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Protein

Lipase-like PAD4

Gene

PAD4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable lipase required downstream of MPK4 for accumulation of the plant defense-potentiating molecule, salicylic acid, thus contributing to the plant innate immunity against invasive biotrophic pathogens and to defense mechanisms upon recognition of microbe-associated molecular patterns (MAMPs). Participates in the regulation of various molecular and physiological processes that influence fitness. Together with SG101, required for programmed cell death (PCD) triggered by NBS-LRR resistance proteins (e.g. RPS4, RPW8.1 and RPW8.2) in response to the fungal toxin fumonisin B1 (FB1) and avirulent pathogens (e.g. P.syringae pv. tomato strain DC3000 avrRps4 and pv. maculicola, turnip crinkle virus (TCV), and H.arabidopsidis isolates CALA2, EMOY2, EMWA1 and HIND4). Together with EDS1, confers a basal resistance by restricting the growth of virulent pathogens (e.g. H.arabidopsidis isolates NOCO2 and EMCO5, E.orontii isolate MGH, and P.syringae pv. tomato strain DC3000 or expressing HopW1-1 (HopPmaA)). Necessary for the salicylic acid-(SA-) dependent systemic acquired resistance (SAR) response that involves expression of multiple defense responses, including synthesis of the phytoalexin camalexin and expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5) in response to pathogens, triggering a signal amplification loop that increases SA levels via EDS5 and SID2, but, together with EDS1, seems to repress the ethylene/jasmonic acid (ET/JA) defense pathway. May also function in response to abiotic stresses such as UV-C light and LSD1-dependent acclimatization to light conditions that promote excess excitation energy (EEE), probably by transducing redox signals and modulating stomatal conductance. Regulates the formation of lysigenous aerenchyma in hypocotyls in response to hypoxia, maybe via hydrogen peroxide production. Modulates leaf senescence in insect-infested tissue and triggers a phloem-based defense mechanism including antibiosis (e.g. green peach aphid (GPA), M.persicae) to limit phloem sap uptake and insect growth, thus providing an EDS1-independent basal resistance to insects. Also involved in regulation of root meristematic zone-targeted growth arrest together with EDS1 and in a VICTR-dependent manner.30 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei118NucleophileBy similarity1
Active sitei178Charge relay systemBy similarity1
Active sitei229Charge relay systemBy similarity1

GO - Molecular functioni

  • lipase activity Source: TAIR
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • aerenchyma formation Source: TAIR
  • cellular response to trehalose stimulus Source: UniProtKB
  • defense response to bacterium, incompatible interaction Source: UniProtKB
  • defense response to insect Source: TAIR
  • ethylene-activated signaling pathway Source: UniProtKB-KW
  • leaf senescence Source: TAIR
  • lipid catabolic process Source: UniProtKB-KW
  • negative regulation of defense response Source: TAIR
  • negative regulation of ethylene-activated signaling pathway Source: UniProtKB
  • plant-type hypersensitive response Source: UniProtKB-KW
  • positive regulation of camalexin biosynthetic process Source: UniProtKB
  • positive regulation of cell death Source: UniProtKB
  • positive regulation of defense response to bacterium Source: UniProtKB
  • positive regulation of defense response to insect Source: UniProtKB
  • positive regulation of salicylic acid mediated signaling pathway Source: UniProtKB
  • regulation of hydrogen peroxide metabolic process Source: TAIR
  • regulation of jasmonic acid mediated signaling pathway Source: UniProtKB
  • regulation of salicylic acid biosynthetic process Source: UniProtKB
  • regulation of salicylic acid mediated signaling pathway Source: UniProtKB
  • response to bacterium Source: UniProtKB
  • response to hypoxia Source: TAIR
  • response to insect Source: UniProtKB
  • response to other organism Source: TAIR
  • response to salicylic acid Source: UniProtKB
  • response to UV-C Source: UniProtKB
  • systemic acquired resistance Source: TAIR
  • systemic acquired resistance, salicylic acid mediated signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Ethylene signaling pathway, Hypersensitive response, Jasmonic acid signaling pathway, Lipid degradation, Lipid metabolism, Plant defense

