LRKS5_ARATH
ID LRKS5_ARATH Reviewed; 652 AA.
AC Q9FG33;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable L-type lectin-domain containing receptor kinase S.5;
DE Short=LecRK-S.5;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRKS5; OrderedLocusNames=At5g06740; ORFNames=MPH15.10;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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; AP002032; BAB09808.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91057.1; -; Genomic_DNA.
DR RefSeq; NP_196292.1; NM_120757.2.
DR AlphaFoldDB; Q9FG33; -.
DR SMR; Q9FG33; -.
DR BioGRID; 15842; 1.
DR STRING; 3702.AT5G06740.1; -.
DR PaxDb; Q9FG33; -.
DR PRIDE; Q9FG33; -.
DR EnsemblPlants; AT5G06740.1; AT5G06740.1; AT5G06740.
DR GeneID; 830563; -.
DR Gramene; AT5G06740.1; AT5G06740.1; AT5G06740.
DR KEGG; ath:AT5G06740; -.
DR Araport; AT5G06740; -.
DR TAIR; locus:2170224; AT5G06740.
DR eggNOG; ENOG502QT06; Eukaryota.
DR HOGENOM; CLU_000288_62_6_1; -.
DR InParanoid; Q9FG33; -.
DR OMA; ILTIACK; -.
DR PhylomeDB; Q9FG33; -.
DR PRO; PR:Q9FG33; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG33; baseline and differential.
DR Genevisible; Q9FG33; 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; IPR019825; Lectin_legB_Mn/Ca_BS.
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; PS00307; LECTIN_LEGUME_BETA; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..652
FT /note="Probable L-type lectin-domain containing receptor
FT kinase S.5"
FT /id="PRO_0000403107"
FT TOPO_DOM 21..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 330..622
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..257
FT /note="Legume-lectin like"
FT ACT_SITE 455
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 336..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
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 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 652 AA; 72868 MW; BA09031B83556AB7 CRC64;
MRFSLAWKLL FLILTCKIET QVKCLKFDFP GFNVSNELEL IRDNSYIVFG AIQVTPDVTG
GPGGTIANQA GRALYKKPFR LWSKHKSATF NTTFVINISN KTDPGGEGLA FVLTPEETAP
QNSSGMWLGM VNERTNRNNE SRIVSVEFDT RKSHSDDLDG NHVALNVNNI NSVVQESLSG
RGIKIDSGLD LTAHVRYDGK NLSVYVSRNL DVFEQRNLVF SRAIDLSAYL PETVYVGFTA
STSNFTELNC VRSWSFEGLK IDGDGNMLWL WITIPIVFIV GIGAFLGALY LRSRSKAGET
NPDIEAELDN CAANPQKFKL RELKRATGNF GAENKLGQGG FGMVFKGKWQ GRDIAVKRVS
EKSHQGKQEF IAEITTIGNL NHRNLVKLLG WCYERKEYLL VYEYMPNGSL DKYLFLEDKS
RSNLTWETRK NIITGLSQAL EYLHNGCEKR ILHRDIKASN VMLDSDFNAK LGDFGLARMI
QQSEMTHHST KEIAGTPGYM APETFLNGRA TVETDVYAFG VLMLEVVSGK KPSYVLVKDN
QNNYNNSIVN WLWELYRNGT ITDAADPGMG NLFDKEEMKS VLLLGLACCH PNPNQRPSMK
TVLKVLTGET SPPDVPTERP AFVWPAMPPS FSDIDYSLTG SQINSLTELT GR
