
RT chitin elicitor signaling in rice.";
RL Plant J. 64:204-214(2010).
RN [6]
RP FUNCTION.
RX PubMed=22891159; DOI=10.1093/pcp/pcs113;
RA Shinya T., Motoyama N., Ikeda A., Wada M., Kamiya K., Hayafune M., Kaku H.,
RA Shibuya N.;
RT "Functional characterization of CEBiP and CERK1 homologs in Arabidopsis and
RT rice reveals the presence of different chitin receptor systems in plants.";
RL Plant Cell Physiol. 53:1696-1706(2012).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23498959; DOI=10.1016/j.chom.2013.02.007;
RA Yamaguchi K., Yamada K., Ishikawa K., Yoshimura S., Hayashi N.,
RA Uchihashi K., Ishihama N., Kishi-Kaboshi M., Takahashi A., Tsuge S.,
RA Ochiai H., Tada Y., Shimamoto K., Yoshioka H., Kawasaki T.;
RT "A receptor-like cytoplasmic kinase targeted by a plant pathogen effector
RT is directly phosphorylated by the chitin receptor and mediates rice
RT immunity.";
RL Cell Host Microbe 13:347-357(2013).
RN [8]
RP FUNCTION, INTERACTION WITH LYP4 AND LYP6, AND SUBCELLULAR LOCATION.
RX PubMed=24964058; DOI=10.1094/mpmi-03-14-0068-r;
RA Kouzai Y., Mochizuki S., Nakajima K., Desaki Y., Hayafune M., Miyazaki H.,
RA Yokotani N., Ozawa K., Minami E., Kaku H., Shibuya N., Nishizawa Y.;
RT "Targeted gene disruption of OsCERK1 reveals its indispensable role in
RT chitin perception and involvement in the peptidoglycan response and
RT immunity in rice.";
RL Mol. Plant Microbe Interact. 27:975-982(2014).
RN [9]
RP FUNCTION, INTERACTION WITH LYP4; LYP6 AND RLCK176, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25335639; DOI=10.1111/tpj.12710;
RA Ao Y., Li Z., Feng D., Xiong F., Liu J., Li J.F., Wang M., Wang J., Liu B.,
RA Wang H.B.;
RT "OsCERK1 and OsRLCK176 play important roles in peptidoglycan and chitin
RT signaling in rice innate immunity.";
RL Plant J. 80:1072-1084(2014).
CC -!- FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface
CC receptor for chitin elicitor (chitooligosaccharides) signaling leading
CC to innate immunity in response to biotic stresses. Involved in the
CC resistance to pathogenic fungi, probably by sensing microbe-associated
CC molecular patterns (MAMP) and pathogen-associated molecular patterns
CC (PAMP) (PubMed:21070404, PubMed:22891159, PubMed:24964058). Involved in
CC the detection of microbial peptidoglycans (PGNs) and mediates PGN
CC response (PubMed:24964058). Plays dual roles in PGN and chitin
CC signaling during innate immunity. Acts as an adapter for LYP4 and LYP6
CC and mediates signal transduction from the extracellular to
CC intracellular spaces. Participates in the activation of defense genes
CC during response to PGN and chitin (PubMed:25335639). Phosphorylates the
CC downstream partner RLCK185 in response to chitin elicitation
CC (PubMed:23498959). {ECO:0000269|PubMed:21070404,
CC ECO:0000269|PubMed:22891159, ECO:0000269|PubMed:23498959,
CC ECO:0000269|PubMed:24964058, ECO:0000269|PubMed:25335639}.
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 Evidence={ECO:0000269|PubMed:23498959};
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; Evidence={ECO:0000269|PubMed:23498959};
CC -!- SUBUNIT: Homooligomer. Interacts with CEBIP (PubMed:21070404).
CC Interacts with LYP4 and LYP6 (PubMed:24964058, PubMed:25335639).
CC Interacts with RLCK176 (PubMed:25335639). {ECO:0000269|PubMed:21070404,
CC ECO:0000269|PubMed:24964058, ECO:0000269|PubMed:25335639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24964058,
CC ECO:0000269|PubMed:25335639}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, shoots and stems,
CC and, to a lower extent, in flowers. {ECO:0000269|PubMed:21070404}.
CC -!- PTM: Autophosphorylated; induced by chitin and derivatives.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Suppression of the defense responses induced by
CC chitin oligosaccharides. {ECO:0000269|PubMed:21070404}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD01244.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD33138.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF24284.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAG99408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG99505.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP004464; BAD01244.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP004592; BAD33138.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF24284.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; BAT06465.1; -; Genomic_DNA.
DR EMBL; AK111766; BAG99408.1; ALT_INIT; mRNA.
DR EMBL; AK112001; BAG99505.1; ALT_INIT; mRNA.
DR RefSeq; XP_015650771.1; XM_015795285.1.
DR AlphaFoldDB; A0A0P0XII1; -.
DR SMR; A0A0P0XII1; -.
DR STRING; 4530.OS08T0538300-01; -.
DR PaxDb; A0A0P0XII1; -.
DR EnsemblPlants; Os08t0538300-01; Os08t0538300-01; Os08g0538300.
DR GeneID; 4346173; -.
DR Gramene; Os08t0538300-01; Os08t0538300-01; Os08g0538300.
DR KEGG; osa:4346173; -.
DR eggNOG; ENOG502QPX8; Eukaryota.
DR OMA; VCRYARY; -.
DR OrthoDB; 684563at2759; -.
DR PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; A0A0P0XII1; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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:0019199; F:transmembrane receptor protein kinase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR044812; CERK1/LYK3-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46204; PTHR46204; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Chitin-binding; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Kinase; Membrane; Nucleotide-binding;
KW Plant defense; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..624
FT /note="Chitin elicitor receptor kinase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5006057118"
FT TOPO_DOM 19..240
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 173..218
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 324..599
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 115..121
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT BINDING 142..148
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT BINDING 330..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..93
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DISULFID 34..160
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DISULFID 91..158
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
SQ SEQUENCE 624 AA; 67068 MW; 62635BB84B57C9CE CRC64;
MEASTSLLVL VLAAAAFAAG TVTEAAGDGC SAGCDLALAS FYVTPNQNVT NMADLFGIGA
ANYRSLAPYN PNIPNLDFIN VGGRVNVYFT CGCRSLPGSP GATYLAGAFP FQMSRGQIYT
SVAANYNNLT TAEWLQATNS YPANNIPDTA VINATVNCSC GDASISPDYG LFLTYPLRAE
DTLASVAATY GLSSQLDVVR RYNPGMESAT GSGIVYIPVK DPNGSYLPLK SPGKGASAGA
IAGGVVAGVV VLAAIFLYII FYRRRKAKQA TLLQSSEDST QLGTISMDKV TPSTIVGPSP
VAGITVDKSV EFSYEELSNA TQGFSIGNKI GQGGFGAVYY AELRGEKAAI KKMDMQATHE
FLAELKVLTH VHHLNLVRLI GYCIESSLFL VYEFIENGNL SQHLRGMGYE PLSWAARIQI
ALDSARGLEY IHEHTVPVYI HRDIKSANIL IDKNYRAKVA DFGLTKLTEV GGTSMPTGTR
VVGTFGYMPP EYARYGDVSP KVDVYAFGVV LYELISAKEA IVRSTESSSD SKGLVYLFEE
ALNSPDPKEG LRTLIDPKLG EDYPIDSILK LTQLAKVCTQ EDPKLRPSMR SVVVALMTLS
STSEFWDMNN LYENQGLVNL MSGR
