LYM2_ARATH
ID LYM2_ARATH Reviewed; 350 AA.
AC O23006; Q8L9K9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=LysM domain-containing GPI-anchored protein 2;
DE AltName: Full=Chitin elicitor-binding protein LYM2;
DE Short=CEBiP LYM2;
DE Flags: Precursor;
GN Name=LYM2; OrderedLocusNames=At2g17120; ORFNames=F6P23.25;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH CHITIN.
RC STRAIN=cv. Columbia;
RX PubMed=22891159; DOI=10.1093/pcp/pcs113;
RA Shinya T., Motoyama N., Ikeda A., Wada M., Kamiya K., Hayafune M., Kaku H.,
RA Shibuya N.;
RT "Functional characterization of CEBiP and CERK1 homologs in Arabidopsis and
RT rice reveals the presence of different chitin receptor systems in plants.";
RL Plant Cell Physiol. 53:1696-1706(2012).
CC -!- FUNCTION: Chitin elicitor-binding protein involved in the perception of
CC chitin oligosaccharide elicitor. {ECO:0000269|PubMed:22891159}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with CERK1 (By similarity).
CC Binds to chitin oligosaccharide elicitor. {ECO:0000250,
CC ECO:0000269|PubMed:22891159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
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DR EMBL; CP002685; AEC06587.1; -; Genomic_DNA.
DR EMBL; AF428464; AAL16233.1; -; mRNA.
DR EMBL; AY056221; AAL07070.1; -; mRNA.
DR EMBL; AY125560; AAM78070.1; -; mRNA.
DR EMBL; AY088373; AAM65912.1; -; mRNA.
DR PIR; C84548; C84548.
DR RefSeq; NP_565406.1; NM_127266.4.
DR AlphaFoldDB; O23006; -.
DR SMR; O23006; -.
DR STRING; 3702.AT2G17120.1; -.
DR PaxDb; O23006; -.
DR PRIDE; O23006; -.
DR ProteomicsDB; 239030; -.
DR EnsemblPlants; AT2G17120.1; AT2G17120.1; AT2G17120.
DR GeneID; 816217; -.
DR Gramene; AT2G17120.1; AT2G17120.1; AT2G17120.
DR KEGG; ath:AT2G17120; -.
DR Araport; AT2G17120; -.
DR TAIR; locus:2827686; AT2G17120.
DR eggNOG; ENOG502QQ9K; Eukaryota.
DR HOGENOM; CLU_047073_0_0_1; -.
DR InParanoid; O23006; -.
DR OMA; IQCALLC; -.
DR OrthoDB; 988909at2759; -.
DR PhylomeDB; O23006; -.
DR PRO; PR:O23006; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O23006; baseline and differential.
DR Genevisible; O23006; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008061; F:chitin binding; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; -; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00257; LysM; 2.
DR PROSITE; PS51782; LYSM; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Chitin-binding; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Plant defense; Reference proteome; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..318
FT /note="LysM domain-containing GPI-anchored protein 2"
FT /id="PRO_0000021629"
FT PROPEP 319..350
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021630"
FT DOMAIN 108..155
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 172..216
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT BINDING 114..120
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 142..149
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT LIPID 318
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
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 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..97
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 38..161
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 95..159
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 97..161
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 221..253
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 248..277
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT CONFLICT 227
FT /note="K -> N (in Ref. 4; AAM65912)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="G -> R (in Ref. 4; AAM65912)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="Q -> R (in Ref. 4; AAM65912)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="D -> G (in Ref. 4; AAM65912)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="N -> S (in Ref. 4; AAM65912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 37739 MW; 9E31B3CCD71F4813 CRC64;
METSCFTLLG LLVSLSFFLT LSAQMTGNFN CSGSTSTCQS LVGYSSKNAT TLRNIQTLFA
VKNLRSILGA NNLPLNTSRD QRVNPNQVVR VPIHCSCSNG TGVSNRDIEY TIKKDDILSF
VATEIFGGLV TYEKISEVNK IPDPNKIEIG QKFWIPLPCS CDKLNGEDVV HYAHVVKLGS
SLGEIAAQFG TDNTTLAQLN GIIGDSQLLA DKPLDVPLKA CSSSVRKDSL DAPLLLSNNS
YVFTANNCVK CTCDALKNWT LSCQSSSEIK PSNWQTCPPF SQCDGALLNA SCRQPRDCVY
AGYSNQTIFT TASPACPDSA GPDNYASTLS SSFNFVIVLI QCALLCLCLL
