LRK31_ARATH
ID LRK31_ARATH Reviewed; 627 AA.
AC Q9ZW09;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable inactive L-type lectin-domain containing receptor kinase III.1;
DE Short=LecRK-III.1;
DE Flags: Precursor;
GN Name=LECRK31; OrderedLocusNames=At2g29220; ORFNames=F16P2.40;
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 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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; AC004561; AAC95213.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08224.1; -; Genomic_DNA.
DR PIR; H84693; H84693.
DR RefSeq; NP_180485.1; NM_128478.2.
DR AlphaFoldDB; Q9ZW09; -.
DR SMR; Q9ZW09; -.
DR PaxDb; Q9ZW09; -.
DR PRIDE; Q9ZW09; -.
DR ProteomicsDB; 238563; -.
DR EnsemblPlants; AT2G29220.1; AT2G29220.1; AT2G29220.
DR GeneID; 817471; -.
DR Gramene; AT2G29220.1; AT2G29220.1; AT2G29220.
DR KEGG; ath:AT2G29220; -.
DR Araport; AT2G29220; -.
DR TAIR; locus:2043162; AT2G29220.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9ZW09; -.
DR OMA; KKITCTT; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZW09; -.
DR PRO; PR:Q9ZW09; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW09; baseline and differential.
DR Genevisible; Q9ZW09; 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: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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Lectin; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..627
FT /note="Probable inactive L-type lectin-domain containing
FT receptor kinase III.1"
FT /id="PRO_0000403083"
FT TOPO_DOM 24..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 353..623
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..262
FT /note="Legume-lectin like"
FT REGION 272..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 381
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 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 627 AA; 68789 MW; 91D9F8100BE1ABB1 CRC64;
MITFKSIALT IIFLSYFVSC VSSQRETKFL NHGFLGANLL NFGSSKVYPS GLLELTNTSM
RQIGQAFHGF PIPLSNPNST NSVSFSTSFI FAITQGTGAP GHGLAFVISP SMDFSGAFPS
NYLGLFNTSN NGNSLNRILA IEFDTVQAVE LNDIDDNHVG IDLNGVISIA SAPAAYFDDR
EAKNISLRLA SGKPVRVWIE YNATETMLNV TLAPLDRPKP SIPLLSRKMN LSGIFSQEHH
VGFSASTGTV ASSHFVLGWS FNIEGKESDF DITKLPSLPD PPPTLSPSPS PPVSTEKKSN
NTMLIIIVAA SATVALMILI FSGFWFLRRD KIFFIGGARK FSYQTISNAT GGFDNSKLLG
ERNSGSFYKG QLAPTEIIAV KKITCTTRQQ KTTLIAEIDA ISKIKQRNLV NLHGYCSKGK
DIYLVYEYVP NGSLDRFLFN NDRPVLTWSD RFCIIKGIAA ALQHLHGEGQ KPLIHGNVKA
SNVLLDEELN ARLGDYGQGS RHSTTGHVAP ELVNTGKVTR DTDVFAFGVL MMEIVCGRKA
IEPTKAPEEI SLVNWVLQGF KKGDLLMSCD TRINRENLVA REVLLVLKTG LLCANRSPES
RPMMKNVFRY LEGTEALPHD DYLFYGV
