LRK91_ARATH
ID LRK91_ARATH Reviewed; 651 AA.
AC Q9LXA5;
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 IX.1 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-IX.1 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=LECRK91 {ECO:0000303|PubMed:19773388};
GN OrderedLocusNames=At5g10530 {ECO:0000312|Araport:AT5G10530};
GN ORFNames=F12B17.120 {ECO:0000312|EMBL:CAB89390.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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).
RN [7]
RP FUNCTION, MUTAGENESIS OF 458-ARG-ASP-459 AND ASP-459, DISRUPTION PHENOTYPE,
RP INTERACTION WITH ABCG40, AND MISCELLANEOUS.
RC STRAIN=cv. Columbia;
RX PubMed=26011556; DOI=10.1094/mpmi-02-15-0025-r;
RA Wang Y., Cordewener J.H.G., America A.H.P., Shan W., Bouwmeester K.,
RA Govers F.;
RT "Arabidopsis lectin receptor kinases LecRK-IX.1 and LecRK-IX.2 are
RT functional analogs in regulating phytophthora resistance and plant cell
RT death.";
RL Mol. Plant Microbe Interact. 28:1032-1048(2015).
CC -!- FUNCTION: Promotes hydrogen peroxide H(2)O(2) production and cell
CC death. {ECO:0000269|PubMed:26011556}.
CC -!- FUNCTION: Involved in resistance response to the pathogenic oomycetes
CC Phytophthora infestans and Phytophthora capsici.
CC {ECO:0000269|PubMed:25083911, ECO:0000269|PubMed:26011556}.
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 -!- SUBUNIT: Interacts with ABCG40. {ECO:0000269|PubMed:26011556}.
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 associated with reduced
CC expression of some defense genes (e.g. PR1, PDF1.2, CYP71B15 and
CC CYP81F2). However, normal defense responses to the fungal pathogen
CC Alternaria brassicicola and to the bacterial pathogen Pseudomonas
CC syringae (PubMed:25083911, PubMed:26011556). Susceptibility to P.
CC brassicae and P. capsici is enhanced in plants impaired in LECRK91 and
CC LECRK92 (PubMed:26011556). {ECO:0000269|PubMed:25083911,
CC ECO:0000269|PubMed:26011556}.
CC -!- MISCELLANEOUS: Both lectin domain and kinase activity are required for
CC resistance to oomycetes, but only the lectin domain is required to
CC trigger cell death. {ECO:0000269|PubMed:26011556}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL353995; CAB89390.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91560.1; -; Genomic_DNA.
DR EMBL; DQ446940; ABE66151.1; -; mRNA.
DR PIR; T49986; T49986.
DR RefSeq; NP_196615.1; NM_121091.2.
DR AlphaFoldDB; Q9LXA5; -.
DR SMR; Q9LXA5; -.
DR BioGRID; 16196; 5.
DR IntAct; Q9LXA5; 5.
DR STRING; 3702.AT5G10530.1; -.
DR PaxDb; Q9LXA5; -.
DR PRIDE; Q9LXA5; -.
DR ProteomicsDB; 238524; -.
DR EnsemblPlants; AT5G10530.1; AT5G10530.1; AT5G10530.
DR GeneID; 830918; -.
DR Gramene; AT5G10530.1; AT5G10530.1; AT5G10530.
DR KEGG; ath:AT5G10530; -.
DR Araport; AT5G10530; -.
DR TAIR; locus:2142499; AT5G10530.
DR eggNOG; ENOG502QQSK; Eukaryota.
DR HOGENOM; CLU_000288_62_6_1; -.
DR InParanoid; Q9LXA5; -.
DR OMA; VWIAYNA; -.
DR PhylomeDB; Q9LXA5; -.
DR PRO; PR:Q9LXA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXA5; differential.
DR Genevisible; Q9LXA5; 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; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR GO; GO:0010726; P:positive regulation of hydrogen peroxide metabolic process; 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 1: Evidence at protein 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..651
FT /note="L-type lectin-domain containing receptor kinase
FT IX.1"
FT /id="PRO_0000403103"
FT TOPO_DOM 20..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 335..616
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 20..251
FT /note="Legume-lectin like"
FT /evidence="ECO:0000305"
FT REGION 630..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 459
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 341..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 23
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 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 458..459
FT /note="RD->AA: In LecRK-IX.1-AA; loss of kinase activity
FT and impaired ability to mediate resistance to
FT Phytophthora."
FT /evidence="ECO:0000269|PubMed:26011556"
FT MUTAGEN 459
FT /note="D->N: In LecRK-IX.1-RN; loss of kinase activity and
FT impaired ability to mediate resistance to Phytophthora."
FT /evidence="ECO:0000269|PubMed:26011556"
SQ SEQUENCE 651 AA; 72005 MW; AF662D98BC8407BD CRC64;
MANSILLFSF VLVLPFVCSV QFNISRFGSD VSEIAYQGDA RANGAVELTN IDYTCRAGWA
TYGKQVPLWN PGTSKPSDFS TRFSFRIDTR NVGYGNYGHG FAFFLAPARI QLPPNSAGGF
LGLFNGTNNQ SSAFPLVYVE FDTFTNPEWD PLDVKSHVGI NNNSLVSSNY TSWNATSHNQ
DIGRVLIFYD SARRNLSVSW TYDLTSDPLE NSSLSYIIDL SKVLPSEVTI GFSATSGGVT
EGNRLLSWEF SSSLELIDIK KSQNDKKGMI IGISVSGFVL LTFFITSLIV FLKRKQQKKK
AEETENLTSI NEDLERGAGP RKFTYKDLAS AANNFADDRK LGEGGFGAVY RGYLNSLDMM
VAIKKFAGGS KQGKREFVTE VKIISSLRHR NLVQLIGWCH EKDEFLMIYE FMPNGSLDAH
LFGKKPHLAW HVRCKITLGL ASALLYLHEE WEQCVVHRDI KASNVMLDSN FNAKLGDFGL
ARLMDHELGP QTTGLAGTFG YMAPEYISTG RASKESDVYS FGVVTLEIVT GRKSVDRRQG
RVEPVTNLVE KMWDLYGKGE VITAIDEKLR IGGFDEKQAE CLMIVGLWCA HPDVNTRPSI
KQAIQVLNLE APVPHLPTKM PVATYHVSSS NTTSVSSGGA TVTFSSAQHG R
