ERG1_ORYSJ
ID ERG1_ORYSJ Reviewed; 159 AA.
AC Q0JHU5; B7FA01; B9EUD1; O50005; O50006; Q7GC09; Q7Y0Z1; Q8LPB3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Elicitor-responsive protein 1;
DE Short=OsERG1 {ECO:0000303|PubMed:23456295};
DE AltName: Full=17 kDa phloem protein;
DE AltName: Full=Fungal elicitor immediate early-responsive gene 1 protein;
DE Short=FIERG1;
DE AltName: Full=RPP17;
GN Name=ERG1; OrderedLocusNames=Os01g0841700, LOC_Os01g62430;
GN ORFNames=OsJ_04036 {ECO:0000312|EMBL:EEE55652.1}, P0406G08;
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], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Nipponbare;
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(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] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION, AND INDUCTION BY FUNGAL ELICITOR.
RX PubMed=14529272; DOI=10.1021/bi034576n;
RA Kim C.Y., Koo Y.D., Jin J.B., Moon B.C., Kang C.H., Kim S.T., Park B.O.,
RA Lee S.Y., Kim M.L., Hwang I., Kang K.Y., Bahk J.D., Lee S.Y., Cho M.J.;
RT "Rice C2-domain proteins are induced and translocated to the plasma
RT membrane in response to a fungal elicitor.";
RL Biochemistry 42:11625-11633(2003).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, AND MUTAGENESIS OF SER-44.
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).
CC Isoform 2 binds to phospholipids in a Ca(2+)-dependent manner in
CC response to pathogen elicitors (PubMed:14529272).
CC {ECO:0000269|PubMed:14529272, ECO:0000305|PubMed:14529272}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14529272}. Cell
CC membrane {ECO:0000269|PubMed:14529272, ECO:0000269|PubMed:23456295}.
CC Note=Translocates to plasma membrane upon fungal elicitor or calcium
CC treatment. {ECO:0000269|PubMed:14529272, ECO:0000269|PubMed:23456295}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ERG1a, Rpp17-1, FIERG1;
CC IsoId=Q0JHU5-1, Q7GC09-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=ERG1b, Rpp17-2, FIERG2;
CC IsoId=Q0JHU5-2, Q7GC09-2;
CC Sequence=VSP_015389;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in young vascular tissues
CC and tiller buds. {ECO:0000269|PubMed:12091721}.
CC -!- INDUCTION: By fungal elicitor and calcium.
CC {ECO:0000269|PubMed:14529272}.
CC -!- PTM: Phosphorylated at Ser-44 by CPK18 in a calcium-dependent manner.
CC {ECO:0000269|PubMed:23456295}.
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DR EMBL; AB060730; BAC06445.1; -; Genomic_DNA.
DR EMBL; AB060730; BAC06446.1; -; Genomic_DNA.
DR EMBL; AP003240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008207; BAF06683.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75163.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE55652.1; -; Genomic_DNA.
DR EMBL; AK243099; BAH01449.1; -; mRNA.
DR RefSeq; XP_015616516.1; XM_015761030.1. [Q0JHU5-2]
DR AlphaFoldDB; Q0JHU5; -.
DR SMR; Q0JHU5; -.
DR STRING; 4530.OS01T0841700-01; -.
DR iPTMnet; Q0JHU5; -.
DR PRIDE; Q0JHU5; -.
DR EnsemblPlants; Os01t0841700-01; Os01t0841700-01; Os01g0841700. [Q0JHU5-2]
DR GeneID; 4327497; -.
DR Gramene; Os01t0841700-01; Os01t0841700-01; Os01g0841700. [Q0JHU5-2]
DR KEGG; osa:4327497; -.
DR eggNOG; KOG1030; Eukaryota.
DR InParanoid; Q0JHU5; -.
DR OMA; NPCWNEV; -.
DR OrthoDB; 1430387at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q0JHU5; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
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 Alternative splicing; Calcium; Calcium/phospholipid-binding; Cell membrane;
KW Cytoplasm; Membrane; Metal-binding; Phosphoprotein; Plant defense;
KW Reference proteome.
FT CHAIN 1..159
FT /note="Elicitor-responsive protein 1"
FT /id="PRO_0000087016"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 44
FT /note="Phosphoserine; by CPK"
FT /evidence="ECO:0000269|PubMed:23456295"
FT VAR_SEQ 24..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015389"
FT MUTAGEN 44
FT /note="S->A: Abolishes phosphorylation, binding to
FT phospholipids and localization to plasma membrane."
FT /evidence="ECO:0000269|PubMed:23456295"
FT MUTAGEN 44
FT /note="S->D: Abolishes phosphorylation and binding to
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:23456295"
SQ SEQUENCE 159 AA; 17736 MW; EAFD855B5AD62D59 CRC64;
MAGSGVLEVH LVDAKGLTGN DFLGEIGKID PYVVVQYRSQ ERKSSVARDQ GKNPSWNEVF
KFQINSTAAT GQHKLFLRLM DHDTFSRDDF LGEATINVTD LISLGMEHGT WEMSESKHRV
VLADKTYHGE IRVSLTFTAS AKAQDHAEQV GGWAHSFRQ
