LRK62_ARATH
ID LRK62_ARATH Reviewed; 682 AA.
AC Q9M021;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=L-type lectin-domain containing receptor kinase VI.2 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-VI.2 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Lectin receptor kinase A4.1 {ECO:0000303|Ref.4};
DE Flags: Precursor;
GN Name=LECRK62 {ECO:0000303|PubMed:19773388};
GN Synonyms=LECRKA4.1 {ECO:0000303|Ref.4};
GN OrderedLocusNames=At5g01540 {ECO:0000312|Araport:AT5G01540};
GN ORFNames=F7A7.60 {ECO:0000312|EMBL:CAB82270.1};
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=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 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, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18987212; DOI=10.1104/pp.108.130583;
RA Xin Z., Wang A., Yang G., Gao P., Zheng Z.-L.;
RT "The Arabidopsis a4 subfamily of lectin receptor kinases negatively
RT regulates abscisic acid response in seed germination.";
RL Plant Physiol. 149:434-444(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 negative regulation of abscisic acid response in
CC seed germination. {ECO:0000269|PubMed:18987212}.
CC -!- FUNCTION: Involved in resistance response to the pathogenic bacteria
CC 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:0000269|PubMed:18987212};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the vascular system and
CC trichomes of the leaves. Also expressed in guard cells, anthers,
CC stigmas and germinating seeds, but not found in petals or roots.
CC Increased susceptibility to the bacteria Pseudomonas syringae,
CC characterized by stronger necrotic symptoms and higher bacterial
CC proliferation (PubMed:25083911). {ECO:0000269|PubMed:18987212,
CC ECO:0000269|PubMed:25083911}.
CC -!- DISRUPTION PHENOTYPE: Slight enhancement in abscisic acid-inhibited
CC germination. Redundant with LECRKA4.2 and LECRKA4.3.
CC {ECO:0000269|PubMed:18987212}.
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; AL161946; CAB82270.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90358.1; -; Genomic_DNA.
DR EMBL; AF361597; AAK32765.1; -; mRNA.
DR EMBL; BT000489; AAN18058.1; -; mRNA.
DR PIR; T48175; T48175.
DR RefSeq; NP_195774.1; NM_120232.2.
DR AlphaFoldDB; Q9M021; -.
DR SMR; Q9M021; -.
DR BioGRID; 16998; 25.
DR IntAct; Q9M021; 23.
DR STRING; 3702.AT5G01540.1; -.
DR PaxDb; Q9M021; -.
DR PRIDE; Q9M021; -.
DR ProteomicsDB; 238801; -.
DR EnsemblPlants; AT5G01540.1; AT5G01540.1; AT5G01540.
DR GeneID; 831722; -.
DR Gramene; AT5G01540.1; AT5G01540.1; AT5G01540.
DR KEGG; ath:AT5G01540; -.
DR Araport; AT5G01540; -.
DR TAIR; locus:2149780; AT5G01540.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9M021; -.
DR OMA; WNARFEI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9M021; -.
DR PRO; PR:Q9M021; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M021; differential.
DR Genevisible; Q9M021; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009845; P:seed germination; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Lectin; Membrane; Nucleotide-binding;
KW Plant defense; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..682
FT /note="L-type lectin-domain containing receptor kinase
FT VI.2"
FT /id="PRO_0000364129"
FT TOPO_DOM 27..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 367..641
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 29..277
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 494
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 373..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 682 AA; 75868 MW; C19750EC2E8E470F CRC64;
MGTQRSMFIV SFLFKLFLFL SVHVRAQRTT TNFAFRGFNG NQSKIRIEGA AMIKPDGLLR
LTDRKSNVTG TAFYHKPVRL LNRNSTNVTI RSFSTSFVFV IIPSSSSNKG FGFTFTLSPT
PYRLNAGSAQ YLGVFNKENN GDPRNHVFAV EFDTVQGSRD DNTDRIGNDI GLNYNSRTSD
LQEPVVYYNN DDHNKKEDFQ LESGNPIQAL LEYDGATQML NVTVYPARLG FKPTKPLISQ
HVPKLLEIVQ EEMYVGFTAS TGKGQSSAHY VMGWSFSSGG ERPIADVLIL SELPPPPPNK
AKKEGLNSQV IVMIVALSAV MLVMLVLLFF FVMYKKRLGQ EETLEDWEID HPRRLRYRDL
YVATDGFKKT GIIGTGGFGT VFKGKLPNSD PIAVKKIIPS SRQGVREFVA EIESLGKLRH
KNLVNLQGWC KHKNDLLLIY DYIPNGSLDS LLYTVPRRSG AVLSWNARFQ IAKGIASGLL
YLHEEWEKIV IHRDVKPSNV LIDSKMNPRL GDFGLARLYE RGTLSETTAL VGTIGYMAPE
LSRNGNPSSA SDVFAFGVLL LEIVCGRKPT DSGTFFLVDW VMELHANGEI LSAIDPRLGS
GYDGGEARLA LAVGLLCCHQ KPASRPSMRI VLRYLNGEEN VPEIDDEWGY SKSSRSEFGS
KLVGYVSSTS ITRVSSTSRI SQ
