LK110_ARATH
ID LK110_ARATH Reviewed; 616 AA.
AC Q3E884;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative L-type lectin-domain containing receptor kinase I.10;
DE Short=LecRK-I.10;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK110; OrderedLocusNames=At5g60310; ORFNames=F15L12.19;
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 (APR-1999) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED97307.1; -; Genomic_DNA.
DR RefSeq; NP_200839.1; NM_125424.2.
DR AlphaFoldDB; Q3E884; -.
DR SMR; Q3E884; -.
DR PaxDb; Q3E884; -.
DR PRIDE; Q3E884; -.
DR EnsemblPlants; AT5G60310.1; AT5G60310.1; AT5G60310.
DR GeneID; 836153; -.
DR Gramene; AT5G60310.1; AT5G60310.1; AT5G60310.
DR KEGG; ath:AT5G60310; -.
DR Araport; AT5G60310; -.
DR TAIR; locus:2144055; AT5G60310.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q3E884; -.
DR OMA; TAISYQY; -.
DR OrthoDB; 346275at2759; -.
DR PhylomeDB; Q3E884; -.
DR PRO; PR:Q3E884; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E884; baseline and differential.
DR Genevisible; Q3E884; 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; PS00307; LECTIN_LEGUME_BETA; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..616
FT /note="Putative L-type lectin-domain containing receptor
FT kinase I.10"
FT /id="PRO_0000403079"
FT TOPO_DOM 23..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 343..616
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..258
FT /note="Legume-lectin like"
FT ACT_SITE 467
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 349..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
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"
SQ SEQUENCE 616 AA; 68667 MW; CBE5228CF11DAC47 CRC64;
MAWGLFQILM ISFFHLIKLS SQQETSFVYE TFRSQENLYL DGSATVLPNG LLQLTNASDH
QMAHVFYKDS IELSSSKPLS FSTHFVCALV PQPGVEGGHG MAFVVSPSMD FSHAESTRYL
GIFNVSKNGS PSSNVLAVEL DTIWNPDFED IDHNHVGIDV NSPLSVGTAS ASYYSDIKGK
NESINLLSGH PIQVWVDYED NMLNVSMAPR EVQKPSRPLL SQHINLSDIY PNRRLFVGFS
AATGTAISYQ YVLSWSFSTS RGSLQRFDIS RLPEVPHPRA EHKNLSPLFI DLLGFLAIMG
LCTLTGMYFF KRGKYAEITE EWENEFGAHR FSYKSLYKAT KGFHKDGFLG KGGFGEVYRG
KLLLSREKAV KRMSHDGDQG LKQFVAEVVS MRCLKHRNLV PLLGYCRRKH EFLLVSDYMT
NGSLDEHLFD DQKPVLSWPQ RLVIIKGIAS ALCYLHTGAD QVVLHRDIKA SNIMLDAEFN
GRLGDFGMAS FHDHGGISDS TCAVGTIGYM APEILYMGAS TRTDVYAFGV FMVEVTCGRR
PVEPQLQLEK QILIEWVPES RPTMEQVILY LNQNLPLPDF SPYTVGISNH SSVLIDAASL
VASRSWSAAS SATNSP
