LYK3_ARATH
ID LYK3_ARATH Reviewed; 651 AA.
AC F4IB81; Q9FZA7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=LysM domain receptor-like kinase 3;
DE Short=LysM-containing receptor-like kinase 3;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=LYK3; OrderedLocusNames=At1g51940; ORFNames=T14L22.13;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
CC -!- FUNCTION: Putative Lysin motif (LysM) receptor kinase that may
CC recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99862.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BX816305; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BX816305; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC015448; AAF99862.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE32737.1; -; Genomic_DNA.
DR EMBL; BX816305; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; G96558; G96558.
DR RefSeq; NP_175606.2; NM_104075.4.
DR AlphaFoldDB; F4IB81; -.
DR SMR; F4IB81; -.
DR STRING; 3702.AT1G51940.1; -.
DR iPTMnet; F4IB81; -.
DR PaxDb; F4IB81; -.
DR PRIDE; F4IB81; -.
DR ProteomicsDB; 238534; -.
DR EnsemblPlants; AT1G51940.1; AT1G51940.1; AT1G51940.
DR GeneID; 841622; -.
DR Gramene; AT1G51940.1; AT1G51940.1; AT1G51940.
DR KEGG; ath:AT1G51940; -.
DR Araport; AT1G51940; -.
DR TAIR; locus:2195814; AT1G51940.
DR eggNOG; ENOG502QR6F; Eukaryota.
DR HOGENOM; CLU_000288_99_2_1; -.
DR InParanoid; F4IB81; -.
DR OMA; NCTDTGR; -.
DR OrthoDB; 684563at2759; -.
DR PRO; PR:F4IB81; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IB81; baseline and differential.
DR Genevisible; F4IB81; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019199; F:transmembrane receptor protein kinase activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR044812; CERK1/LYK3-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46204; PTHR46204; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51782; LYSM; 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; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..651
FT /note="LysM domain receptor-like kinase 3"
FT /id="PRO_0000420829"
FT TOPO_DOM 20..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 142..186
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 341..628
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 196..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 347..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 410
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 513
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
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 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..76
FT /evidence="ECO:0000250"
FT DISULFID 31..133
FT /evidence="ECO:0000250"
FT DISULFID 74..131
FT /evidence="ECO:0000250"
SQ SEQUENCE 651 AA; 71445 MW; F0EBF68BF9D91F2D CRC64;
MNLTFYIFFL SLLPSFSSSK PMNCSDTTRL CSSFLAFKPN QNQSFSVIQS MFDVLPQDIT
ADISGGYFFI KKNCSCLTTT HQYTTNTTFT IRQNVGYVYN VTVSAYSGLA FPPNTTRAAR
AGAVVSVQLL CGCSSGLWNY LMSYVAMAGD SVQSLSSRFG VSMDRIEDVN GILNLDNITA
GDLLYIPLDS VPGEPYETSK INPPAPSPAP ASSLANGNIS DDQVNHTAKS GSHVPYIWIV
GGLGVVLALL VLCILVCICL RSSSCSSSEE DGNGHNFQIL RKSGFFCGSG RYNCCRSGDF
RQTNGETQVV AIPKALGDGM FEIEKPMVFT YEEIRAATDE FSDSNLLGHG NYGSVYFGLL
REQEVAVKRM TATKTKEFAA EMKVLCKVHH SNLVELIGYA ATVDELFVVY EYVRKGMLKS
HLHDPQSKGN TPLSWIMRNQ IALDAARGLE YIHEHTKTHY VHRDIKTSNI LLDEAFRAKI
SDFGLAKLVE KTGEGEISVT KVVGTYGYLA PEYLSDGLAT SKSDIYAFGV VLFEIISGRE
AVIRTEAIGT KNPERRPLAS IMLAVLKNSP DSMNMSSLKE FVDPNMMDLY PHDCLFKIAT
LAKQCVDDDP ILRPNMKQVV ISLSQILLSS IEWEATLAGN SQVFSGLVQG R
