PAD4_ARATH
ID PAD4_ARATH Reviewed; 541 AA.
AC Q9S745; B0ZUC0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Lipase-like PAD4;
DE EC=2.3.1.-;
DE AltName: Full=Protein ENHANCED DISEASE SUSCEPTIBILITY 9;
DE AltName: Full=Protein PHYTOALEXIN DEFICIENT 4;
DE Short=AtPAD4;
GN Name=PAD4; Synonyms=EDS9; OrderedLocusNames=At3g52430; ORFNames=F22O6.190;
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION,
RP AND INDUCTION BY P.SYRINGAE AND SALICYLIC ACID (SA).
RC STRAIN=cv. Columbia;
RX PubMed=10557364; DOI=10.1073/pnas.96.23.13583;
RA Jirage D., Tootle T.L., Reuber T.L., Frost L.N., Feys B.J., Parker J.E.,
RA Ausubel F.M., Glazebrook J.;
RT "Arabidopsis thaliana PAD4 encodes a lipase-like gene that is important for
RT salicylic acid signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13583-13588(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REVIEW ON PLANT DEFENSE.
RC STRAIN=cv. Aa-0, cv. Ak-1, cv. Bay-0, cv. Columbia, cv. Di-0, cv. Gu-0,
RC cv. HOG, cv. Landsberg erecta, cv. Sha, cv. Sorbo, and cv. Tsu-0;
RX PubMed=19064707; DOI=10.1534/genetics.108.097279;
RA Caldwell K.S., Michelmore R.W.;
RT "Arabidopsis thaliana genes encoding defense signaling and recognition
RT proteins exhibit contrasting evolutionary dynamics.";
RL Genetics 181:671-684(2009).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 227-434, AND REVIEW ON PLANT DEFENSE.
RX PubMed=18245336; DOI=10.1534/genetics.107.083279;
RA Bakker E.G., Traw M.B., Toomajian C., Kreitman M., Bergelson J.;
RT "Low levels of polymorphism in genes that control the activation of defense
RT response in Arabidopsis thaliana.";
RL Genetics 178:2031-2043(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8725243; DOI=10.1093/genetics/143.2.973;
RA Glazebrook J., Rogers E.E., Ausubel F.M.;
RT "Isolation of Arabidopsis mutants with enhanced disease susceptibility by
RT direct screening.";
RL Genetics 143:973-982(1996).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9136026; DOI=10.1093/genetics/146.1.381;
RA Glazebrook J., Zook M., Mert F., Kagan I., Rogers E.E., Crute I.R.,
RA Holub E.B., Hammerschmidt R., Ausubel F.M.;
RT "Phytoalexin-deficient mutants of Arabidopsis reveal that PAD4 encodes a
RT regulatory factor and that four PAD genes contribute to downy mildew
RT resistance.";
RL Genetics 146:381-392(1997).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9634589; DOI=10.2307/3870687;
RA Zhou N., Tootle T.L., Tsui F., Klessig D.F., Glazebrook J.;
RT "PAD4 functions upstream from salicylic acid to control defense responses
RT in Arabidopsis.";
RL Plant Cell 10:1021-1030(1998).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9881167; DOI=10.1046/j.1365-313x.1998.00319.x;
RA Reuber T.L., Plotnikova J.M., Dewdney J., Rogers E.E., Wood W.,
RA Ausubel F.M.;
RT "Correlation of defense gene induction defects with powdery mildew
RT susceptibility in Arabidopsis enhanced disease susceptibility mutants.";
RL Plant J. 16:473-485(1998).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10796016; DOI=10.1094/mpmi.2000.13.5.503;
RA Gupta V., Willits M.G., Glazebrook J.;
RT "Arabidopsis thaliana EDS4 contributes to salicylic acid (SA)-dependent
RT expression of defense responses: evidence for inhibition of jasmonic acid
RT signaling by SA.";
RL Mol. Plant Microbe Interact. 13:503-511(2000).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11041879; DOI=10.2307/3871195;
RA Asai T., Stone J.M., Heard J.E., Kovtun Y., Yorgey P., Sheen J.,
RA Ausubel F.M.;
RT "Fumonisin B1-induced cell death in arabidopsis protoplasts requires
RT jasmonate-, ethylene-, and salicylate-dependent signaling pathways.";
RL Plant Cell 12:1823-1836(2000).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH EDS1, AND INDUCTION BY
RP SALICYLIC ACID AND PATHOGENS.
