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LYP4_ORYSJ
ID   LYP4_ORYSJ              Reviewed;         401 AA.
AC   Q67UE8;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=LysM domain-containing GPI-anchored protein LYP4 {ECO:0000305};
DE   AltName: Full=LysM domain-containing protein 4 {ECO:0000303|PubMed:22872757};
DE            Short=Os-LYP4 {ECO:0000303|PubMed:22872757};
DE   Flags: Precursor;
GN   Name=LYP4 {ECO:0000303|PubMed:22872757};
GN   OrderedLocusNames=Os09g0452200 {ECO:0000312|EMBL:BAF25249.1},
GN   LOC_Os09g27890 {ECO:0000305};
GN   ORFNames=OJ1163_C07.33 {ECO:0000312|EMBL:BAD38221.1},
GN   OsJ_29593 {ECO:0000312|EMBL:EEE69832.1},
GN   P0488D02.10 {ECO:0000312|EMBL:BAD38015.1};
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
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   [7]
RP   FUNCTION, AND INTERACTION WITH LYP6 AND CEBIP.
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   [8]
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   [9]
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 LYP6 (PubMed:23299421). Interacts with CEBIP
CC       (PubMed:23299421, PubMed:24964058). Interacts with CERK1
CC       (PubMed:24964058, PubMed:25335639). {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 infection with the bacterial pathogen Xanthomonas
CC       oryzae pv. oryzae. {ECO:0000269|PubMed:22872757}.
CC   -!- MISCELLANEOUS: Plants silencing LYP4 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}.
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DR   EMBL; AP005393; BAD38015.1; -; Genomic_DNA.
DR   EMBL; AP005559; BAD38221.1; -; Genomic_DNA.
DR   EMBL; AP008215; BAF25249.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT08391.1; -; Genomic_DNA.
DR   EMBL; CM000146; EEE69832.1; -; Genomic_DNA.
DR   EMBL; AK059479; BAG87005.1; -; mRNA.
DR   EMBL; AK106042; BAG97526.1; -; mRNA.
DR   RefSeq; XP_015610852.1; XM_015755366.1.
DR   AlphaFoldDB; Q67UE8; -.
DR   SMR; Q67UE8; -.
DR   STRING; 4530.OS09T0452200-01; -.
DR   PaxDb; Q67UE8; -.
DR   PRIDE; Q67UE8; -.
DR   EnsemblPlants; Os09t0452200-01; Os09t0452200-01; Os09g0452200.
DR   EnsemblPlants; Os09t0452200-02; Os09t0452200-02; Os09g0452200.
DR   GeneID; 4347230; -.
DR   Gramene; Os09t0452200-01; Os09t0452200-01; Os09g0452200.
DR   Gramene; Os09t0452200-02; Os09t0452200-02; Os09g0452200.
DR   KEGG; osa:4347230; -.
DR   eggNOG; ENOG502QWAT; Eukaryota.
DR   HOGENOM; CLU_047073_3_0_1; -.
DR   InParanoid; Q67UE8; -.
DR   OMA; VNDMANA; -.
DR   OrthoDB; 873442at2759; -.
DR   PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
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; 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; Immunity;
KW   Innate immunity; Lipoprotein; Membrane; Plant defense; Receptor;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..373
FT                   /note="LysM domain-containing GPI-anchored protein LYP4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5010141336"
FT   PROPEP          374..401
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440896"
FT   DOMAIN          106..156
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          175..218
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   LIPID           373
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        30..96
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT   DISULFID        36..162
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT   DISULFID        94..160
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT   DISULFID        96..162
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT   DISULFID        223..255
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8C7"
FT   DISULFID        250..279
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8C7"
SQ   SEQUENCE   401 AA;  40680 MW;  5C5B4951625AD2C0 CRC64;
     MPPPLLLLLL LAAAAAAVAP ARSKSTLESC SSSTACPALL SYTLYADLKL AELAALFSAD
     PLAILAANSI DFAVPDPADR ILPAGLPLRV PVPCACSDGI RRVTTVRYVA RPGDTLASVA
     SSVYGGLTTP DWISDSNGIL GAKPDAAVDA GTTLFVPLHC ACFGGVDNGL PAVYLTYVAG
     KGDTVAAVAQ RYRTTATDLM SVNDMATPEL AAGDIIVVPL PACTSSFPAF TADYGLAVAN
     GTYAVTANRC VQCSCGPGNL DLFCVPAPLA DSTCSSMQCA NSSMMLGNFT LLMTSSGCSV
     TSCSYGGFVN GTILTTLTTA LKPQCPGPHQ YPPLIPPPTS SFFETYLGPS PTPMASEGGV
     MAGMAPTSTP AASSGPPPAG RHVVGDVLGA FALCLVGNLL W
 
 
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