ERG3_ORYSJ
ID ERG3_ORYSJ Reviewed; 144 AA.
AC Q0JBH9; B7E8T2; O82550; Q7F9X0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Elicitor-responsive protein 3;
DE Short=OsERG3 {ECO:0000303|PubMed:23456295};
DE AltName: Full=16 kDa phloem protein;
DE AltName: Full=RPP16;
GN Name=ERG3; OrderedLocusNames=Os04g0531100, LOC_Os04g44870;
GN ORFNames=OsJ_014914, OSJNBa0081C01.13;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare; TISSUE=Phloem;
RX PubMed=12091721; DOI=10.1093/pcp/pcf083;
RA Asano T., Kusano H., Okuda T., Kubo N., Shimada H., Kadowaki K.;
RT "Rpp16 and Rpp17, from a common origin, have different protein
RT characteristics but both genes are predominantly expressed in rice phloem
RT tissues.";
RL Plant Cell Physiol. 43:668-674(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21756975; DOI=10.1016/j.bbagen.2011.06.021;
RA Kang C.H., Moon B.C., Park H.C., Koo S.C., Jeon J.M., Cheong Y.H.,
RA Chung W.S., Lim C.O., Kim J.Y., Yoon B.D., Lee S.Y., Kim C.Y.;
RT "Rice OsERG3 encodes an unusual small C2-domain protein containing a
RT Ca(2+)-binding module but lacking phospholipid-binding properties.";
RL Biochim. Biophys. Acta 1810:1317-1322(2011).
RN [9]
RP PHOSPHORYLATION AT SER-40.
RX PubMed=23456295; DOI=10.1007/s10059-013-2185-0;
RA Kang C.H., Moon B.C., Park H.C., Koo S.C., Chi Y.H., Cheong Y.H.,
RA Yoon B.D., Lee S.Y., Kim C.Y.;
RT "Rice small C2-domain proteins are phosphorylated by calcium-dependent
RT protein kinase.";
RL Mol. Cells 35:381-387(2013).
CC -!- FUNCTION: May play a role in plant defense signaling (Probable). Does
CC not bind to phospholipids in a Ca(2+)-dependent manner in vitro
CC (PubMed:21756975). {ECO:0000269|PubMed:21756975,
CC ECO:0000305|PubMed:21756975}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21756975}.
CC Note=Does not translocate to plasma membrane upon fungal elicitor or
CC calcium treatment. {ECO:0000269|PubMed:21756975}.
CC -!- TISSUE SPECIFICITY: Expressed in phloem. {ECO:0000269|PubMed:12091721}.
CC -!- INDUCTION: By fungal elicitor and calcium.
CC {ECO:0000269|PubMed:21756975}.
CC -!- PTM: Phosphorylated at Ser-40 by CPK18 in a calcium-dependent manner.
CC {ECO:0000305|PubMed:23456295}.
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DR EMBL; AB060729; BAC06444.1; -; Genomic_DNA.
DR EMBL; AL662984; CAE03867.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15308.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90213.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31431.1; -; Genomic_DNA.
DR EMBL; AK063584; BAG88779.1; -; mRNA.
DR RefSeq; XP_015637255.1; XM_015781769.1.
DR AlphaFoldDB; Q0JBH9; -.
DR SMR; Q0JBH9; -.
DR IntAct; Q0JBH9; 13.
DR STRING; 4530.OS04T0531100-01; -.
DR iPTMnet; Q0JBH9; -.
DR PaxDb; Q0JBH9; -.
DR PRIDE; Q0JBH9; -.
DR EnsemblPlants; Os04t0531100-01; Os04t0531100-01; Os04g0531100.
DR GeneID; 4336487; -.
DR Gramene; Os04t0531100-01; Os04t0531100-01; Os04g0531100.
DR KEGG; osa:4336487; -.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_109145_1_1_1; -.
DR InParanoid; Q0JBH9; -.
DR OMA; GWKQSSF; -.
DR OrthoDB; 1430387at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q0JBH9; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Phosphoprotein; Plant defense;
KW Reference proteome.
FT CHAIN 1..144
FT /note="Elicitor-responsive protein 3"
FT /id="PRO_0000087026"
FT DOMAIN 1..103
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 40
FT /note="Phosphoserine; by CPK"
FT /evidence="ECO:0000305|PubMed:23456295"
SQ SEQUENCE 144 AA; 15869 MW; 880B443AB076BA62 CRC64;
MVQGTLEVLL VGAKGLENTD YLCNMDPYAV LKCRSQEQKS SVASGKGSDP EWNETFMFSV
THNATELIIK LMDSDSGTDD DFVGEATISL EAIYTEGSIP PTVYNVVKEE EYRGEIKVGL
TFTPEDDRDR GLSEEDIGGW KQSS
