LRK54_ARATH
ID LRK54_ARATH Reviewed; 658 AA.
AC O22833;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=L-type lectin-domain containing receptor kinase V.4 {ECO:0000303|PubMed:19773388};
DE Short=Arabidopsis thaliana lectin-receptor kinase c1 {ECO:0000303|PubMed:19773388};
DE Short=AthlecRK-c1 {ECO:0000303|Ref.5};
DE Short=LecRK-V.4 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=LECRK54 {ECO:0000303|PubMed:19773388};
GN Synonyms=LECRKC1 {ECO:0000303|Ref.5};
GN OrderedLocusNames=At2g43700 {ECO:0000312|Araport:AT2G43700};
GN ORFNames=F18O19.19 {ECO:0000312|EMBL:AAB64036.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=10350082; DOI=10.1023/a:1006136701595;
RA Herve C., Serres J., Dabos P., Canut H., Barre A., Rouge P., Lescure B.;
RT "Characterization of the Arabidopsis lecRK-a genes: members of a
RT superfamily encoding putative receptors with an extracellular domain
RT homologous to legume lectins.";
RL Plant Mol. Biol. 39:671-682(1999).
RN [5]
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 [6]
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 [7]
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; AC002333; AAB64036.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10309.1; -; Genomic_DNA.
DR EMBL; AY074631; AAL69447.1; -; mRNA.
DR PIR; D84869; D84869.
DR RefSeq; NP_181898.1; NM_129932.6.
DR AlphaFoldDB; O22833; -.
DR SMR; O22833; -.
DR BioGRID; 4308; 18.
DR IntAct; O22833; 18.
DR PaxDb; O22833; -.
DR PRIDE; O22833; -.
DR ProteomicsDB; 238778; -.
DR EnsemblPlants; AT2G43700.1; AT2G43700.1; AT2G43700.
DR GeneID; 818972; -.
DR Gramene; AT2G43700.1; AT2G43700.1; AT2G43700.
DR KEGG; ath:AT2G43700; -.
DR Araport; AT2G43700; -.
DR TAIR; locus:2043909; AT2G43700.
DR eggNOG; ENOG502QR0Z; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; O22833; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O22833; -.
DR PRO; PR:O22833; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22833; baseline and differential.
DR Genevisible; O22833; 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; 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 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..658
FT /note="L-type lectin-domain containing receptor kinase V.4"
FT /id="PRO_0000403092"
FT TOPO_DOM 26..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 334..592
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..248
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 460
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 340..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 658 AA; 73906 MW; 66E871108F732BB1 CRC64;
MSRTIGSRVI FLILALFCCT ENSRGKLVMQ GSAGFFKGYR TLTSTKKHAY GQAFEDEIVP
FKNSANDTVT SFSVTFFFAI APEDKHKGAH GMAFVISPTR GITGASADQY LGIFNKANNG
DSSNHVIAVE LDINKDEEFG DINDNHVGIN INGMRSIKFA PAGYYDQEGQ FKDLSLISGS
LLRVTILYSQ MEKQLNVTLS SPEEAYYPNK PLLSLNQDLS PYILENMYVG FSASTGSVRA
MHYMLSWFVH GGVDVPNLDL GIPTFPPYPK EKSLVYRIVL VTSLALVLFV ALVASALSIF
FYRRHKKVKE VLEEWEIQCG PHRFAYKELF KATKGFKQLL GKGGFGQVFK GTLPGSDAEI
AVKRISHDSK QGMQEFLAEI STIGRLRHQN LVRLQGYCRY KEELYLVYDF MPNGSLDKYL
YHRANQEQLT WNQRFKIIKD IASALCYLHH EWVQVVIHRD IKPANVLIDH QMNARLGDFG
LAKLYDQGYD PQTSRVAGTF WYIAPELIRS GRATTGTDVY AFGLFMLEVS CGRRLIERRT
ASDEVVLAEW TLKCWENGDI LEAVNDGIRH EDNREQLELV LKLGVLCSHQ AVAIRPDMSK
VVQILGGDLQ LPDNLLDIVK AEKVRMWSET SESVLGVLTS QGSIGTLTLT EPFTSRGR