RX PubMed=11574472; DOI=10.1093/emboj/20.19.5400;
RA Feys B.J., Moisan L.J., Newman M.-A., Parker J.E.;
RT "Direct interaction between the Arabidopsis disease resistance signaling
RT proteins, EDS1 and PAD4.";
RL EMBO J. 20:5400-5411(2001).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11595797; DOI=10.2307/3871503;
RA Rusterucci C., Aviv D.H., Holt B.F. III, Dangl J.L., Parker J.E.;
RT "The disease resistance signaling components EDS1 and PAD4 are essential
RT regulators of the cell death pathway controlled by LSD1 in Arabidopsis.";
RL Plant Cell 13:2211-2224(2001).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11826312; DOI=10.1105/tpc.010376;
RA Nawrath C., Heck S., Parinthawong N., Metraux J.-P.;
RT "EDS5, an essential component of salicylic acid-dependent signaling for
RT disease resistance in Arabidopsis, is a member of the MATE transporter
RT family.";
RL Plant Cell 14:275-286(2002).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11846877; DOI=10.1046/j.0960-7412.2001.01229.x;
RA van der Biezen E.A., Freddie C.T., Kahn K., Parker J.E., Jones J.D.;
RT "Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR
RT genes and confers downy mildew resistance through multiple signalling
RT components.";
RL Plant J. 29:439-451(2002).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14617091; DOI=10.1046/j.1365-313x.2003.01881.x;
RA Heck S., Grau T., Buchala A., Metraux J.P., Nawrath C.;
RT "Genetic evidence that expression of NahG modifies defence pathways
RT independent of salicylic acid biosynthesis in the Arabidopsis-Pseudomonas
RT syringae pv. tomato interaction.";
RL Plant J. 36:342-352(2003).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15447647; DOI=10.1111/j.1365-313x.2004.02200.x;
RA Song J.T., Lu H., McDowell J.M., Greenberg J.T.;
RT "A key role for ALD1 in activation of local and systemic defenses in
RT Arabidopsis.";
RL Plant J. 40:200-212(2004).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15347794; DOI=10.1104/pp.104.043646;
RA Mateo A., Muhlenbock P., Rusterucci C., Chang C.C., Miszalski Z.,
RA Karpinska B., Parker J.E., Mullineaux P.M., Karpinski S.;
RT "LESION SIMULATING DISEASE 1 is required for acclimation to conditions that
RT promote excess excitation energy.";
RL Plant Physiol. 136:2818-2830(2004).
RN [19]
RP REVIEW.
RX PubMed=15939664; DOI=10.1016/j.pbi.2005.05.010;
RA Wiermer M., Feys B.J., Parker J.E.;
RT "Plant immunity: the EDS1 regulatory node.";
RL Curr. Opin. Plant Biol. 8:383-389(2005).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16353557; DOI=10.1094/mpmi-18-1226;
RA McDowell J.M., Williams S.G., Funderburg N.T., Eulgem T., Dangl J.L.;
RT "Genetic analysis of developmentally regulated resistance to downy mildew
RT (Hyaloperonospora parasitica) in Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 18:1226-1234(2005).
RN [21]
RP FUNCTION, INTERACTION WITH EDS1, AND SUBCELLULAR LOCATION.
RX PubMed=16040633; DOI=10.1105/tpc.105.033910;
RA Feys B.J., Wiermer M., Bhat R.A., Moisan L.J., Medina-Escobar N., Neu C.,
RA Cabral A., Parker J.E.;
RT "Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals within an
RT ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity.";
RL Plant Cell 17:2601-2613(2005).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15773856; DOI=10.1111/j.1365-313x.2005.02356.x;
RA Xiao S., Calis O., Patrick E., Zhang G., Charoenwattana P., Muskett P.,
RA Parker J.E., Turner J.G.;
RT "The atypical resistance gene, RPW8, recruits components of basal defence
RT for powdery mildew resistance in Arabidopsis.";
RL Plant J. 42:95-110(2005).
