EDR4_ARATH
ID EDR4_ARATH Reviewed; 615 AA.
AC Q9FHK4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Protein ENHANCED DISEASE RESISTANCE 4 {ECO:0000303|PubMed:25747881};
GN Name=EDR4 {ECO:0000303|PubMed:25747881};
GN Synonyms=Y-1 {ECO:0000303|PubMed:15618630};
GN OrderedLocusNames=At5g05190 {ECO:0000312|Araport:AT5G05190};
GN ORFNames=K2A11.6 {ECO:0000312|EMBL:BAB09695.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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].
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 INTERACTION WITH RLK902, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15618630; DOI=10.1271/bbb.68.2581;
RA Tarutani Y., Sasaki A., Yasuda M., Nakashita H., Yoshida S., Yamaguchi I.,
RA Suzuki Y.;
RT "Identification of three clones which commonly interact with the kinase
RT domains of highly homologous two receptor-like kinases, RLK902 and RKL1.";
RL Biosci. Biotechnol. Biochem. 68:2581-2587(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY POWDERY
RP MILDEW, AND INTERACTION WITH EDR1 AND CHC2.
RC STRAIN=cv. Columbia;
RX PubMed=25747881; DOI=10.1105/tpc.114.134668;
RA Wu G., Liu S., Zhao Y., Wang W., Kong Z., Tang D.;
RT "ENHANCED DISEASE RESISTANCE4 associates with CLATHRIN HEAVY CHAIN2 and
RT modulates plant immunity by regulating relocation of EDR1 in Arabidopsis.";
RL Plant Cell 27:857-873(2015).
CC -!- FUNCTION: Plays a negative role in salicylic acid (SA)-mediated
CC resistance to powdery mildew (e.g. Golovinomyces cichoracearum). May
CC modulate plant immunity by regulating the relocation of EDR1 by
CC interacting with CHC2 and modulating endocytosis.
CC {ECO:0000269|PubMed:25747881}.
CC -!- SUBUNIT: Interacts with RLK902 (PubMed:15618630). Binds and recruits
CC EDR1 at the powdery mildew (e.g. G.cichoracearum) penetration site on
CC the plasma membrane. Interacts with CHC2 (PubMed:25747881).
CC {ECO:0000269|PubMed:15618630, ECO:0000269|PubMed:25747881}.
CC -!- INTERACTION:
CC Q9FHK4; Q17TI5: BRX; NbExp=3; IntAct=EBI-1544548, EBI-4426649;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25747881}.
CC Endosome {ECO:0000269|PubMed:25747881}. Note=Displays dynamic movement
CC in cells with accumulation at the plasma membrane around pathogenic
CC fungus penetration site. {ECO:0000269|PubMed:25747881}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and rosette leaves, and weakly
CC in inflorescences. Not detected in roots.
CC {ECO:0000269|PubMed:15618630}.
CC -!- INDUCTION: Rapid but transient induction by wounding, salicylic acid
CC treatment or pathogen infection (PubMed:15618630). Accumulates at the
CC penetration site of powdery mildew (e.g. G.cichoracearum) infection
CC (PubMed:25747881). {ECO:0000269|PubMed:15618630,
CC ECO:0000269|PubMed:25747881}.
CC -!- DISRUPTION PHENOTYPE: Mild, hypersensitive response-like lesions under
CC long-day conditions at late growth stages. Enhanced salicylic acid (SA)
CC accumulation and SA signaling-dependent disease resistance to
CC Golovinomyces cichoracearum UCSC1 associated with enhanced H(2)O(2)
CC accumulation and callose deposition in the infection site as well as
CC higher expression of defense-related genes (PRs). Reduced endocytosis
CC rates. {ECO:0000269|PubMed:25747881}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB018111; BAB09695.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90839.1; -; Genomic_DNA.
DR EMBL; AY099876; AAM20727.1; -; mRNA.
DR EMBL; BT008380; AAP37739.1; -; mRNA.
DR RefSeq; NP_196138.1; NM_120601.5.
DR AlphaFoldDB; Q9FHK4; -.
DR BioGRID; 15680; 13.
DR IntAct; Q9FHK4; 18.
DR STRING; 3702.AT5G05190.1; -.
DR iPTMnet; Q9FHK4; -.
DR PaxDb; Q9FHK4; -.
DR PRIDE; Q9FHK4; -.
DR ProteomicsDB; 247074; -.
DR EnsemblPlants; AT5G05190.1; AT5G05190.1; AT5G05190.
DR GeneID; 830401; -.
DR Gramene; AT5G05190.1; AT5G05190.1; AT5G05190.
DR KEGG; ath:AT5G05190; -.
DR Araport; AT5G05190; -.
DR TAIR; locus:2156799; AT5G05190.
DR eggNOG; ENOG502S3VJ; Eukaryota.
DR HOGENOM; CLU_403676_0_0_1; -.
DR InParanoid; Q9FHK4; -.
DR OMA; CCHYHSC; -.
DR OrthoDB; 1206637at2759; -.
DR PhylomeDB; Q9FHK4; -.
DR PRO; PR:Q9FHK4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHK4; baseline and differential.
DR Genevisible; Q9FHK4; AT.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:1900150; P:regulation of defense response to fungus; IEP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR040244; EDR4-like.
DR InterPro; IPR021480; Zinc_ribbon_12.
DR PANTHER; PTHR31105; PTHR31105; 1.
DR Pfam; PF11331; zinc_ribbon_12; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Endocytosis; Endosome; Membrane; Plant defense;
KW Reference proteome.
FT CHAIN 1..615
FT /note="Protein ENHANCED DISEASE RESISTANCE 4"
FT /id="PRO_0000317077"
FT REGION 46..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..129
FT /evidence="ECO:0000255"
FT COMPBIAS 46..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 68351 MW; E798692403CA81C0 CRC64;
MASQTGQKIR LVRCPKCLKI LQEDEDVPVY QCGGCSAILQ AKRRNIAPSS TPSAGETERA
QANEPQSVPE TNNVSSSSGQ DTVLPSSPGR SVDQEYEKGR NASMESTEKE LDDLELSNGD
GTNEIQEQEC SLGDSEKNER EDNSRLESHM MNTVAEAAGS GSSSGSLSVD HVVAARASNP
SGNSEISPDA SPVEEKQSQL DILANKTPSA YDVVAARASN SSGNAEISPD ASPVEEKQSQ
LDYPANKTSS AYDGSESSSD EREGQLLDDD EQWNALQKIR SGKFEMHRYP GYKEQGASSS
SPFSENRRNG ITTYNERHQN RSLQLEGPGG RLGRQGRRHV TEQLRPDMPF YPRESYTRGS
PSHPSHDEFD RYPRAHSLQM PSYAGGMNHD FVDYMYHNNP RARGQGQGSR ISGEMGRNHG
GWYSGQLHNS YSSYSASPQR PMEQPEYHPR WRREIVSDVE DHQRNRHAGH HHELQTRRLR
ERQRVAKRHV RPTAGGAPFV SCYSCSENLQ LPVDFLIFKR KHHLLRCGTC TTVLRFSLQS
RNHLVPAVTH DINANRNSNS TSESPIDKAP SKPEKLRSSV QDEELPVARG SPLHRLMGYS
TVSQVFKVSQ RPPSI
