LRK17_ARATH
ID LRK17_ARATH Reviewed; 668 AA.
AC Q9LSS0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=L-type lectin-domain containing receptor kinase I.7 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-I.7 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=LECRK17 {ECO:0000303|PubMed:19773388};
GN OrderedLocusNames=At5g60270 {ECO:0000312|Araport:AT5G60270};
GN ORFNames=F15L12.9 {ECO:0000312|EMBL:BAA97507.1};
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].
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 (SEP-2004) 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).
CC -!- FUNCTION: Involved in resistance response to the pathogenic oomycetes
CC Phytophthora infestans and Phytophthora capsici.
CC {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.
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; AB026632; BAA97507.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97301.1; -; Genomic_DNA.
DR EMBL; AK175514; BAD43277.1; -; mRNA.
DR RefSeq; NP_200835.1; NM_125420.4.
DR AlphaFoldDB; Q9LSS0; -.
DR SMR; Q9LSS0; -.
DR STRING; 3702.AT5G60270.1; -.
DR PaxDb; Q9LSS0; -.
DR PRIDE; Q9LSS0; -.
DR ProteomicsDB; 238673; -.
DR EnsemblPlants; AT5G60270.1; AT5G60270.1; AT5G60270.
DR GeneID; 836149; -.
DR Gramene; AT5G60270.1; AT5G60270.1; AT5G60270.
DR KEGG; ath:AT5G60270; -.
DR Araport; AT5G60270; -.
DR TAIR; locus:2144015; AT5G60270.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9LSS0; -.
DR OMA; TRMGRAT; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LSS0; -.
DR PRO; PR:Q9LSS0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSS0; baseline and differential.
DR Genevisible; Q9LSS0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..668
FT /note="L-type lectin-domain containing receptor kinase I.7"
FT /id="PRO_0000403076"
FT TOPO_DOM 22..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 341..620
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..256
FT /note="Legume-lectin like"
FT /evidence="ECO:0000305"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 347..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 668 AA; 73955 MW; BA19F3249EA25BE3 CRC64;
MIRGLLLGII WMIFCVCSSF QQETPFVYNN FGHVDHLHLD GSARIIPSGG ILQLTNATNS
QIGHVFYEKP IEFKSSESVS FSTYFVCALL PAGDPSGHGM TFFVSHSTDF KGAEATRYFG
IFNRNGSTST RVLAVELDTS LASDVKDISD NHVGIDVNSA ESITSANASY FSDKEGKKID
IKLLSGDPIQ VWVDYEGTTL NVSLAPLRNK KPSRPLLSST SINLTDILQG RRMFVGFSGS
TGSSMSYQYI LGWSFSKSMA SLPNIDISKL PKVPHSSTKK KSTSPVLSVL LGLIAFIVLG
ILVVAYLYRR NLYSEVREEW EKEYGPIRYS YKSLYKATKG FNRSEFLGRG GFGEVYKGTL
PRSRELREVA VKRVSHDGEH GMKQFVAEIV SMRSLKHRSL VPLLGYCRRK HELLLVSEYM
PNGSLDHYLF NHDRLSLPWW RRLAILRDIA SALSYLHTEA DQVVIHRDIK AANVMLDAEF
NGRLGDFGMS RLYDRGADPS TTAAVGTVGY MAPELTTMGA STGTDVYAFG VFLLEVTCGR
RPVEPGLPEA KRFLIKWVSE CWKRSSLIDA RDPRLTEFSS QEVEKVLKLG LLCANLAPDS
RPAMEQVVQY LNGNLALPEF WPNSPGIGVL SPMALSPAPL VIPSLSFSSS SSNNSMFITH
SVLYGSGR