RN [23]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY GREEN PEACH APHID.
RX PubMed=16299172; DOI=10.1104/pp.105.070433;
RA Pegadaraju V., Knepper C., Reese J., Shah J.;
RT "Premature leaf senescence modulated by the Arabidopsis PHYTOALEXIN
RT DEFICIENT4 gene is associated with defense against the phloem-feeding green
RT peach aphid.";
RL Plant Physiol. 139:1927-1934(2005).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16813576; DOI=10.1111/j.1365-313x.2006.02806.x;
RA Brodersen P., Petersen M., Bjorn Nielsen H., Zhu S., Newman M.A.,
RA Shokat K.M., Rietz S., Parker J., Mundy J.;
RT "Arabidopsis MAP kinase 4 regulates salicylic acid- and jasmonic
RT acid/ethylene-dependent responses via EDS1 and PAD4.";
RL Plant J. 47:532-546(2006).
RN [25]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18055613; DOI=10.1105/tpc.106.048843;
RA Muehlenbock P., Plaszczyca M., Plaszczyca M., Mellerowicz E., Karpinski S.;
RT "Lysigenous aerenchyma formation in Arabidopsis is controlled by LESION
RT SIMULATING DISEASE1.";
RL Plant Cell 19:3819-3830(2007).
RN [26]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=17725549; DOI=10.1111/j.1365-313x.2007.03241.x;
RA Pegadaraju V., Louis J., Singh V., Reese J.C., Bautor J., Feys B.J.,
RA Cook G., Parker J.E., Shah J.;
RT "Phloem-based resistance to green peach aphid is controlled by Arabidopsis
RT PHYTOALEXIN DEFICIENT4 without its signaling partner ENHANCED DISEASE
RT SUSCEPTIBILITY1.";
RL Plant J. 52:332-341(2007).
RN [27]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17431038; DOI=10.1073/pnas.0609259104;
RA Chandra-Shekara A.C., Venugopal S.C., Barman S.R., Kachroo A., Kachroo P.;
RT "Plastidial fatty acid levels regulate resistance gene-dependent defense
RT signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7277-7282(2007).
RN [28]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18005228; DOI=10.1111/j.1365-313x.2007.03369.x;
RA Tsuda K., Sato M., Glazebrook J., Cohen J.D., Katagiri F.;
RT "Interplay between MAMP-triggered and SA-mediated defense responses.";
RL Plant J. 53:763-775(2008).
RN [29]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18266921; DOI=10.1111/j.1365-313x.2008.03439.x;
RA Lee M.W., Jelenska J., Greenberg J.T.;
RT "Arabidopsis proteins important for modulating defense responses to
RT Pseudomonas syringae that secrete HopW1-1.";
RL Plant J. 54:452-465(2008).
RN [30]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20367470; DOI=10.1094/mpmi-23-5-0618;
RA Louis J., Leung Q., Pegadaraju V., Reese J., Shah J.;
RT "PAD4-dependent antibiosis contributes to the ssi2-conferred hyper-
RT resistance to the green peach aphid.";
RL Mol. Plant Microbe Interact. 23:618-627(2010).
RN [31]
RP FUNCTION, INTERACTION WITH EDS1, INDUCTION BY HYALOPERONOSPORA
RP ARABIDOPSIDIS, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=21434927; DOI=10.1111/j.1469-8137.2011.03675.x;
RA Rietz S., Stamm A., Malonek S., Wagner S., Becker D., Medina-Escobar N.,
RA Vlot A.C., Feys B.J., Niefind K., Parker J.E.;
RT "Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to and
RT dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis immunity.";
RL New Phytol. 191:107-119(2011).
RN [32]
RP INDUCTION BY GREEN PEACH APHID AND TREHALOSE.
RX PubMed=21426427; DOI=10.1111/j.1365-313x.2011.04583.x;
RA Singh V., Louis J., Ayre B.G., Reese J.C., Pegadaraju V., Shah J.;
RT "TREHALOSE PHOSPHATE SYNTHASE11-dependent trehalose metabolism promotes
RT Arabidopsis thaliana defense against the phloem-feeding insect Myzus
RT persicae.";
RL Plant J. 67:94-104(2011).
