EDR2_ARATH
ID EDR2_ARATH Reviewed; 718 AA.
AC F4JSE7; B3H6R3; F4JSE6; O49417; Q56W91;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Protein ENHANCED DISEASE RESISTANCE 2;
GN Name=EDR2; OrderedLocusNames=At4g19040; ORFNames=F13C5.210;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-718 (ISOFORMS 1/2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16212604; DOI=10.1111/j.1365-313x.2005.02523.x;
RA Tang D., Ade J., Frye C.A., Innes R.W.;
RT "Regulation of plant defense responses in Arabidopsis by EDR2, a PH and
RT START domain-containing protein.";
RL Plant J. 44:245-257(2005).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND PLECKSTRIN
RP HOMOLOGY DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=17612410; DOI=10.1186/1471-2229-7-35;
RA Vorwerk S., Schiff C., Santamaria M., Koh S., Nishimura M., Vogel J.,
RA Somerville C., Somerville S.;
RT "EDR2 negatively regulates salicylic acid-based defenses and cell death
RT during powdery mildew infections of Arabidopsis thaliana.";
RL BMC Plant Biol. 7:35-35(2007).
CC -!- FUNCTION: Negative regulator of the salicylic acid- (SA-) mediated
CC resistance to pathogens, including the biotrophic powdery mildew
CC pathogens Golovinomyces cichoracearum and Blumeria graminis, and the
CC downy mildew pathogen Hyaloperonospora parasitica, probably by limiting
CC the initiation of cell death and the establishment of the
CC hypersensitive response (HR). Prevents ethylene-induced senescence.
CC Binds to phosphatidylinositol-4-phosphate (PtdIns(4)P) in vitro.
CC {ECO:0000269|PubMed:16212604, ECO:0000269|PubMed:17612410}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17612410}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17612410}. Cell membrane
CC {ECO:0000269|PubMed:17612410}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17612410}. Endosome membrane
CC {ECO:0000269|PubMed:17612410}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17612410}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4JSE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JSE7-2; Sequence=VSP_054322;
CC Name=3;
CC IsoId=F4JSE7-3; Sequence=VSP_054323, VSP_054324;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in all tissues and organs,
CC including leaves, roots, flowers, stems and siliques.
CC {ECO:0000269|PubMed:16212604}.
CC -!- DOMAIN: The pleckstrin homology domain (3-110) binds to
CC phosphatidylinositol-4-phosphate (PtdIns(4)P).
CC -!- DISRUPTION PHENOTYPE: Enhanced disease resistance salicylic acid-(SA-)
CC dependent to the biotrophic powdery mildew pathogen Erysiphe
CC cichoracearum at a late stage of the infection process and
CC characterized by the formation of necrotic lesions. Enhanced ethylene-
CC induced senescence phenotype. In edr2-6, exaggerated chlorosis and
CC necrosis response to attack by pathogens (e.g. Hyaloperonospora
CC parasitica, Golovinomyces cichoracearum and Blumeria graminis), but not
CC in response to abiotic stresses or attack by the bacterial pathogen
CC Pseudomonas syringae, characterized by initiation of cell death at
CC infection site and hyper sensitive response (HR).
CC {ECO:0000269|PubMed:16212604, ECO:0000269|PubMed:17612410}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY090340; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BX827233; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA16761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021711; CAA16761.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161550; CAB78906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84130.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84132.1; -; Genomic_DNA.
DR EMBL; AY090340; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX827233; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK222155; BAD95241.1; -; mRNA.
DR PIR; T05041; T05041.
DR RefSeq; NP_001190769.1; NM_001203840.1. [F4JSE7-3]
DR RefSeq; NP_193639.2; NM_118022.5. [F4JSE7-1]
DR AlphaFoldDB; F4JSE7; -.
DR SMR; F4JSE7; -.
DR STRING; 3702.AT4G19040.2; -.
DR iPTMnet; F4JSE7; -.
DR PaxDb; F4JSE7; -.
DR PRIDE; F4JSE7; -.
DR ProteomicsDB; 247073; -. [F4JSE7-1]
DR EnsemblPlants; AT4G19040.1; AT4G19040.1; AT4G19040. [F4JSE7-1]
DR EnsemblPlants; AT4G19040.3; AT4G19040.3; AT4G19040. [F4JSE7-3]
DR GeneID; 827642; -.
DR Gramene; AT4G19040.1; AT4G19040.1; AT4G19040. [F4JSE7-1]
DR Gramene; AT4G19040.3; AT4G19040.3; AT4G19040. [F4JSE7-3]
DR KEGG; ath:AT4G19040; -.
DR Araport; AT4G19040; -.
DR TAIR; locus:2117134; AT4G19040.
DR eggNOG; ENOG502QS0N; Eukaryota.
DR HOGENOM; CLU_018946_0_0_1; -.
DR OMA; RIPVMAN; -.
DR PRO; PR:F4JSE7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JSE7; baseline and differential.
DR Genevisible; F4JSE7; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1900056; P:negative regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IMP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IMP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR045096; EDR2-like.
DR InterPro; IPR009769; EDR2_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR12136; PTHR12136; 1.
DR Pfam; PF07059; EDR2_C; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50848; START; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Endosome;
KW Ethylene signaling pathway; Hypersensitive response; Membrane;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..718
FT /note="Protein ENHANCED DISEASE RESISTANCE 2"
FT /id="PRO_0000428905"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..110
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 180..392
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 134..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 146
FT /note="Q -> QSAISFR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054322"
FT VAR_SEQ 285..287
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054323"
FT VAR_SEQ 474
FT /note="E -> GVHPIK (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054324"
SQ SEQUENCE 718 AA; 81847 MW; 8C9A7078D0CFCA7A CRC64;
MSKVVYEGWM VRYGRRKIGR SYIHMRYFVL EPRLLAYYKK KPQDYQVPIK TMLIDGNCRV
EDRGLKTHHG HMVYVLSVYN KKEKSHRITM AAFNIQEALM WKEKIESVID QHQESQVPNG
QQYVSFEYKS GMDTGRTASS SDHESQFSAA EDEEDSRRSL MRRTTIGNGP PESVLDWTKE
FDAELANQNS DNQAFSRKHW RLLQCQNGLR IFEELLEVDY LPRSCSRAMK AVGVVEATCE
EIFELLMSMD GTRYEWDCSF QFGSLVEEVD GHTAVLYHRL LLDWFPMIVW PRDLCYVRYW
RRNDDGSYVV LFRSREHENC GPQPGCVRAH LESGGYNISP LKPRNGRPRT QVQHLIQIDL
KGWGAGYLPA FQQHCLLQML NSVAGLREWF SQTDERGVHT RIPVMVNMAS SSLSLTKSGK
SLHKSAFSLD QTNSVNRNSL LMDEDSDDDD EFQIAESEQE PETSKPETDV KRPEEEPAHN
IDLSCFSGNL KRNENENARN CWRISDGNNF KVRGKNFGQE KRKIPAGKHL MDLVAVDWFK
DSKRIDHVAR RKGCAAQVAA EKGLFSMVVN VQVPGSTHYS MVFYFVMKEL VPGSLLQRFV
DGDDEFRNSR LKLIPLVPKG SWIVRQSVGS TPCLLGKAVD CNYIRGPTYL EIDVDIGSST
VANGVLGLVI GVITSLVVEM AFLVQANTAE EQPERLIGAV RVSHIELSSA IVPNLESE
