CEBIP_ORYSJ
ID CEBIP_ORYSJ Reviewed; 356 AA.
AC Q8H8C7; B7ELL0; Q1ESX3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chitin elicitor-binding protein {ECO:0000303|PubMed:16829581};
DE Short=CEBiP {ECO:0000303|PubMed:16829581};
DE Short=OsCEBiP {ECO:0000303|PubMed:27238968};
DE AltName: Full=Lysin motif-containing protein 1;
DE Short=Os-LYP1;
DE Flags: Precursor;
GN Name=CEBIP {ECO:0000303|PubMed:16829581};
GN OrderedLocusNames=Os03g0133400 {ECO:0000312|EMBL:BAS82158.1},
GN LOC_Os03g04110 {ECO:0000312|EMBL:ABF93833.1};
GN ORFNames=OJ1006F06.19 {ECO:0000312|EMBL:AAN05509.1},
GN OsJ_30068 {ECO:0000312|EMBL:EAZ45419.1};
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], PROTEIN SEQUENCE OF 29-60; 171-177; 182-187 AND
RP 205-210, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH CHITIN
RP OLIGOSACCHARIDE ELICITOR, AND GLYCOSYLATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=16829581; DOI=10.1073/pnas.0508882103;
RA Kaku H., Nishizawa Y., Ishii-Minami N., Akimoto-Tomiyama C., Dohmae N.,
RA Takio K., Minami E., Shibuya N.;
RT "Plant cells recognize chitin fragments for defense signaling through a
RT plasma membrane receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11086-11091(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH CHITIN AND CERK1, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=21070404; DOI=10.1111/j.1365-313x.2010.04324.x;
RA Shimizu T., Nakano T., Takamizawa D., Desaki Y., Ishii-Minami N.,
RA Nishizawa Y., Minami E., Okada K., Yamane H., Kaku H., Shibuya N.;
RT "Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate
RT chitin elicitor signaling in rice.";
RL Plant J. 64:204-214(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH CHITIN.
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).
RN [10]
RP INTERACTION WITH LYP4 AND LYP6.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 29-325 IN COMPLEX WITH CHITIN,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-63; ASN-89; ASN-184 AND ASN-306.
RX PubMed=27238968; DOI=10.1016/j.str.2016.04.014;
RA Liu S., Wang J., Han Z., Gong X., Zhang H., Chai J.;
RT "Molecular mechanism for fungal cell wall recognition by rice chitin
RT receptor OsCEBiP.";
RL Structure 24:1192-1200(2016).
CC -!- FUNCTION: Chitin elicitor-binding protein involved in the perception
CC and transduction of chitin oligosaccharide elicitor signal for defense
CC responses. {ECO:0000269|PubMed:16829581, ECO:0000269|PubMed:21070404,
CC ECO:0000269|PubMed:22891159}.
CC -!- SUBUNIT: Forms homooligomer. Interacts with CERK1. Binds to chitin
CC oligosaccharide elicitor. Interacts with LYP4 and LYP6
CC (PubMed:24964058). {ECO:0000269|PubMed:16829581,
CC ECO:0000269|PubMed:21070404, ECO:0000269|PubMed:22891159,
CC ECO:0000269|PubMed:24964058}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16829581};
CC Single-pass membrane protein {ECO:0000269|PubMed:16829581}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, shoots, stems and
CC flowers. {ECO:0000269|PubMed:21070404}.
CC -!- INDUCTION: By chitin oligosaccharide elicitor.
CC {ECO:0000269|PubMed:16829581}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16829581}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE95828.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB206975; BAE95828.1; ALT_INIT; mRNA.
DR EMBL; AC099399; AAN05509.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF93833.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10789.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82158.1; -; Genomic_DNA.
DR EMBL; CM000146; EAZ45419.1; -; Genomic_DNA.
DR EMBL; AK073032; BAG93257.1; -; mRNA.
DR RefSeq; XP_015630176.1; XM_015774690.1.
DR PDB; 5JCD; X-ray; 2.40 A; A/B/C=29-223.
DR PDB; 5JCE; X-ray; 2.51 A; A/B=29-325.
DR PDBsum; 5JCD; -.
DR PDBsum; 5JCE; -.
DR AlphaFoldDB; Q8H8C7; -.
DR SMR; Q8H8C7; -.
DR STRING; 4530.OS03T0133400-01; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR iPTMnet; Q8H8C7; -.
DR PaxDb; Q8H8C7; -.
DR PRIDE; Q8H8C7; -.
DR EnsemblPlants; Os03t0133400-01; Os03t0133400-01; Os03g0133400.
DR Gramene; Os03t0133400-01; Os03t0133400-01; Os03g0133400.
DR KEGG; osa:4331523; -.
DR eggNOG; ENOG502QQ9K; Eukaryota.
DR HOGENOM; CLU_047073_0_0_1; -.
DR InParanoid; Q8H8C7; -.
DR OMA; IQCALLC; -.
DR OrthoDB; 988909at2759; -.
DR PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q8H8C7; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
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 SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS51782; LYSM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chitin-binding; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Plant defense; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:16829581"
FT CHAIN 29..356
FT /note="Chitin elicitor-binding protein"
FT /id="PRO_0000283613"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 111..158
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 175..219
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT BINDING 50..51
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT BINDING 117..123
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT BINDING 145..152
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT BINDING 182
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT BINDING 186
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT BINDING 211..213
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..100
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD, ECO:0007744|PDB:5JCE"
FT DISULFID 41..164
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD"
FT DISULFID 98..162
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCD, ECO:0007744|PDB:5JCE"
FT DISULFID 100..164
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT DISULFID 224..257
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT DISULFID 252..274
FT /evidence="ECO:0000269|PubMed:27238968,
FT ECO:0007744|PDB:5JCE"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:5JCD"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5JCD"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5JCD"
FT TURN 233..237
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5JCE"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5JCE"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5JCE"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5JCE"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:5JCE"
SQ SEQUENCE 356 AA; 37200 MW; 007D7BED10AB98FE CRC64;
MASLTAALAT PAAAALLLLV LLAAPASAAN FTCAVASGTT CKSAILYTSP NATTYGNLVA
RFNTTTLPDL LGANGLPDGT LSSAPVAANS TVKIPFRCRC NGDVGQSDRL PIYVVQPQDG
LDAIARNVFN AFVTYQEIAA ANNIPDPNKI NVSQTLWIPL PCSCDKEEGS NVMHLAYSVG
KGENTSAIAA KYGVTESTLL TRNKIDDPTK LQMGQILDVP LPVCRSSISD TSADHNLMLL
PDGTYGFTAG NCIRCSCSST TYQLNCTAVQ NKGCPSVPLC NGTLKLGETN GTGCGSTTCA
YSGYSNSSSL IIQTSLATNQ TTACQRGGSG RSQFARSMWS MSVISFHMVL IIICFL