RN [33]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH EDS1.
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).
RN [34]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VICTR, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=23275581; DOI=10.1105/tpc.112.107235;
RA Kim T.H., Kunz H.H., Bhattacharjee S., Hauser F., Park J., Engineer C.,
RA Liu A., Ha T., Parker J.E., Gassmann W., Schroeder J.I.;
RT "Natural variation in small molecule-induced TIR-NB-LRR signaling induces
RT root growth arrest via EDS1- and PAD4-complexed R protein VICTR in
RT Arabidopsis.";
RL Plant Cell 24:5177-5192(2012).
RN [35]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-118.
RX PubMed=22353573; DOI=10.1104/pp.112.193417;
RA Louis J., Gobbato E., Mondal H.A., Feys B.J., Parker J.E., Shah J.;
RT "Discrimination of Arabidopsis PAD4 activities in defense against green
RT peach aphid and pathogens.";
RL Plant Physiol. 158:1860-1872(2012).
RN [36]
RP INDUCTION BY GREEN PEACH APHID.
RX PubMed=22990443; DOI=10.4161/psb.22088;
RA Louis J., Mondal H.A., Shah J.;
RT "Green peach aphid infestation induces Arabidopsis PHYTOALEXIN-DEFICIENT4
RT expression at site of insect feeding.";
RL Plant Signal. Behav. 7:1431-1433(2012).
RN [37]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23400705; DOI=10.1104/pp.112.208116;
RA Wituszynska W., Slesak I., Vanderauwera S., Szechynska-Hebda M., Kornas A.,
RA Van Der Kelen K., Muhlenbock P., Karpinska B., Mackowski S.,
RA Van Breusegem F., Karpinski S.;
RT "Lesion simulating disease1, enhanced disease susceptibility1, and
RT phytoalexin deficient4 conditionally regulate cellular signaling
RT homeostasis, photosynthesis, water use efficiency, and seed yield in
RT Arabidopsis.";
RL Plant Physiol. 161:1795-1805(2013).
RN [38]
RP INTERACTION WITH EDS1, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF MET-16;
RP LEU-21 AND PHE-143.
RX PubMed=24331460; DOI=10.1016/j.chom.2013.11.006;
RA Wagner S., Stuttmann J., Rietz S., Guerois R., Brunstein E., Bautor J.,
RA Niefind K., Parker J.E.;
RT "Structural basis for signaling by exclusive EDS1 heteromeric complexes
RT with SAG101 or PAD4 in plant innate immunity.";
RL Cell Host Microbe 14:619-630(2013).
CC -!- FUNCTION: Probable lipase required downstream of MPK4 for accumulation
CC of the plant defense-potentiating molecule, salicylic acid, thus
CC contributing to the plant innate immunity against invasive biotrophic
CC pathogens and to defense mechanisms upon recognition of microbe-
CC associated molecular patterns (MAMPs). Participates in the regulation
CC of various molecular and physiological processes that influence
CC fitness. Together with SG101, required for programmed cell death (PCD)
CC triggered by NBS-LRR resistance proteins (e.g. RPS4, RPW8.1 and RPW8.2)
CC in response to the fungal toxin fumonisin B1 (FB1) and avirulent
CC pathogens (e.g. P.syringae pv. tomato strain DC3000 avrRps4 and pv.
CC maculicola, turnip crinkle virus (TCV), and H.arabidopsidis isolates
CC CALA2, EMOY2, EMWA1 and HIND4). Together with EDS1, confers a basal
CC resistance by restricting the growth of virulent pathogens (e.g.
CC H.arabidopsidis isolates NOCO2 and EMCO5, E.orontii isolate MGH, and
CC P.syringae pv. tomato strain DC3000 or expressing HopW1-1 (HopPmaA)).
