LRK55_ARATH
ID LRK55_ARATH Reviewed; 661 AA.
AC Q96285; O04752; O04836;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=L-type lectin-domain containing receptor kinase V.5 {ECO:0000303|PubMed:19773388};
DE Short=Arabidopsis thaliana lectin-receptor kinase a1 {ECO:0000303|PubMed:19773388};
DE Short=Ath.lecRK1 {ECO:0000303|PubMed:19773388};
DE Short=AthlecRK-a1 {ECO:0000303|Ref.5};
DE Short=LecRK-V.5 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:8637009};
DE Flags: Precursor;
GN Name=LECRK55 {ECO:0000303|PubMed:19773388};
GN Synonyms=LECRKA1 {ECO:0000303|Ref.5};
GN OrderedLocusNames=At3g59700 {ECO:0000312|Araport:AT3G59700};
GN ORFNames=T16L24.250 {ECO:0000312|EMBL:CAB75467.1};
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 [GENOMIC DNA / MRNA], AUTOPHOSPHORYLATION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=8637009; DOI=10.1006/jmbi.1996.0286;
RA Herve C., Dabos P., Galaud J.P., Rouge P., Lescure B.;
RT "Characterization of an Arabidopsis thaliana gene that defines a new class
RT of putative plant receptor kinases with an extracellular lectin-like
RT domain.";
RL J. Mol. Biol. 258:778-788(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION, AND 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: Confers resistance to the pathogenic oomycetes Phytophthora
CC infestans and Phytophthora capsici, but confers susceptibility to the
CC pathogenic bacteria Pseudomonas syringae.
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 ECO:0000269|PubMed:8637009};
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 ECO:0000269|PubMed:8637009};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10350082};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in stems, leaves, flowers
CC and siliques. {ECO:0000269|PubMed:8637009}.
CC -!- PTM: Autophosphorylated on a Ser residue. {ECO:0000269|PubMed:8637009}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to the oomycetes
CC Phytophthora brassicae and Phytophthora capsici but enhanced resistance
CC to the pathogenic bacteria Pseudomonas syringae.
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; AF001168; AAB58725.1; -; Genomic_DNA.
DR EMBL; X91630; CAA62824.1; -; mRNA.
DR EMBL; AL138659; CAB75467.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79957.1; -; Genomic_DNA.
DR PIR; S68589; S68589.
DR RefSeq; NP_191529.1; NM_115832.3.
DR AlphaFoldDB; Q96285; -.
DR SMR; Q96285; -.
DR BioGRID; 10453; 10.
DR IntAct; Q96285; 10.
DR STRING; 3702.AT3G59700.1; -.
DR iPTMnet; Q96285; -.
DR PaxDb; Q96285; -.
DR PRIDE; Q96285; -.
DR ProteomicsDB; 238523; -.
DR EnsemblPlants; AT3G59700.1; AT3G59700.1; AT3G59700.
DR GeneID; 825139; -.
DR Gramene; AT3G59700.1; AT3G59700.1; AT3G59700.
DR KEGG; ath:AT3G59700; -.
DR Araport; AT3G59700; -.
DR TAIR; locus:2097493; AT3G59700.
DR eggNOG; ENOG502QR0Z; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q96285; -.
DR OMA; WIVELWE; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q96285; -.
DR PRO; PR:Q96285; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96285; baseline and differential.
DR Genevisible; Q96285; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
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:1900425; P:negative regulation of defense response to bacterium; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; 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; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..661
FT /note="L-type lectin-domain containing receptor kinase V.5"
FT /id="PRO_0000403093"
FT TOPO_DOM 26..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 338..596
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 30..250
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 344..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 661 AA; 74436 MW; C4833F3001314E38 CRC64;
MSRELIILCQ PILVLFLTLF YNSHGYFVSQ GSVGIGFNGY FTLTNTTKHT FGQAFENEHV
EIKNSSTGVI SSFSVNFFFA IVPEHNQQGS HGMTFVISPT RGLPGASSDQ YLGIFNKTNN
GKASNNVIAI ELDIHKDEEF GDIDDNHVGI NINGLRSVAS ASAGYYDDKD GSFKKLSLIS
REVMRLSIVY SQPDQQLNVT LFPAEIPVPP LKPLLSLNRD LSPYLLEKMY LGFTASTGSV
GAIHYLMGWL VNGVIEYPRL ELSIPVLPPY PKKTSNRTKT VLAVCLTVSV FAAFVASWIG
FVFYLRHKKV KEVLEEWEIQ YGPHRFAYKE LFNATKGFKE KQLLGKGGFG QVYKGTLPGS
DAEIAVKRTS HDSRQGMSEF LAEISTIGRL RHPNLVRLLG YCRHKENLYL VYDYMPNGSL
DKYLNRSENQ ERLTWEQRFR IIKDVATALL HLHQEWVQVI IHRDIKPANV LIDNEMNARL
GDFGLAKLYD QGFDPETSKV AGTFGYIAPE FLRTGRATTS TDVYAFGLVM LEVVCGRRII
ERRAAENEEY LVDWILELWE NGKIFDAAEE SIRQEQNRGQ VELVLKLGVL CSHQAASIRP
AMSVVMRILN GVSQLPDNLL DVVRAEKFRE WPETSMELLL LDVNTSSSLE LTDSSFVSHG
R
