LRK53_ARATH
ID LRK53_ARATH Reviewed; 664 AA.
AC O22834;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable L-type lectin-domain containing receptor kinase V.3;
DE Short=Arabidopsis thaliana lectin-receptor kinase c2;
DE Short=AthlecRK-c2;
DE Short=LecRK-V.3;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK53; Synonyms=LECRKC2; OrderedLocusNames=At2g43690;
GN ORFNames=F18O19.20;
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 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 [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).
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; AAB64037.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10308.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61263.1; -; Genomic_DNA.
DR PIR; C84869; C84869.
DR RefSeq; NP_001318417.1; NM_001337051.1.
DR RefSeq; NP_181897.1; NM_129931.2.
DR AlphaFoldDB; O22834; -.
DR SMR; O22834; -.
DR BioGRID; 4307; 8.
DR IntAct; O22834; 8.
DR PaxDb; O22834; -.
DR EnsemblPlants; AT2G43690.1; AT2G43690.1; AT2G43690.
DR EnsemblPlants; AT2G43690.3; AT2G43690.3; AT2G43690.
DR GeneID; 818971; -.
DR Gramene; AT2G43690.1; AT2G43690.1; AT2G43690.
DR Gramene; AT2G43690.3; AT2G43690.3; AT2G43690.
DR KEGG; ath:AT2G43690; -.
DR Araport; AT2G43690; -.
DR TAIR; locus:2043939; AT2G43690.
DR eggNOG; ENOG502QR0Z; Eukaryota.
DR HOGENOM; CLU_000288_62_6_1; -.
DR InParanoid; O22834; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O22834; -.
DR PRO; PR:O22834; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22834; baseline and differential.
DR Genevisible; O22834; 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; IBA:GO_Central.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; 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..664
FT /note="Probable L-type lectin-domain containing receptor
FT kinase V.3"
FT /id="PRO_0000403091"
FT TOPO_DOM 27..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 335..617
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..250
FT /note="Legume-lectin like"
FT ACT_SITE 461
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
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 69
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 122
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 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 664 AA; 74398 MW; F234E2645A8FFA6C CRC64;
MSMSCKINWL MVLVIIALSN LESSLGRLVF EGSAGLMNGF TTLTNTKKHA YGQAFNDEPF
PFKNSVNGNM TSFSFTFFFA IVPEHIDKGS HGIAFVISPT RGIPGASADQ YLGIFNDTND
GNSSNHIIAV ELDIHKDDEF GDIDDNHVGI NINGMRSIVS APAGYYDQNG QFKNLSLISG
NLLRVTILYS QEEKQLNVTL SPAEEANVPK WPLLSLNKDL SPYLSKNMYI GFTASTGSVG
AIHYMWMWYV FTFIIVPKLD FDIPTFPPYP KAESQVKLIV LVTFLTLALF VALAASALIV
FFYKRHKKLL EVLEEWEVEC GPHRFSYKEL FNATNGFKQL LGEGGFGPVF KGTLSGSNAK
IAVKRVSHDS SQGMRELLAE ISTIGRLRHP NLVRLLGYCR YKEELYLVYD FLPNGSLDKY
LYGTSDQKQL SWSQRFKIIK DVASALSYLH HGWIHVVIHR DIKPANVLID DKMNASLGDF
GLAKVYDQGY DPQTSRVAGT FGYMAPEIMR TGRPTMGTDV YAFGMFMLEV SCDRKLFEPR
AESEEAILTN WAINCWENGD IVEAATERIR QDNDKGQLEL VLKLGVLCSH EAEEVRPDMA
TVVKILNGVS ELPDNLLDIV RSEKLENWYE RYSKVIDPVT TEESIGNLAI TEPILPSGRP
RLFL