CC Necessary for the salicylic acid-(SA-) dependent systemic acquired
CC resistance (SAR) response that involves expression of multiple defense
CC responses, including synthesis of the phytoalexin camalexin and
CC expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5)
CC in response to pathogens, triggering a signal amplification loop that
CC increases SA levels via EDS5 and SID2, but, together with EDS1, seems
CC to repress the ethylene/jasmonic acid (ET/JA) defense pathway. May also
CC function in response to abiotic stresses such as UV-C light and LSD1-
CC dependent acclimatization to light conditions that promote excess
CC excitation energy (EEE), probably by transducing redox signals and
CC modulating stomatal conductance. Regulates the formation of lysigenous
CC aerenchyma in hypocotyls in response to hypoxia, maybe via hydrogen
CC peroxide production. Modulates leaf senescence in insect-infested
CC tissue and triggers a phloem-based defense mechanism including
CC antibiosis (e.g. green peach aphid (GPA), M.persicae) to limit phloem
CC sap uptake and insect growth, thus providing an EDS1-independent basal
CC resistance to insects. Also involved in regulation of root meristematic
CC zone-targeted growth arrest together with EDS1 and in a VICTR-dependent
CC manner. {ECO:0000269|PubMed:10557364, ECO:0000269|PubMed:10796016,
CC ECO:0000269|PubMed:11041879, ECO:0000269|PubMed:11574472,
CC ECO:0000269|PubMed:11595797, ECO:0000269|PubMed:11826312,
CC ECO:0000269|PubMed:11846877, ECO:0000269|PubMed:14617091,
CC ECO:0000269|PubMed:15347794, ECO:0000269|PubMed:15447647,
CC ECO:0000269|PubMed:15773856, ECO:0000269|PubMed:16040633,
CC ECO:0000269|PubMed:16299172, ECO:0000269|PubMed:16353557,
CC ECO:0000269|PubMed:16813576, ECO:0000269|PubMed:17431038,
CC ECO:0000269|PubMed:17725549, ECO:0000269|PubMed:18005228,
CC ECO:0000269|PubMed:18055613, ECO:0000269|PubMed:18266921,
CC ECO:0000269|PubMed:20367470, ECO:0000269|PubMed:21434927,
CC ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:22353573,
CC ECO:0000269|PubMed:23275581, ECO:0000269|PubMed:23400705,
CC ECO:0000269|PubMed:8725243, ECO:0000269|PubMed:9136026,
CC ECO:0000269|PubMed:9634589, ECO:0000269|PubMed:9881167}.
CC -!- SUBUNIT: Part of a nuclear complex made of EDS1, SG101 and PAD4 that
CC can be redirected to the cytoplasm in the presence of an extranuclear
CC form of EDS1. Sabilized by direct interaction with EDS1 in infected
CC leaves. Part of a nuclear protein complex made of VICTR, PAD4 and EDS1
CC (PubMed:23275581). Interacts with VICTR (PubMed:23275581). Interacts
CC with EDS1 (PubMed:24331460). {ECO:0000269|PubMed:11574472,
CC ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:21434927,
CC ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:23275581,
CC ECO:0000269|PubMed:24331460}.
CC -!- INTERACTION:
CC Q9S745; Q9SU72: EDS1; NbExp=8; IntAct=EBI-1390441, EBI-1390454;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Can move to the
CC cytoplasm when in complex with EDS1.
CC -!- INDUCTION: By benzothiadiazole (BTH), at site of green peach aphid
CC feeding (GPA, M.persicae) via TPS11-dependent trehalose accumulation,
CC and H.arabidopsidis. Induced by P.syringae in a NPR1-independent
CC manner, and by salicylic acid (SA) in a NPR1-dependent manner.
CC {ECO:0000269|PubMed:10557364, ECO:0000269|PubMed:11574472,
CC ECO:0000269|PubMed:16299172, ECO:0000269|PubMed:21426427,
CC ECO:0000269|PubMed:21434927, ECO:0000269|PubMed:22990443}.
