LRK92_ARATH
ID LRK92_ARATH Reviewed; 675 AA.
AC Q9LSL5; Q56YD3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=L-type lectin-domain containing receptor kinase IX.2 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-IX.2 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=LECRK92 {ECO:0000303|PubMed:19773388};
GN OrderedLocusNames=At5g65600 {ECO:0000312|Araport:AT5G65600};
GN ORFNames=K21L13.11 {ECO:0000312|EMBL:BAA98179.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] OF 8-457.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX DOI=10.1080/0735-260291044287;
RA Barre A., Herve C., Lescure B., Rouge P.;
RT "Lectin receptor kinases in plants.";
RL Crit. Rev. Plant Sci. 21:379-399(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19773388; DOI=10.1093/jxb/erp277;
RA Bouwmeester K., Govers F.;
RT "Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and
RT expression profiles.";
RL J. Exp. Bot. 60:4383-4396(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25083911; DOI=10.1094/mpmi-06-14-0191-r;
RA Wang Y., Bouwmeester K., Beseh P., Shan W., Govers F.;
RT "Phenotypic analyses of Arabidopsis T-DNA insertion lines and expression
RT profiling reveal that multiple L-type lectin receptor kinases are involved
RT in plant immunity.";
RL Mol. Plant Microbe Interact. 27:1390-1402(2014).
RN [7]
RP FUNCTION, MUTAGENESIS OF 474-ARG-ASP-475 AND ASP-475, DISRUPTION PHENOTYPE,
RP INTERACTION WITH ABCG40, AND MISCELLANEOUS.
RC STRAIN=cv. Columbia;
RX PubMed=26011556; DOI=10.1094/mpmi-02-15-0025-r;
RA Wang Y., Cordewener J.H.G., America A.H.P., Shan W., Bouwmeester K.,
RA Govers F.;
RT "Arabidopsis lectin receptor kinases LecRK-IX.1 and LecRK-IX.2 are
RT functional analogs in regulating phytophthora resistance and plant cell
RT death.";
RL Mol. Plant Microbe Interact. 28:1032-1048(2015).
RN [8]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=26795144; DOI=10.1007/s00299-015-1926-2;
RA Wang Y., Nsibo D.L., Juhar H.M., Govers F., Bouwmeester K.;
RT "Ectopic expression of Arabidopsis L-type lectin receptor kinase genes
RT LecRK-I.9 and LecRK-IX.1 in Nicotiana benthamiana confers Phytophthora
RT resistance.";
RL Plant Cell Rep. 35:845-855(2016).
CC -!- FUNCTION: Promotes hydrogen peroxide H(2)O(2) production and cell
CC death. {ECO:0000269|PubMed:26011556}.
CC -!- FUNCTION: Involved in resistance response to the pathogenic oomycetes
CC Phytophthora infestans and Phytophthora capsici.
CC {ECO:0000269|PubMed:25083911, ECO:0000269|PubMed:26011556,
CC ECO:0000269|PubMed:26795144}.
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:0000255|PROSITE-ProRule:PRU00159};
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:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with ABCG40. {ECO:0000269|PubMed:26011556}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9LSR8};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to the oomycetes
CC Phytophthora brassicae and Phytophthora capsici associated with reduced
CC expression of some defense genes (e.g. PR1, PDF1.2, CYP71B15 and
CC CYP81F2). However, normal defense responses to the fungal pathogen
CC Alternaria brassicicola and to the bacterial pathogen Pseudomonas
CC syringae (PubMed:25083911, PubMed:26011556). Susceptibility to P.
CC brassicae and P. capsici is enhanced in plants impaired in LECRK91 and
CC LECRK92 (PubMed:26011556). {ECO:0000269|PubMed:25083911,
CC ECO:0000269|PubMed:26011556}.
CC -!- BIOTECHNOLOGY: Confers enhanced resistance to late blight mediated by
CC the pathogenic oomycetes Phytophthora infestans and Phytophthora
CC capsici when transfected into Nicotiana benthamiana. This resistance is
CC associated with a high induction of protease inhibitor genes.
CC {ECO:0000269|PubMed:26795144}.
