LRK32_ARATH
ID LRK32_ARATH Reviewed; 623 AA.
AC Q9ZW11;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative inactive L-type lectin-domain containing receptor kinase III.2 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-III.2 {ECO:0000303|PubMed:19773388};
DE Flags: Precursor;
GN Name=LECRK32 {ECO:0000303|PubMed:19773388};
GN OrderedLocusNames=At2g29250 {ECO:0000312|Araport:AT2G29250};
GN ORFNames=F16P2.37 {ECO:0000312|EMBL:AAC95210.1};
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=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 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 [4]
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 [5]
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9LSR8};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000305}.
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; AC004561; AAC95210.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08225.1; -; Genomic_DNA.
DR PIR; C84694; C84694.
DR RefSeq; NP_180488.1; NM_128481.1.
DR AlphaFoldDB; Q9ZW11; -.
DR SMR; Q9ZW11; -.
DR BioGRID; 2824; 30.
DR IntAct; Q9ZW11; 29.
DR PaxDb; Q9ZW11; -.
DR PRIDE; Q9ZW11; -.
DR EnsemblPlants; AT2G29250.1; AT2G29250.1; AT2G29250.
DR GeneID; 817474; -.
DR Gramene; AT2G29250.1; AT2G29250.1; AT2G29250.
DR KEGG; ath:AT2G29250; -.
DR Araport; AT2G29250; -.
DR TAIR; locus:2043127; AT2G29250.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9ZW11; -.
DR OMA; RRCDKRI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZW11; -.
DR PRO; PR:Q9ZW11; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW11; baseline and differential.
DR Genevisible; Q9ZW11; 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: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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Lectin; Membrane;
KW Nucleotide-binding; Plant defense; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..623
FT /note="Putative inactive L-type lectin-domain containing
FT receptor kinase III.2"
FT /id="PRO_0000403084"
FT TOPO_DOM 24..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 352..616
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..262
FT /note="Legume-lectin like"
FT BINDING 358..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 623 AA; 68216 MW; 158216ABB930827E CRC64;
MANTYKSIAV SIIFLLYFSC VSSQQQTKFL NHGFLEANLL KSGSSKIHPS GHLELTNTSM
RQIGQAFHGF PIPFLNPNSS NLVSFPTSFV FAITPGPGAP GHGLAFVISP SLDFSGALPS
NYLGLFNTSN NGNSLNCILA VEFDTVQAVE LNDIDDNHVG IDLNGVISIE STSAEYFDDR
EAKNISLRLA SGKPIRVWIE YNATETMLNV TLAPLDRPKP KLPLLSRKLN LSGIISEENY
VGFSAATGTV TSSHFVLGWS FSIEGKASDF DITKLPSLPD PLPPLSPSPS PPVSVMKNSS
NTMLIIIIAA SAIFGILILS FLAVCFFRRT ENFTGGARKF SHQTISSATG GFDNSKLLGE
GNSGSFYKGQ LAPTEIIAVK RITCNTRQEK TALIAEIDAI SKVKQRNLVD LHGYCSKGNE
IYLVYEYVIN RSLDRFLFSN DLPVLKWVHR FCIIKGIASA LQHLHAEVQK PLIHGNVKAS
NVLLDGELNA RLGDYGHGSR HSTTGHVAPE LVNTGKATCA TDVFEFGVLI MEIVCGRRAI
EPTKEPVEIS LVNWVLRGVK SGNLLRRCDK RIKKKNLVSE EVLLVLKTGL LCVRRSPEDR
PMMKKVLEYL NGTEHLPHDD YVV
