LYK4_ARATH
ID LYK4_ARATH Reviewed; 612 AA.
AC O64825;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=LysM domain receptor-like kinase 4;
DE Short=LysM-containing receptor-like kinase 4;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LYK4; OrderedLocusNames=At2g23770; ORFNames=F27L4.5;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CHITIN, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY CHITIN AND FLAGELLIN.
RX PubMed=22744984; DOI=10.1104/pp.112.201699;
RA Wan J., Tanaka K., Zhang X.-C., Son G.H., Brechenmacher L., Nguyen T.H.N.,
RA Stacey G.;
RT "LYK4, a lysin motif receptor-like kinase, is important for chitin
RT signaling and plant innate immunity in Arabidopsis.";
RL Plant Physiol. 160:396-406(2012).
CC -!- FUNCTION: Lysin motif (LysM) receptor kinase that functions as a cell
CC surface receptor in chitin elicitor (chitooligosaccharides) signaling
CC leading to innate immunity. Recognizes microbe-derived N-
CC acetylglucosamine (NAG)-containing ligands. Involved in the resistance
CC to the pathogenic fungus Alternaria brassicicola and to the bacterial
CC pathogen the bacterial pathogen Pseudomonas syringae pv tomato DC3000,
CC probably by sensing microbe-associated molecular pattern (MAMP) and
CC pathogen-associated molecular patterns (PAMP). May play a role in
CC detecting peptidoglycans (e.g. PGNs) during bacterial growth.
CC {ECO:0000269|PubMed:22744984}.
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: Homooligomer (By similarity). Binds to chitin oligosaccharide
CC elicitors. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22744984};
CC Single-pass membrane protein {ECO:0000269|PubMed:22744984}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves (predominantly in
CC hydathodes, apical meristems and stipules) and buds.
CC {ECO:0000269|PubMed:22744984}.
CC -!- INDUCTION: Moderately induced by chitin oligomers (e.g. chitohexaose
CC (6-mer) and chitooctaose (8-mer)) and flagellin (e.g. flg22).
CC {ECO:0000269|PubMed:22744984}.
CC -!- PTM: Autophosphorylated; induced by chitin and derivatives.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced induction of chitin-responsive genes and
CC diminished chitin-induced cytosolic calcium elevation, accompanied by
CC an enhanced susceptibility to both the bacterial pathogen Pseudomonas
CC syringae pv. tomato DC3000 and the fungal pathogen Alternaria
CC brassicicola. {ECO:0000269|PubMed:22744984}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC004482; AAC17086.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07489.1; -; Genomic_DNA.
DR PIR; T02414; T02414.
DR RefSeq; NP_179957.1; NM_127940.2.
DR AlphaFoldDB; O64825; -.
DR SMR; O64825; -.
DR BioGRID; 2261; 2.
DR IntAct; O64825; 1.
DR STRING; 3702.AT2G23770.1; -.
DR iPTMnet; O64825; -.
DR PaxDb; O64825; -.
DR PRIDE; O64825; -.
DR ProteomicsDB; 238745; -.
DR EnsemblPlants; AT2G23770.1; AT2G23770.1; AT2G23770.
DR GeneID; 816909; -.
DR Gramene; AT2G23770.1; AT2G23770.1; AT2G23770.
DR KEGG; ath:AT2G23770; -.
DR Araport; AT2G23770; -.
DR TAIR; locus:2049029; AT2G23770.
DR eggNOG; ENOG502QSFN; Eukaryota.
DR HOGENOM; CLU_000288_99_1_1; -.
DR InParanoid; O64825; -.
DR OMA; SCAGEYY; -.
DR OrthoDB; 898801at2759; -.
DR PhylomeDB; O64825; -.
DR PRO; PR:O64825; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64825; baseline and differential.
DR Genevisible; O64825; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071323; P:cellular response to chitin; IEP:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Chitin-binding; Disulfide bond; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..612
FT /note="LysM domain receptor-like kinase 4"
FT /id="PRO_0000420830"
FT TOPO_DOM 23..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 119..165
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 186..231
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 283..601
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 240..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 125..131
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 154..160
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 289..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..110
FT /evidence="ECO:0000250"
FT DISULFID 55..171
FT /evidence="ECO:0000250"
FT DISULFID 108..169
FT /evidence="ECO:0000250"
SQ SEQUENCE 612 AA; 66619 MW; 8A446D6D82090746 CRC64;
MISFSFHLLV FILLSLSSFA TAQQPYVGIS TTDCSVSDNT TSVFGYSCNG LNKTCQAYVI
FRSTPSFSTV TSISSLFSVD PSLVSSLNDA SPSTSFPSGQ QVIIPLTCSC TGDDSQSNIT
YTIQPNDSYF AIANDTLQGL STCQALAKQN NVSSQSLFPG MRIVVPIRCA CPTAKQINED
GVKYLMSYTV VFEDTIAIIS DRFGVETSKT LKANEMSFEN SEVFPFTTIL IPLVNPPANT
NSLIPPPPPP PPQSVSPPPL SPDGRKSKKK TWVYALAGVL GGALVLSVIG AAIFCLSKKK
TKTQTQEETG NLDSFMGKKP PMSDQEFDPL DGLSGMVVES LKVYKFHELQ SATSDFTSSS
SIGGSGYIGK INGDGAMIKK IEGNASEEVN LLSKLNHLNI IRLSGFCFHE GDWYLVYEHA
SNGSLSEWIH TTKSLLSLTQ KLQIALDIAT GLNYLHNFAD PPYVHRDLNS NNVFLDLEFR
AKIGSLGSAR STTEDFVLTK HVEGTRGYLA PEYLEHGLVS TKLDVYAFGV VLLEIVTGKE
ASELKKEIDE GKAIDEILIH GRLLPEGLTS FVERLVVDCL KKDHLNRPSM DENVMSLSKI
LAATQNWEES SY
