LRK13_ARATH
ID LRK13_ARATH Reviewed; 664 AA.
AC Q9M3D8;
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.3 {ECO:0000303|PubMed:19773388};
DE Short=AtLecRK2 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-I.3 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15067507};
DE AltName: Full=Salt-responsive receptor protein kinase 1 {ECO:0000305|PubMed:15067507};
DE Flags: Precursor;
GN Name=LECRK13 {ECO:0000303|PubMed:19773388};
GN Synonyms=AtLecRK2 {ECO:0000303|PubMed:19773388},
GN SR1 {ECO:0000305|PubMed:15067507};
GN OrderedLocusNames=At3g45410 {ECO:0000312|Araport:AT3G45410};
GN ORFNames=F18N11.170 {ECO:0000312|EMBL:CAB72490.1};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, AND INDUCTION BY SALT AND
RP ETHYLENE.
RX PubMed=15067507; DOI=10.1007/s00122-004-1641-9;
RA He X.-J., Zhang Z.-G., Yan D.-Q., Zhang J.-S., Chen S.-Y.;
RT "A salt-responsive receptor-like kinase gene regulated by the ethylene
RT signaling pathway encodes a plasma membrane serine/threonine kinase.";
RL Theor. Appl. Genet. 109:377-383(2004).
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 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 fungus
CC Alternaria brassicicola. {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:15067507};
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:15067507};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15067507};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flowers, and, to a
CC lower extent, in leaves. {ECO:0000269|PubMed:15067507}.
CC -!- INDUCTION: By salt and ethylene (ET). {ECO:0000269|PubMed:15067507}.
CC -!- PTM: Autophosphorylated on Ser and Thr residues.
CC {ECO:0000269|PubMed:15067507}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to the fungus Alternaria
CC brassicicola. {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; AY376441; AAQ83688.1; -; mRNA.
DR EMBL; AL132953; CAB72490.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78027.1; -; Genomic_DNA.
DR PIR; T47481; T47481.
DR RefSeq; NP_190127.1; NM_114410.3.
DR AlphaFoldDB; Q9M3D8; -.
DR SMR; Q9M3D8; -.
DR STRING; 3702.AT3G45410.1; -.
DR iPTMnet; Q9M3D8; -.
DR PaxDb; Q9M3D8; -.
DR PRIDE; Q9M3D8; -.
DR ProteomicsDB; 238391; -.
DR EnsemblPlants; AT3G45410.1; AT3G45410.1; AT3G45410.
DR GeneID; 823679; -.
DR Gramene; AT3G45410.1; AT3G45410.1; AT3G45410.
DR KEGG; ath:AT3G45410; -.
DR Araport; AT3G45410; -.
DR TAIR; locus:2078337; AT3G45410.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9M3D8; -.
DR OMA; CTNAMPE; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9M3D8; -.
DR PRO; PR:Q9M3D8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M3D8; baseline and differential.
DR Genevisible; Q9M3D8; 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; IDA:TAIR.
DR GO; GO:0071369; P:cellular response to ethylene stimulus; IEP:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..664
FT /note="L-type lectin-domain containing receptor kinase I.3"
FT /id="PRO_0000403072"
FT TOPO_DOM 22..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 342..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..257
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 348..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 55
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 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 664 AA; 73910 MW; 29A6D323710F1FF0 CRC64;
MACRLYLALI FSCVYLICLS SQQETGFVYN GFEQADLFID GIAKILPDGL LQLTNTTELQ
MGHAFFKKPF DFDPSSSLSF YTHFVCALVP PKLGADGGHG IVFVVSPSID LSHAYATQYL
GVFSNLTNGT SSSHLLAIEL DTVKTVEFNE LEKPHVGIDL NSPISVESAL PSYFSNALGK
NISINLLSGE PIQVWVDYDG SFLNVTLAPI EIKKPNQPLI SRAINLSEIF QEKMYVGFSS
STGNLLSNHY ILGWSFSRRK EQLQSLNLST LPRVPLPKEE KKKLSPLLIG LVILLVIPVV
MVLGGVYWYR RKKYAEVKEW WEKEYGPHRF SYKSLYKATN GFRKDCRVGK GGFGEVYKGT
LPGGRHIAVK RLSHDAEQGM KQFVAEVVTM GNLQHRNLVP LLGYCRRKCE LLLVSEYMPN
GSLDQYLFHE GNPSPSWYQR ISILKDIASA LSYLHTGTKQ VVLHRDIKAS NVMLDSEFNG
RLGDFGMAKF HDRGTNLSAT AAVGTIGYMA PELITMGTSM KTDVYAFGAF LLEVICGRRP
VEPELPVGKQ YLVKWVYECW KEACLFKTRD PRLGVEFLPE EVEMVLKLGL LCTNAMPESR
PAMEQVVQYL NQDLPLPIFS PSTPGIGAFM PVSMEALSAI GVSSVRNSSV SMFVTHTILD
GHGR
