LRK21_ARATH
ID LRK21_ARATH Reviewed; 674 AA.
AC Q9FIF1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable L-type lectin-domain containing receptor kinase II.1;
DE Short=LecRK-II.1;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK21; OrderedLocusNames=At5g59260; ORFNames=MNC17.17;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 [4]
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; AB016890; BAB09771.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97163.1; -; Genomic_DNA.
DR RefSeq; NP_200734.1; NM_125316.2.
DR AlphaFoldDB; Q9FIF1; -.
DR SMR; Q9FIF1; -.
DR BioGRID; 21288; 9.
DR IntAct; Q9FIF1; 9.
DR PaxDb; Q9FIF1; -.
DR PRIDE; Q9FIF1; -.
DR ProteomicsDB; 238393; -.
DR EnsemblPlants; AT5G59260.1; AT5G59260.1; AT5G59260.
DR GeneID; 836044; -.
DR Gramene; AT5G59260.1; AT5G59260.1; AT5G59260.
DR KEGG; ath:AT5G59260; -.
DR Araport; AT5G59260; -.
DR TAIR; locus:2168509; AT5G59260.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9FIF1; -.
DR OMA; FNKTMFV; -.
DR OrthoDB; 418528at2759; -.
DR PhylomeDB; Q9FIF1; -.
DR PRO; PR:Q9FIF1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIF1; baseline and differential.
DR Genevisible; Q9FIF1; 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; 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; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..674
FT /note="Probable L-type lectin-domain containing receptor
FT kinase II.1"
FT /id="PRO_0000403081"
FT TOPO_DOM 25..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 355..633
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..274
FT /note="Legume-lectin like"
FT ACT_SITE 480
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 361..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 74484 MW; 1759CA3FD695CD6C CRC64;
MAGVLGSVVF WLIIGIHVTF LVFAQEGDHF VYYDFRNADL ELDGMANTNH GPLHLTNNTN
TGTGHAFYNI PIKFTASSLS SFSFSTEFVF AIFPLQKSTY GHGMAFVVSP TKDLRSNGSA
NSNLGIFNRA NDNKTATHIF AVELDTNQNS ESFDKGGNDV GIDINSIVSV ESADASYFNA
RKGKNISLPL ASGKSILVWI DYDGIEKVLN VTLAPVQTPK PDSPYFSSFI KPKVPLLSRS
INLSEIFTET MYVGFSGSTG SIKSNQYILG WSFKQGGKAE SLDISRLSNP PPSPKRFPLK
EVLGATISTI AFLTLGGIVY LYKKKKYAEV LEQWEKEYSP QRYSFRILYK ATKGFRENQL
LGAGGFGKVY KGILPSGTQI AVKRVYHDAE QGMKQYVAEI ASMGRLRHKN LVHLLGYCRR
KGELLLVYDY MPNGSLDDYL FHKNKLKDLT WSQRVNIIKG VASALLYLHE EWEQVVLHRD
IKASNILLDA DLNGKLGDFG LARFHDRGVN LEATRVVGTI GYMAPELTAM GVTTTCTDVY
AFGAFILEVV CGRRPVDPDA PREQVILVKW VASCGKRDAL TDTVDSKLID FKVEEAKLLL
KLGMLCSQIN PENRPSMRQI LQYLEGNVSV PAISFGTVAL GIPNISHETV TQMTTTSSSA
NFSFEDVTVL FGGR