CC -!- DISRUPTION PHENOTYPE: Impaired camalexin accumulation, reduced
CC synthesis of salicylic acid (SA) and ethylene (ET), and altered
CC expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5)
CC upon some pathogenic infections (e.g. P.syringae) and microbe-
CC associated molecular patterns (MAMPs) recognition. Loss of the systemic
CC acquired resistance response. Reduced fitness characterized by lower
CC seed yield and survival rate. Increased sensitivity to P.syringae,
CC H.arabidopsidis, turnip crinkle virus (TCV) and E.orontii. These
CC phenotypes are reversed by SA treatment. Altered sensitivity to
CC jasmonic acid (JA) and ethylene (ET) signaling. Decreased
CC susceptibility to the fungal toxin fumonisin B1 (FB1) that mediates
CC programmed cell death (PCD). Impaired induction of EDS5/SID1 expression
CC after UV-C light exposure and pathogen attack. Altered LSD1-dependent
CC acclimatization to light conditions that promote excess excitation
CC energy (EEE). Impaired formation of lysigenous aerenchyma in response
CC to hypoxia. Reduced resistance against green peach aphid (GPA,
CC M.persicae) due to increased phloem sap uptake, reduced accumulation of
CC antibiotic activity in petiole exudates, and delayed leaf senescence in
CC insect-infested tissue, including chlorophyll loss, cell death, and
CC senescence associated genes (SAG) expression. Loss of [5-(3,4-
CC dichlorophenyl)furan-2-yl]-piperidine-1-ylmethanethione- (DFPM-)
CC induced root growth arrest and inhibition of stomatal closing mediated
CC by abscisic acid (ABA). {ECO:0000269|PubMed:10557364,
CC ECO:0000269|PubMed:10796016, ECO:0000269|PubMed:11041879,
CC ECO:0000269|PubMed:11574472, ECO:0000269|PubMed:11595797,
CC ECO:0000269|PubMed:11826312, ECO:0000269|PubMed:11846877,
CC ECO:0000269|PubMed:14617091, ECO:0000269|PubMed:15347794,
CC ECO:0000269|PubMed:15447647, ECO:0000269|PubMed:15773856,
CC ECO:0000269|PubMed:16299172, ECO:0000269|PubMed:16353557,
CC ECO:0000269|PubMed:16813576, ECO:0000269|PubMed:17431038,
CC ECO:0000269|PubMed:17725549, ECO:0000269|PubMed:18005228,
CC ECO:0000269|PubMed:18055613, ECO:0000269|PubMed:18266921,
CC ECO:0000269|PubMed:20367470, ECO:0000269|PubMed:22353573,
CC ECO:0000269|PubMed:23275581, ECO:0000269|PubMed:23400705,
CC ECO:0000269|PubMed:8725243, ECO:0000269|PubMed:9136026,
CC ECO:0000269|PubMed:9634589, ECO:0000269|PubMed:9881167}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF188329; AAF09479.1; -; mRNA.
DR EMBL; EF470727; ABR46037.1; -; Genomic_DNA.
DR EMBL; EF470728; ABR46038.1; -; Genomic_DNA.
DR EMBL; EF470729; ABR46039.1; -; Genomic_DNA.
DR EMBL; EF470731; ABR46041.1; -; Genomic_DNA.
DR EMBL; EF470733; ABR46043.1; -; Genomic_DNA.
DR EMBL; EF470735; ABR46045.1; -; Genomic_DNA.
DR EMBL; EF470736; ABR46046.1; -; Genomic_DNA.
DR EMBL; EF470737; ABR46047.1; -; Genomic_DNA.
DR EMBL; EF470741; ABR46051.1; -; Genomic_DNA.
DR EMBL; EF470742; ABR46052.1; -; Genomic_DNA.
DR EMBL; EF470743; ABR46053.1; -; Genomic_DNA.
DR EMBL; AL050300; CAB43438.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78945.1; -; Genomic_DNA.
DR EMBL; EU405144; ABZ02805.1; -; Genomic_DNA.
DR EMBL; EU405145; ABZ02806.1; -; Genomic_DNA.
DR EMBL; EU405146; ABZ02807.1; -; Genomic_DNA.
DR EMBL; EU405149; ABZ02810.1; -; Genomic_DNA.
DR EMBL; EU405150; ABZ02811.1; -; Genomic_DNA.
DR EMBL; EU405152; ABZ02813.1; -; Genomic_DNA.
