LYP6_ORYSJ
ID LYP6_ORYSJ Reviewed; 409 AA.
AC Q69T51; Q0DDQ4; Q4VVD8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=LysM domain-containing GPI-anchored protein LYP6 {ECO:0000305};
DE AltName: Full=LysM domain-containing protein 6 {ECO:0000303|PubMed:22872757};
DE Short=Os-LYP6 {ECO:0000303|PubMed:22872757};
DE Flags: Precursor;
GN Name=LYP6 {ECO:0000303|PubMed:22872757};
GN OrderedLocusNames=Os06g0208800 {ECO:0000312|PROSITE:PS51782},
GN LOC_Os06g10660 {ECO:0000305};
GN ORFNames=P0664C05.26 {ECO:0000312|EMBL:BAD35901.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhong J., Liu B., Wang H., Wang J.;
RT "GPI-anchored protein.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22872757; DOI=10.1105/tpc.112.102475;
RA Liu B., Li J.F., Ao Y., Qu J., Li Z., Su J., Zhang Y., Liu J., Feng D.,
RA Qi K., He Y., Wang J., Wang H.B.;
RT "Lysin motif-containing proteins LYP4 and LYP6 play dual roles in
RT peptidoglycan and chitin perception in rice innate immunity.";
RL Plant Cell 24:3406-3419(2012).
RN [6]
RP FUNCTION, AND INTERACTION WITH LYP4.
RX PubMed=23299421; DOI=10.4161/psb.22980;
RA Liu B., Li J.F., Ao Y., Li Z., Liu J., Feng D., Qi K., He Y., Zeng L.,
RA Wang J., Wang H.B.;
RT "OsLYP4 and OsLYP6 play critical roles in rice defense signal
RT transduction.";
RL Plant Signal. Behav. 8:E22980-E22980(2013).
RN [7]
RP INTERACTION WITH CERK1 AND CEBIP.
RX PubMed=24964058; DOI=10.1094/mpmi-03-14-0068-r;
RA Kouzai Y., Mochizuki S., Nakajima K., Desaki Y., Hayafune M., Miyazaki H.,
RA Yokotani N., Ozawa K., Minami E., Kaku H., Shibuya N., Nishizawa Y.;
RT "Targeted gene disruption of OsCERK1 reveals its indispensable role in
RT chitin perception and involvement in the peptidoglycan response and
RT immunity in rice.";
RL Mol. Plant Microbe Interact. 27:975-982(2014).
RN [8]
RP INTERACTION WITH CERK1, AND SUBCELLULAR LOCATION.
RX PubMed=25335639; DOI=10.1111/tpj.12710;
RA Ao Y., Li Z., Feng D., Xiong F., Liu J., Li J.F., Wang M., Wang J., Liu B.,
RA Wang H.B.;
RT "OsCERK1 and OsRLCK176 play important roles in peptidoglycan and chitin
RT signaling in rice innate immunity.";
RL Plant J. 80:1072-1084(2014).
CC -!- FUNCTION: Functions in innate immunity. Functions as pattern
CC recognition receptor (PRR), sensing bacterial peptidoglycan (PGN) and
CC fungal chitin at the cell surface. Involved in resistance against the
CC bacterial pathogen Xanthomonas oryzae pv. oryzae (Xoo) and the fungal
CC pathogen Magnaporthe oryzae. Binds PGN and fungal chitin in vitro
CC (PubMed:22872757). Involved in microbe-associated molecular patterns
CC (MAMPs) perception and participates in the activation of defense genes
CC against the bacterial pathogen Xanthomonas oryzae pv. oryzicola (Xoc)
CC or the fungal pathogen Magnaporthe oryzae (PubMed:23299421).
CC {ECO:0000269|PubMed:22872757, ECO:0000269|PubMed:23299421}.
CC -!- SUBUNIT: Interacts with LYP4 (PubMed:23299421). Interacts with CERK1
CC (PubMed:24964058, PubMed:25335639). Interacts with CEBIP
CC (PubMed:24964058). {ECO:0000269|PubMed:23299421,
CC ECO:0000269|PubMed:24964058, ECO:0000269|PubMed:25335639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22872757,
CC ECO:0000269|PubMed:25335639}; Lipid-anchor, GPI-anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:22872757}.
CC -!- INDUCTION: Induced by bacterial peptidoglycan, cell wall muropeptides,
CC chitin, N-acetylchitohexaose, lipopolysaccharide, and flg22 flagellin.
CC Induced by infection with the bacterial pathogen Xanthomonas oryzae pv.
CC oryzae. {ECO:0000269|PubMed:22872757}.
CC -!- MISCELLANEOUS: Plants silencing LYP6 exhibit significant compromised
CC defense responses and enhanced susceptibility toward the bacterial
CC pathogen Xanthomonas oryzae and the fungal pathogen Magnaporthe oryzae.
CC {ECO:0000269|PubMed:22872757}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF19019.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY603381; AAT99435.1; -; mRNA.
DR EMBL; AP004758; BAD35901.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19019.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; BAS96723.1; -; Genomic_DNA.
DR RefSeq; XP_015641500.1; XM_015786014.1.
DR AlphaFoldDB; Q69T51; -.
DR SMR; Q69T51; -.
DR STRING; 4530.OS06T0208800-01; -.
DR PaxDb; Q69T51; -.
DR PRIDE; Q69T51; -.
DR EnsemblPlants; Os06t0208800-01; Os06t0208800-01; Os06g0208800.
DR GeneID; 4340448; -.
DR Gramene; Os06t0208800-01; Os06t0208800-01; Os06g0208800.
DR KEGG; osa:4340448; -.
DR eggNOG; ENOG502QWAT; Eukaryota.
DR InParanoid; Q69T51; -.
DR OrthoDB; 873442at2759; -.
DR PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Immunity;
KW Innate immunity; Lipoprotein; Membrane; Plant defense; Receptor;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..387
FT /note="LysM domain-containing GPI-anchored protein LYP6"
FT /evidence="ECO:0000255"
FT /id="PRO_5010141498"
FT PROPEP 388..409
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440897"
FT DOMAIN 110..160
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 179..222
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 353..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 387
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..100
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 40..166
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 98..164
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 100..166
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 227..259
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT DISULFID 254..282
FT /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT CONFLICT 257
FT /note="C -> S (in Ref. 1; AAT99435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 40504 MW; DC3FEAA244502EF5 CRC64;
MAGWPAAEAA GALVVAILAA AAGGAAGKTT IEPCAGADTC AALLGYTLYA DMKVSEVAAL
FGADPRAVLA ANALDFASPG AANRILPAGL PLRVPTRCAC SDGVRKSVAV RYSARPADTL
ASVADVVFAG LASADQIRTA NGLSAEDPDA PLDAGATLVV PLPCACFNST DNNLPAVYLS
YVVRVGDTVQ SIAATHATTV TDISNVNAMG SPIVAPGDIL AIPLPACASM FPNSASDYGL
LVANGTYALT AGNCVQCSCG PGDLKLYCTP ASLTASCSSM QCPNSNLMLG NVTAQSTSGG
CNVSSCSYAG LVNGTIATSL SSGLQPTCPG PHQFPPLRAT PIAVNQGSYL APSPAPGAGE
AGGDIPGFPG SSNVSPANGP SGSVSQAASV NRPHQIVALI LSVALYFQM
