LYK2_ARATH
ID LYK2_ARATH Reviewed; 654 AA.
AC Q9SGI7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein LYK2;
DE AltName: Full=LysM domain receptor-like kinase 2;
DE AltName: Full=LysM-containing receptor-like kinase 2;
DE Flags: Precursor;
GN Name=LYK2; OrderedLocusNames=At3g01840; ORFNames=F28J7.37;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
CC -!- FUNCTION: May recognize microbe-derived N-acetylglucosamine (NAG)-
CC containing ligands. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
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; AC010797; AAF03457.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73723.1; -; Genomic_DNA.
DR RefSeq; NP_186833.1; NM_111050.2.
DR AlphaFoldDB; Q9SGI7; -.
DR SMR; Q9SGI7; -.
DR STRING; 3702.AT3G01840.1; -.
DR PaxDb; Q9SGI7; -.
DR PRIDE; Q9SGI7; -.
DR ProteomicsDB; 238533; -.
DR EnsemblPlants; AT3G01840.1; AT3G01840.1; AT3G01840.
DR GeneID; 820047; -.
DR Gramene; AT3G01840.1; AT3G01840.1; AT3G01840.
DR KEGG; ath:AT3G01840; -.
DR Araport; AT3G01840; -.
DR TAIR; locus:2082359; AT3G01840.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_99_1_1; -.
DR InParanoid; Q9SGI7; -.
DR OMA; REWMDSA; -.
DR OrthoDB; 298310at2759; -.
DR PhylomeDB; Q9SGI7; -.
DR PRO; PR:Q9SGI7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SGI7; baseline and differential.
DR Genevisible; Q9SGI7; 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:0004672; F:protein kinase activity; IEA:InterPro.
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 InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..654
FT /note="Protein LYK2"
FT /id="PRO_0000420828"
FT TOPO_DOM 26..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 177..217
FT /note="LysM; degenerate"
FT DOMAIN 324..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..338
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 CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..102
FT /evidence="ECO:0000250"
FT DISULFID 57..163
FT /evidence="ECO:0000250"
FT DISULFID 100..161
FT /evidence="ECO:0000250"
SQ SEQUENCE 654 AA; 73162 MW; 7062B2519B9B3F7A CRC64;
MAVSVSKQYM TSLVVILLFI SLSSLSPTST SHSCDPVEEE EEASSFGYVC HSNLQKCHTF
AILRAKPPFY SLSDLSRHLG LDADDEYVPK GQLLLIPIEC RCNGSIYEAS LIKNCVKGDT
FRSVSQSLQG LTTCLSIREK NPHISEDKLG DNIKLRLAIR CSCPQEGVSN ASFLVTYPVG
VRDSVSSLAV RFNTTEDAIV SANNKSGVVP LKPALIPLDH KPEKQGSRKR NPSKKKRSKM
KLMIAVSSAI AGVCGLVTLM VFGYLHWKKE TQIQTQTQKW ISNKDPETRQ LSLSIRTTSD
KKISFEGSQD GSILDSHNTV GTTTPRKPVL EIYAFEELEK ATENFSSSNH IKGSVYFGSL
KGKDLAIKQV NADEMKRFDF GLLNDQSHYY NHNVIRVLGT CFREIDQDSY LVFEYARNGS
LWDWIQNKLA IKNQFIESCY CFLAWKQRIK ICHDVAIALK YMHRINYVHG NIKSRNIFLN
EDLRGKVGNF GMSKCVTNEL ATEENLIESS LSPASDIFAY GIIVMEVLSG QTPDMLLGLQ
EVETTSLGTQ ETFVSEWSRL RRLLGDKEKL REVMDSTLGE SYSVDSAFEI ASIARDCTAE
EAESRPSAVE IAERVSRLVD DDEDEEDEAV IDRESTLISE SSYKPLVKKS SIID
