LRKS6_ARATH
ID LRKS6_ARATH Reviewed; 691 AA.
AC Q9FHX3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=L-type lectin-domain containing receptor kinase S.6 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-S.6 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=LECRKS6 {ECO:0000303|PubMed:19773388};
GN OrderedLocusNames=At5g42120 {ECO:0000312|Araport:AT5G42120};
GN ORFNames=MJC20.23 {ECO:0000312|EMBL:BAB08445.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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).
CC -!- FUNCTION: Involved in resistance response to the pathogenic oomycetes
CC Phytophthora infestans and Phytophthora capsici and to the pathogenic
CC bacteria Pseudomonas syringae. {ECO:0000269|PubMed:25083911}.
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 -!- 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 and to the bacteria
CC Pseudomonas syringae, characterized by stronger necrotic symptoms.
CC {ECO:0000269|PubMed:25083911}.
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}.
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DR EMBL; AB017067; BAB08445.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94770.1; -; Genomic_DNA.
DR EMBL; DQ447030; ABE66214.1; -; mRNA.
DR RefSeq; NP_199027.1; NM_123577.2.
DR AlphaFoldDB; Q9FHX3; -.
DR SMR; Q9FHX3; -.
DR STRING; 3702.AT5G42120.1; -.
DR iPTMnet; Q9FHX3; -.
DR PaxDb; Q9FHX3; -.
DR PRIDE; Q9FHX3; -.
DR ProteomicsDB; 238570; -.
DR EnsemblPlants; AT5G42120.1; AT5G42120.1; AT5G42120.
DR GeneID; 834217; -.
DR Gramene; AT5G42120.1; AT5G42120.1; AT5G42120.
DR KEGG; ath:AT5G42120; -.
DR Araport; AT5G42120; -.
DR TAIR; locus:2165740; AT5G42120.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9FHX3; -.
DR OMA; TEFATMV; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FHX3; -.
DR PRO; PR:Q9FHX3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHX3; baseline and differential.
DR Genevisible; Q9FHX3; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
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 Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..691
FT /note="L-type lectin-domain containing receptor kinase S.6"
FT /id="PRO_0000403108"
FT TOPO_DOM 26..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 366..653
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..257
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 500
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 372..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 691 AA; 76556 MW; 181AC6B8B7A06A5F CRC64;
MNHHHYSLVI FHLILFLSLD FPTLSHRFSP PLQNLTLYGD AFFRDRTISL TQQQPCFPSV
TTPPSKPSSS GIGRALYVYP IKFLEPSTNT TASFSCRFSF SIIASPSCPF GDGFAFLITS
NADSFVFSNG FLGLPNPDDS FIAVEFDTRF DPVHGDINDN HVGIDVSSIF SVSSVDAISK
GFDLKSGKKM MAWIEYSDVL KLIRVWVGYS RVKPTSPVLS TQIDLSGKVK EYMHVGFSAS
NAGIGSALHI VERWKFRTFG SHSDAIQEEE EEKDEECLVC SGEVSENPKE IHRKGFNFRV
TVVGLKIPVW SLLPGLAAIV ILVAFIVFSL ICGKKRISEE ADSNSGLVRM PGRLSLAEIK
SATSGFNENA IVGQGASATV YRGSIPSIGS VAVKRFDREH WPQCNRNPFT TEFTTMTGYL
RHKNLVQFQG WCSEGTETAL VFEYLPNGSL SEFLHKKPSS DPSEEIIVLS WKQRVNIILG
VASALTYLHE ECERQIIHRD VKTCNIMLDA EFNAKLGDFG LAEIYEHSAL LAGRAATLPA
GTMGYLAPEY VYTGVPSEKT DVYSFGVVVL EVCTGRRPVG DDGAVLVDLM WSHWETGKVL
DGADIMLREE FDAEEMERVL MVGMVCAHPD SEKRPRVKDA VRIIRGEAPL PVLPARRPLL
RIRPANEAEE MIVDGLVGED LPWMTPKSHF S
