LYM3_ARATH
ID LYM3_ARATH Reviewed; 423 AA.
AC Q6NPN4; Q9CAP5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=LysM domain-containing GPI-anchored protein 3;
DE Flags: Precursor;
GN Name=LYM3; OrderedLocusNames=At1g77630; ORFNames=T5M16.22;
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PEPTIDOGLYCAN.
RC STRAIN=cv. Columbia;
RX PubMed=22106285; DOI=10.1073/pnas.1112862108;
RA Willmann R., Lajunen H.M., Erbs G., Newman M.-A., Kolb D., Tsuda K.,
RA Katagiri F., Fliegmann J., Bono J.-J., Cullimore J.V., Jehle A.K.,
RA Goetz F., Kulik A., Molinaro A., Lipka V., Gust A.A., Nuernberger T.;
RT "Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial
RT peptidoglycan sensing and immunity to bacterial infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19824-19829(2011).
CC -!- FUNCTION: Required as a cell surface receptor for peptidoglycan (PGN)
CC elicitor signaling leading to innate immunity. Plays an essential role
CC in detecting PGNs and restricting bacterial growth (of Pseudomonas
CC syringae pv. tomato DC3000 for example). {ECO:0000269|PubMed:22106285}.
CC -!- SUBUNIT: Interacts with peptidoglycans. {ECO:0000269|PubMed:22106285}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- DISRUPTION PHENOTYPE: Impaired sensitivity to peptidoglycans (PGNs)
CC leading to higher susceptibility to infection with virulent Pseudomonas
CC syringae pv. tomato DC3000. {ECO:0000269|PubMed:22106285}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51658.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010704; AAG51658.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36002.1; -; Genomic_DNA.
DR EMBL; BT010885; AAR24663.1; -; mRNA.
DR EMBL; AK176769; BAD44532.1; -; mRNA.
DR PIR; H96805; H96805.
DR RefSeq; NP_177886.2; NM_106411.4.
DR AlphaFoldDB; Q6NPN4; -.
DR SMR; Q6NPN4; -.
DR STRING; 3702.AT1G77630.1; -.
DR PaxDb; Q6NPN4; -.
DR PRIDE; Q6NPN4; -.
DR ProteomicsDB; 238684; -.
DR EnsemblPlants; AT1G77630.1; AT1G77630.1; AT1G77630.
DR GeneID; 844098; -.
DR Gramene; AT1G77630.1; AT1G77630.1; AT1G77630.
DR KEGG; ath:AT1G77630; -.
DR Araport; AT1G77630; -.
DR TAIR; locus:2204720; AT1G77630.
DR eggNOG; ENOG502QWAT; Eukaryota.
DR HOGENOM; CLU_047073_3_0_1; -.
DR InParanoid; Q6NPN4; -.
DR OrthoDB; 873442at2759; -.
DR PhylomeDB; Q6NPN4; -.
DR PRO; PR:Q6NPN4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NPN4; baseline and differential.
DR Genevisible; Q6NPN4; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IMP:TAIR.
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 SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Plant defense; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..394
FT /note="LysM domain-containing GPI-anchored protein 3"
FT /id="PRO_0000252123"
FT PROPEP 395..423
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000252124"
FT DOMAIN 107..154
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 173..216
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT LIPID 394
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
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 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..97
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 37..160
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 95..158
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 97..160
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 221..253
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 248..276
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
SQ SEQUENCE 423 AA; 44152 MW; B067C6FEBD5ED6D0 CRC64;
MKNPEKPLLL FLILASSLAS MATAKSTIEP CSSKDTCNSL LGYTLYTDLK VTEVASLFQV
DPVSMLLSNS IDISYPDVEN HVLPAKLFLK IPITCSCVDG IRKSLSTHYK TRTSDTLGSI
ADSVYGGLVS PEQIQVANSE TDLSVLDVGT KLVIPLPCAC FNGTDESLPA LYLSYVVRGI
DTMAGIAKRF STSVTDLTNV NAMGAPDINP GDILAVPLLA CSSNFPKYAT DYGLIIPNGS
YALTAGHCVQ CSCVLGSRSM YCEPASISVS CSSMRCRNSN FMLGNITSQQ SSSGCKLTTC
SYNGFASGTI LTTLSMSLQP RCPGPQQLAP LIAPPDNVPK ELMYLPSPSP SPSPEFDDIA
GGGSSIAAVP AASPGGATVS SSNSIPGNPA NGPGGSISIA SCPLSYYSFI ALLIPIGSCF
FVF