CC -!- MISCELLANEOUS: Both lectin domain and kinase activity are required for
CC resistance to oomycetes, but only the lectin domain is required to
CC trigger cell death. {ECO:0000269|PubMed:26011556}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94319.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD94319.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB026639; BAA98179.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98075.1; -; Genomic_DNA.
DR EMBL; AK221390; BAD94319.1; ALT_SEQ; mRNA.
DR RefSeq; NP_201363.1; NM_125958.2.
DR AlphaFoldDB; Q9LSL5; -.
DR SMR; Q9LSL5; -.
DR STRING; 3702.AT5G65600.1; -.
DR PaxDb; Q9LSL5; -.
DR PRIDE; Q9LSL5; -.
DR ProteomicsDB; 238677; -.
DR EnsemblPlants; AT5G65600.1; AT5G65600.1; AT5G65600.
DR GeneID; 836686; -.
DR Gramene; AT5G65600.1; AT5G65600.1; AT5G65600.
DR KEGG; ath:AT5G65600; -.
DR Araport; AT5G65600; -.
DR TAIR; locus:2155685; AT5G65600.
DR eggNOG; ENOG502QQSK; Eukaryota.
DR HOGENOM; CLU_000288_62_6_1; -.
DR InParanoid; Q9LSL5; -.
DR OMA; PEYVMKG; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LSL5; -.
DR PRO; PR:Q9LSL5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSL5; baseline and differential.
DR Genevisible; Q9LSL5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IDA:UniProtKB.
DR GO; GO:0140426; P:PAMP-triggered immunity signalling pathway; IPI:TAIR.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:TAIR.
DR GO; GO:0010726; P:positive regulation of hydrogen peroxide metabolic process; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; SSF49899; 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; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; Plant defense; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..675
FT /note="L-type lectin-domain containing receptor kinase
FT IX.2"
FT /id="PRO_0000403104"
FT TOPO_DOM 36..281
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 350..631
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..269
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 356..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 474..475
FT /note="RD->AA: In LecRK-IX.2-AA; loss of kinase activity
FT and impaired ability to mediate resistance to
FT Phytophthora."
FT /evidence="ECO:0000269|PubMed:26011556"
FT MUTAGEN 475
FT /note="D->N: In LecRK-IX.2-RN; loss of kinase activity and
FT impaired ability to mediate resistance to Phytophthora."
FT /evidence="ECO:0000269|PubMed:26011556"
SQ SEQUENCE 675 AA; 75295 MW; 287FA7CF1F4ACBE7 CRC64;
MLYFIFCQNL SSSSSMSNSI LFLSLFLFLP FVVDSLYFNF TSFRQGDPGD IFYHGDATPD
EDGTVNFNNA EQTSQVGWIT YSKKVPIWSH KTGKASDFST SFSFKIDARN LSADGHGICF
FLAPMGAQLP AYSVGGFLNL FTRKNNYSSS FPLVHVEFDT FNNPGWDPND VGSHVGINNN
SLVSSNYTSW NASSHSQDIC HAKISYDSVT KNLSVTWAYE LTATSDPKES SSLSYIIDLA
KVLPSDVMFG FIAAAGTNTE EHRLLSWELS SSLDSDKADS RIGLVIGISA SGFVFLTFMV
ITTVVVWSRK QRKKKERDIE NMISINKDLE REAGPRKFSY KDLVSATNRF SSHRKLGEGG
FGAVYEGNLK EINTMVAVKK LSGDSRQGKN EFLNEVKIIS KLRHRNLVQL IGWCNEKNEF
LLIYELVPNG SLNSHLFGKR PNLLSWDIRY KIGLGLASAL LYLHEEWDQC VLHRDIKASN
IMLDSEFNVK LGDFGLARLM NHELGSHTTG LAGTFGYMAP EYVMKGSASK ESDIYSFGIV
LLEIVTGRKS LERTQEDNSD TESDDEKSLV EKVWELYGKQ ELITSCVDDK LGEDFDKKEA
ECLLVLGLWC AHPDKNSRPS IKQGIQVMNF ESPLPDLPLK RPVAMYYIST TTSSSSPSVN
SNGVSVTFSG IEYGR
