ID   EDSBC_ARATH             Reviewed;         629 AA.
AC   Q9SU71;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Protein EDS1B {ECO:0000305};
DE   AltName: Full=Enhanced disease susceptibility 1 protein B;
GN   Name=EDS1B; Synonyms=EDS1-80 {ECO:0000303|PubMed:22072959}, EDS1L;
GN   OrderedLocusNames=At3g48080 {ECO:0000312|Araport:AT3G48080};
GN   ORFNames=T17F15.50 {ECO:0000312|EMBL:CAB41131.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   IDENTIFICATION.
RX   PubMed=15031411; DOI=10.1105/tpc.020479;
RA   Yang S., Hua J.;
RT   "A haplotype-specific Resistance gene regulated by BONZAI1 mediates
RT   temperature-dependent growth control in Arabidopsis.";
RL   Plant Cell 16:1060-1071(2004).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALICYLIC ACID AND VIRUS
RP   INFECTION, AND INTERACTION WITH PAD4 AND SAG101.
RC   STRAIN=cv. Columbia;
RX   PubMed=22072959; DOI=10.1371/journal.ppat.1002318;
RA   Zhu S., Jeong R.-D., Venugopal S.C., Lapchyk L., Navarre D., Kachroo A.,
RA   Kachroo P.;
RT   "SAG101 forms a ternary complex with EDS1 and PAD4 and is required for
RT   resistance signaling against turnip crinkle virus.";
RL   PLoS Pathog. 7:E1002318-E1002318(2011).
CC   -!- FUNCTION: Acts as a second functional copy of EDS1. Can mediate HRT-
CC       mediated resistance to turnip crinkle virus.
CC       {ECO:0000269|PubMed:22072959, ECO:0000305|PubMed:15031411}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with PAD4 and SAG101
CC       (PubMed:22072959). Part of a nuclear complex made of EDS1, PAD4 and
CC       SAG101, that can be redirected to the cytoplasm in the presence of an
CC       extranuclear form of EDS1 (PubMed:22072959). Does not interact with
CC       itself or with EDS1 (PubMed:22072959). {ECO:0000269|PubMed:22072959}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22072959}. Cytoplasm
CC       {ECO:0000269|PubMed:22072959}. Note=Found in both the nucleus and
CC       diffuse in the cytosol when associated with PAD4 and only in the
CC       nucleus when associated with SAG101. {ECO:0000269|PubMed:22072959}.
CC   -!- INDUCTION: Up-regulated by salicylic acid or upon turnip crinkle virus
CC       infection. {ECO:0000269|PubMed:22072959}.
CC   -!- DISRUPTION PHENOTYPE: No effect on RPS4-mediated resistance against
CC       avrRps4 bacteria, due to the redundancy with EDS1.
CC       {ECO:0000269|PubMed:22072959}.
CC   -!- MISCELLANEOUS: Ecotypes cv. Landsberg erecta and cv. Di-17 express a
CC       probably non-functional truncated protein comprising of only the first
CC       162 amino acids. This protein is not expressed in cv. Wassilewskija.
CC       {ECO:0000269|PubMed:22072959}.
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DR   EMBL; AL049658; CAB41131.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78365.1; -; Genomic_DNA.
DR   EMBL; AF462816; AAL58907.1; -; mRNA.
DR   EMBL; BT000828; AAN33203.1; -; mRNA.
DR   PIR; T06675; T06675.
DR   RefSeq; NP_190391.1; NM_114677.3.
DR   AlphaFoldDB; Q9SU71; -.
DR   SMR; Q9SU71; -.
DR   ComplexPortal; CPX-1617; EDS1-SAG101 complex, variant EDS1B.
DR   ComplexPortal; CPX-1618; EDS1-PAD4 complex, variant EDS1B.
DR   ComplexPortal; CPX-1619; EDS1-PAD4-SAG101 complex, variant EDS1B.
DR   STRING; 3702.AT3G48080.1; -.
DR   ESTHER; arath-T17F15.50; Plant_lipase_EDS1-like.
DR   PaxDb; Q9SU71; -.
DR   PRIDE; Q9SU71; -.
DR   ProteomicsDB; 247068; -.
DR   EnsemblPlants; AT3G48080.1; AT3G48080.1; AT3G48080.
DR   GeneID; 823963; -.
DR   Gramene; AT3G48080.1; AT3G48080.1; AT3G48080.
DR   KEGG; ath:AT3G48080; -.
DR   Araport; AT3G48080; -.
DR   TAIR; locus:2097840; AT3G48080.
DR   eggNOG; ENOG502QR4E; Eukaryota.
DR   HOGENOM; CLU_016367_2_0_1; -.
DR   InParanoid; Q9SU71; -.
DR   OMA; RIFCHAV; -.
DR   OrthoDB; 372547at2759; -.
DR   PhylomeDB; Q9SU71; -.
DR   PRO; PR:Q9SU71; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SU71; baseline and differential.
DR   Genevisible; Q9SU71; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106093; C:EDS1 disease-resistance complex; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0009626; P:plant-type hypersensitive response; IC:ComplexPortal.
DR   GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IC:ComplexPortal.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR044214; EDS1-like.
DR   InterPro; IPR041266; EDS1_EP.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   PANTHER; PTHR47090; PTHR47090; 1.
DR   Pfam; PF18117; EDS1_EP; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Nucleus; Plant defense; Reference proteome.
FT   CHAIN           1..629
FT                   /note="Protein EDS1B"
FT                   /id="PRO_0000431442"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P19515"
FT   ACT_SITE        187
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P19515"
FT   ACT_SITE        317
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P19515"
SQ   SEQUENCE   629 AA;  71631 MW;  99E75961EE50FBCB CRC64;
     MAFEALTGVN GDLVTISWMA SKGANQTEHY LKEEVGGTVF FAFRASFSSE DLFATENTSP
     FGEIKMKRNQ FPCMRSIGND VDTTVNEAFL KSLEVLIGPR TSFHASVQSA VDRKQQVVFT
     GHSFGGATAI LATVWYLETY FIRDAYAAPE PRCVTFGAPL VGDYIFKHAL GRENWSRFFV
     NFVTRFDIVP RIMLARKTTI EQTLSYVLGK LDSTRAPIHE SDQVITEFYT RVMRDTYTVA
     SKAVCQLIGN GEAFLETLSS FYELSPYRPV GTFVFSTQKR LVVVNNSDAI LQMLFYTCQS
     NDEQELSVIP FLSIRDHHGY EELVQSIGIK LLNHLDLHNP LLDGENSIGS ALDDLGMSTR
     ARQCIHAALE AEKQRVENQK KIETKRDQIV ERLTWIVEVY KPKCQAHKNG YYDSFKDSNE
     ENDFKANVKR VELAGIFDEV LGLVKKGQLP DGFEGSRGWI NLATQYRRLI EPLDISNYHG
     QLKNEDTGPY MLHGRPSRYK YAQRGYEHDI LKPTGMIAKD VFWSKVNGLN LGLQQDIQEI
     LKNSGSECGS CFWAEVEELK GKPYEEVQVR FKTLEGLLEG WIKDGEVDEK EIFLEGSTFR
     KWWNTLPDSH KIHAPLYPRE RMMDETRAT