DR EMBL; EU405153; ABZ02814.1; -; Genomic_DNA.
DR EMBL; EU405155; ABZ02816.1; -; Genomic_DNA.
DR EMBL; EU405159; ABZ02820.1; -; Genomic_DNA.
DR EMBL; EU405161; ABZ02822.1; -; Genomic_DNA.
DR EMBL; EU405162; ABZ02823.1; -; Genomic_DNA.
DR EMBL; EU405163; ABZ02824.1; -; Genomic_DNA.
DR EMBL; EU405164; ABZ02825.1; -; Genomic_DNA.
DR EMBL; EU405173; ABZ02834.1; -; Genomic_DNA.
DR EMBL; EU405174; ABZ02835.1; -; Genomic_DNA.
DR EMBL; EU405175; ABZ02836.1; -; Genomic_DNA.
DR EMBL; EU405177; ABZ02838.1; -; Genomic_DNA.
DR EMBL; EU405180; ABZ02841.1; -; Genomic_DNA.
DR EMBL; EU405181; ABZ02842.1; -; Genomic_DNA.
DR EMBL; EU405183; ABZ02844.1; -; Genomic_DNA.
DR EMBL; EU405188; ABZ02849.1; -; Genomic_DNA.
DR EMBL; EU405190; ABZ02851.1; -; Genomic_DNA.
DR EMBL; EU405192; ABZ02853.1; -; Genomic_DNA.
DR EMBL; EU405193; ABZ02854.1; -; Genomic_DNA.
DR EMBL; EU405194; ABZ02855.1; -; Genomic_DNA.
DR EMBL; EU405195; ABZ02856.1; -; Genomic_DNA.
DR EMBL; EU405197; ABZ02858.1; -; Genomic_DNA.
DR EMBL; EU405205; ABZ02866.1; -; Genomic_DNA.
DR EMBL; EU405206; ABZ02867.1; -; Genomic_DNA.
DR EMBL; EU405208; ABZ02869.1; -; Genomic_DNA.
DR EMBL; EU405209; ABZ02870.1; -; Genomic_DNA.
DR EMBL; EU405210; ABZ02871.1; -; Genomic_DNA.
DR EMBL; EU405212; ABZ02873.1; -; Genomic_DNA.
DR EMBL; EU405213; ABZ02874.1; -; Genomic_DNA.
DR EMBL; EU405214; ABZ02875.1; -; Genomic_DNA.
DR EMBL; EU405215; ABZ02876.1; -; Genomic_DNA.
DR EMBL; EU405217; ABZ02878.1; -; Genomic_DNA.
DR EMBL; EU405219; ABZ02880.1; -; Genomic_DNA.
DR EMBL; EU405223; ABZ02884.1; -; Genomic_DNA.
DR EMBL; EU405224; ABZ02885.1; -; Genomic_DNA.
DR EMBL; EU405228; ABZ02889.1; -; Genomic_DNA.
DR EMBL; EU405231; ABZ02892.1; -; Genomic_DNA.
DR EMBL; EU405232; ABZ02893.1; -; Genomic_DNA.
DR EMBL; EU405237; ABZ02898.1; -; Genomic_DNA.
DR PIR; T08456; T08456.
DR RefSeq; NP_190811.1; NM_115103.4.
DR AlphaFoldDB; Q9S745; -.
DR SMR; Q9S745; -.
DR BioGRID; 9726; 2.
DR ComplexPortal; CPX-1324; EDS1-PAD4 complex, variant EDS1.
DR ComplexPortal; CPX-1325; EDS1-PAD4-SAG101 complex, variant EDS1.
DR ComplexPortal; CPX-1618; EDS1-PAD4 complex, variant EDS1B.
DR ComplexPortal; CPX-1619; EDS1-PAD4-SAG101 complex, variant EDS1B.
DR IntAct; Q9S745; 1.
DR STRING; 3702.AT3G52430.1; -.
DR ESTHER; arath-PAD4; Plant_lipase_EDS1-like.
DR PaxDb; Q9S745; -.
DR PRIDE; Q9S745; -.
DR ProteomicsDB; 226046; -.
