ERG1_ORYSI
ID ERG1_ORYSI Reviewed; 159 AA.
AC A2WWV5; O50005; O50006; Q7GC09; Q7Y0Z1; Q8LPB3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Elicitor-responsive protein 1;
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; ORFNames=OsI_004298;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ERG1A AND ERG1B),
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Milyang 117;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: May play a role in plant defense signaling. Isoform 2 binds
CC to phospholipids in a Ca(2+)-dependent manner in response to pathogen
CC elicitors.
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}. Note=Partially translocated to
CC plasma membrane upon elicitor treatment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ERG1a; Synonyms=Rpp17-1, FIERG1;
CC IsoId=A2WWV5-1, Q7GC09-1;
CC Sequence=Displayed;
CC Name=ERG1b; Synonyms=Rpp17-2, FIERG2;
CC IsoId=A2WWV5-2, Q7GC09-2;
CC Sequence=VSP_027800;
CC -!- INDUCTION: Isoform 2 is induced by fungal elicitor, Ca(2+) ionophore,
CC mastoparan, and the Ca(2+)-ATPase inhibitor BHQ. Induction by fungal
CC elicitor strongly reduced by treatment with the Ca(2+) channel blocker
CC BAPTA. {ECO:0000269|PubMed:14529272}.
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DR EMBL; U95135; AAC04627.1; -; mRNA.
DR EMBL; U95136; AAC04628.1; -; mRNA.
DR EMBL; AF512505; AAP47157.1; -; Genomic_DNA.
DR EMBL; CM000126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T04314; T04314.
DR PIR; T04363; T04363.
DR AlphaFoldDB; A2WWV5; -.
DR SMR; A2WWV5; -.
DR STRING; 39946.A2WWV5; -.
DR EnsemblPlants; BGIOSGA004776-TA; BGIOSGA004776-PA; BGIOSGA004776. [A2WWV5-1]
DR Gramene; BGIOSGA004776-TA; BGIOSGA004776-PA; BGIOSGA004776. [A2WWV5-1]
DR HOGENOM; CLU_109145_1_0_1; -.
DR OMA; NPCWNEV; -.
DR Proteomes; UP000007015; Chromosome 1.
DR ExpressionAtlas; A2WWV5; differential.
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 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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium/phospholipid-binding; Cell membrane;
KW Cytoplasm; Membrane; Metal-binding; Reference proteome.
FT CHAIN 1..159
FT /note="Elicitor-responsive protein 1"
FT /id="PRO_0000300242"
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 VAR_SEQ 25..27
FT /note="Missing (in isoform ERG1b)"
FT /evidence="ECO:0000303|PubMed:14529272"
FT /id="VSP_027800"
FT CONFLICT 11
FT /note="L -> F (in Ref. 2; AAP47157)"
FT /evidence="ECO:0000305"
FT CONFLICT 28..30
FT /note="KID -> NIH (in Ref. 2; AAC04627)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> Q (in Ref. 2; AAP47157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 17736 MW; EAFD855B5AD62D59 CRC64;
MAGSGVLEVH LVDAKGLTGN DFLGEIGKID PYVVVQYRSQ ERKSSVARDQ GKNPSWNEVF
KFQINSTAAT GQHKLFLRLM DHDTFSRDDF LGEATINVTD LISLGMEHGT WEMSESKHRV
VLADKTYHGE IRVSLTFTAS AKAQDHAEQV GGWAHSFRQ
