LYK5_ARATH
ID LYK5_ARATH Reviewed; 664 AA.
AC O22808;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein LYK5;
DE AltName: Full=LysM domain receptor-like kinase 5;
DE AltName: Full=LysM-containing receptor-like kinase 5;
DE Flags: Precursor;
GN Name=LYK5; OrderedLocusNames=At2g33580; ORFNames=F4P9.35;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY CHITIN.
RX PubMed=22744984; DOI=10.1104/pp.112.201699;
RA Wan J., Tanaka K., Zhang X.-C., Son G.H., Brechenmacher L., Nguyen T.H.N.,
RA Stacey G.;
RT "LYK4, a lysin motif receptor-like kinase, is important for chitin
RT signaling and plant innate immunity in Arabidopsis.";
RL Plant Physiol. 160:396-406(2012).
CC -!- FUNCTION: May recognize microbe-derived N-acetylglucosamine (NAG)-
CC containing ligands. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Moderately induced by chitin oligomers (e.g. chitohexaose
CC (6-mer) and chitooctaose (8-mer)). {ECO:0000269|PubMed:22744984}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC002332; AAB80675.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08855.1; -; Genomic_DNA.
DR EMBL; AF370600; AAK43919.1; -; mRNA.
DR EMBL; BT046191; ACI49790.1; -; mRNA.
DR PIR; C84747; C84747.
DR RefSeq; NP_180916.1; NM_128918.5.
DR AlphaFoldDB; O22808; -.
DR SMR; O22808; -.
DR BioGRID; 3270; 13.
DR IntAct; O22808; 10.
DR STRING; 3702.AT2G33580.1; -.
DR SwissPalm; O22808; -.
DR PaxDb; O22808; -.
DR PRIDE; O22808; -.
DR ProteomicsDB; 238746; -.
DR EnsemblPlants; AT2G33580.1; AT2G33580.1; AT2G33580.
DR GeneID; 817923; -.
DR Gramene; AT2G33580.1; AT2G33580.1; AT2G33580.
DR KEGG; ath:AT2G33580; -.
DR Araport; AT2G33580; -.
DR TAIR; locus:2050987; AT2G33580.
DR eggNOG; ENOG502QSFN; Eukaryota.
DR HOGENOM; CLU_000288_99_1_1; -.
DR InParanoid; O22808; -.
DR OMA; QNPLHDS; -.
DR OrthoDB; 560620at2759; -.
DR PhylomeDB; O22808; -.
DR PRO; PR:O22808; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22808; baseline and differential.
DR Genevisible; O22808; 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:0008061; F:chitin binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0071323; P:cellular response to chitin; IEP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..664
FT /note="Protein LYK5"
FT /id="PRO_0000420831"
FT TOPO_DOM 27..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 195..238
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 351..643
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..141
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 164..170
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 357..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..114
FT /evidence="ECO:0000250"
FT DISULFID 58..181
FT /evidence="ECO:0000250"
FT DISULFID 112..179
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 72569 MW; 4EF6E14FB1AE97E6 CRC64;
MAACTLHALS VTLFLLLFFA VSPAKAQQPY VNNHQLACEV RVYDNITNGF TCNGPPSCRS
YLTFWSQPPY NTADSIAKLL NVSAAEIQSI NNLPTATTRI PTRELVVIPA NCSCSSSSGG
FYQHNATYNL SGNRGDETYF SVANDTYQAL STCQAMMSQN RYGERQLTPG LNLLVPLRCA
CPTAKQTTAG FKYLLTYLVA MGDSISGIAE MFNSTSAAIT EGNELTSDNI FFFTPVLVPL
TTEPTKIVIS PSPPPPPVVA TPPQTPVDPP GSSSSHKWIY IGIGIGAGLL LLLSILALCF
YKRRSKKKSL PSSLPEENKL FDSSTKQSIP TTTTTQWSID LSNSSEAFGL KSAIESLTLY
RFNDLQSATS NFSDENRIKG SVYRATINGD DAAVKVIKGD VSSSEINLLK KLNHSNIIRL
SGFCIREGTS YLVFEYSENG SISDWLHSSG KKSLTWKQRV EIARDVAEAL DYLHNYITPP
HIHKNLESTN ILLDSNFRAK IANFGVARIL DEGDLDLQLT RHVEGTQGYL APEYVENGVI
TSKLDVFAFG VAVLELLSGR EAVTIHKKKE GEEEVEMLCK VINSVLGGEN VREKLKEFMD
PSLGNEYPLE LAYTMAQLAK SCVATDLNSR PSVTQVLTTL SMIVSSSIDW EPSDDLLRSG
SLGN