DR EnsemblPlants; AT3G52430.1; AT3G52430.1; AT3G52430.
DR GeneID; 824408; -.
DR Gramene; AT3G52430.1; AT3G52430.1; AT3G52430.
DR KEGG; ath:AT3G52430; -.
DR Araport; AT3G52430; -.
DR TAIR; locus:2079939; AT3G52430.
DR eggNOG; ENOG502SBGF; Eukaryota.
DR HOGENOM; CLU_016367_2_0_1; -.
DR InParanoid; Q9S745; -.
DR OMA; KIFDKWW; -.
DR OrthoDB; 508556at2759; -.
DR PhylomeDB; Q9S745; -.
DR PRO; PR:Q9S745; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S745; baseline and differential.
DR Genevisible; Q9S745; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0106093; C:EDS1 disease-resistance complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016298; F:lipase activity; ISS:TAIR.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0010618; P:aerenchyma formation; IMP:TAIR.
DR GO; GO:0071327; P:cellular response to trehalose stimulus; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0002213; P:defense response to insect; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IGI:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:ComplexPortal.
DR GO; GO:1901183; P:positive regulation of camalexin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1900367; P:positive regulation of defense response to insect; IMP:UniProtKB.
DR GO; GO:0080151; P:positive regulation of salicylic acid mediated signaling pathway; IGI:UniProtKB.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:TAIR.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IGI:UniProtKB.
DR GO; GO:0080142; P:regulation of salicylic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IDA:UniProtKB.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IDA:UniProtKB.
DR GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR041266; EDS1_EP.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF18117; EDS1_EP; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Ethylene signaling pathway; Hydrolase; Hypersensitive response;
KW Jasmonic acid signaling pathway; Lipid degradation; Lipid metabolism;
KW Nucleus; Plant defense; Reference proteome; Transferase.
FT CHAIN 1..541
FT /note="Lipase-like PAD4"
FT /id="PRO_0000429488"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P19515"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P19515"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P19515"
FT MUTAGEN 16
FT /note="M->A: Loss of interaction with EDS1; when associated
FT with S-21. Loss of interaction with EDS1; when associated
FT with S-21 and A-143."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 21
FT /note="L->S: Loss of interaction with EDS1; when associated
FT with A-16. Loss of interaction with EDS1; when associated
FT with A-16 and A-143."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 118
FT /note="S->A: Loss of antibiosis and deterrence against
FT green peach aphid (GPA, M.persicae) feeding, but normal
FT leaf senescence and plant defense against pathogens."
FT /evidence="ECO:0000269|PubMed:22353573"
FT MUTAGEN 143
FT /note="F->A: Loss of interaction with EDS1; when associated
FT with A-16 and S-21."
FT /evidence="ECO:0000269|PubMed:24331460"
SQ SEQUENCE 541 AA; 60985 MW; D6D5D3EBB522C11A CRC64;
MDDCRFETSE LQASVMISTP LFTDSWSSCN TANCNGSIKI HDIAGITYVA IPAVSMIQLG
NLVGLPVTGD VLFPGLSSDE PLPMVDAAIL KLFLQLKIKE GLELELLGKK LVVITGHSTG
GALAAFTALW LLSQSSPPSF RVFCITFGSP LLGNQSLSTS ISRSRLAHNF CHVVSIHDLV
PRSSNEQFWP FGTYLFCSDK GGVCLDNAGS VRLMFNILNT TATQNTEEHQ RYGHYVFTLS
HMFLKSRSFL GGSIPDNSYQ AGVALAVEAL GFSNDDTSGV LVKECIETAT RIVRAPILRS
AELANELASV LPARLEIQWY KDRCDASEEQ LGYYDFFKRY SLKRDFKVNM SRIRLAKFWD
TVIKMVETNE LPFDFHLGKK WIYASQFYQL LAEPLDIANF YKNRDIKTGG HYLEGNRPKR
YEVIDKWQKG VKVPEECVRS RYASTTQDTC FWAKLEQAKE WLDEARKESS DPQRRSLLRE
KIVPFESYAN TLVTKKEVSL DVKAKNSSYS VWEANLKEFK CKMGYENEIE MVVDESDAME
T