Protein family/group databases

ESTHERiarath-PAD4. Plant_lipase_EDS1-like.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase-like PAD4 (EC:2.3.1.-)
Alternative name(s):
Protein ENHANCED DISEASE SUSCEPTIBILITY 9
Protein PHYTOALEXIN DEFICIENT 4
Short name:
AtPAD4
Gene namesi
Name:PAD4
Synonyms:EDS9
Ordered Locus Names:At3g52430
ORF Names:F22O6.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G52430.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Impaired camalexin accumulation, reduced synthesis of salicylic acid (SA) and ethylene (ET), and altered expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5) upon some pathogenic infections (e.g. P.syringae) and microbe-associated molecular patterns (MAMPs) recognition. Loss of the systemic acquired resistance response. Reduced fitness characterized by lower seed yield and survival rate. Increased sensitivity to P.syringae, H.arabidopsidis, turnip crinkle virus (TCV) and E.orontii. These phenotypes are reversed by SA treatment. Altered sensitivity to jasmonic acid (JA) and ethylene (ET) signaling. Decreased susceptibility to the fungal toxin fumonisin B1 (FB1) that mediates programmed cell death (PCD). Impaired induction of EDS5/SID1 expression after UV-C light exposure and pathogen attack. Altered LSD1-dependent acclimatization to light conditions that promote excess excitation energy (EEE). Impaired formation of lysigenous aerenchyma in response to hypoxia. Reduced resistance against green peach aphid (GPA, M.persicae) due to increased phloem sap uptake, reduced accumulation of antibiotic activity in petiole exudates, and delayed leaf senescence in insect-infested tissue, including chlorophyll loss, cell death, and senescence associated genes (SAG) expression. Loss of [5-(3,4-dichlorophenyl)furan-2-yl]-piperidine-1-ylmethanethione- (DFPM-) induced root growth arrest and inhibition of stomatal closing mediated by abscisic acid (ABA).27 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16M → A: Loss of interaction with EDS1; when associated with S-21. Loss of interaction with EDS1; when associated with S-21 and A-143. 1 Publication1
Mutagenesisi21L → S: Loss of interaction with EDS1; when associated with A-16. Loss of interaction with EDS1; when associated with A-16 and A-143. 1 Publication1
Mutagenesisi118S → A: Loss of antibiosis and deterrence against green peach aphid (GPA, M.persicae) feeding, but normal leaf senescence and plant defense against pathogens. 1 Publication1
Mutagenesisi143F → A: Loss of interaction with EDS1; when associated with A-16 and S-21. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004294881 – 541Lipase-like PAD4Add BLAST541

Proteomic databases

PaxDbiQ9S745.

Expressioni

Inductioni

By benzothiadiazole (BTH), at site of green peach aphid feeding (GPA, M.persicae) via TPS11-dependent trehalose accumulation, and H.arabidopsidis. Induced by P.syringae in a NPR1-independent manner, and by salicylic acid (SA) in a NPR1-dependent manner.6 Publications

Gene expression databases

GenevisibleiQ9S745. AT.

Interactioni

Subunit structurei

Part of a nuclear complex made of EDS1, SG101 and PAD4 that can be redirected to the cytoplasm in the presence of an extranuclear form of EDS1. Sabilized by direct interaction with EDS1 in infected leaves. Part of a nuclear protein complex made of VICTR, PAD4 and EDS1 (PubMed:23275581). Interacts with VICTR (PubMed:23275581). Interacts with EDS1 (PubMed:24331460).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EDS1Q9SU724EBI-1390441,EBI-1390454

Protein-protein interaction databases

BioGridi9726. 2 interactors.
IntActiQ9S745. 1 interactor.
STRINGi3702.AT3G52430.1.

Structurei

3D structure databases

ProteinModelPortaliQ9S745.
SMRiQ9S745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Phylogenomic databases

eggNOGiENOG410IJZD. Eukaryota.
ENOG410Y7YA. LUCA.
InParanoidiQ9S745.
OMAiRTKGHYM.
OrthoDBiEOG093606VH.
PhylomeDBiQ9S745.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
[Graphical view]
PfamiPF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9S745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDCRFETSE LQASVMISTP LFTDSWSSCN TANCNGSIKI HDIAGITYVA
60 70 80 90 100
IPAVSMIQLG NLVGLPVTGD VLFPGLSSDE PLPMVDAAIL KLFLQLKIKE
110 120 130 140 150
GLELELLGKK LVVITGHSTG GALAAFTALW LLSQSSPPSF RVFCITFGSP
160 170 180 190 200
LLGNQSLSTS ISRSRLAHNF CHVVSIHDLV PRSSNEQFWP FGTYLFCSDK
210 220 230 240 250
GGVCLDNAGS VRLMFNILNT TATQNTEEHQ RYGHYVFTLS HMFLKSRSFL
260 270 280 290 300
GGSIPDNSYQ AGVALAVEAL GFSNDDTSGV LVKECIETAT RIVRAPILRS
310 320 330 340 350
AELANELASV LPARLEIQWY KDRCDASEEQ LGYYDFFKRY SLKRDFKVNM
360 370 380 390 400
SRIRLAKFWD TVIKMVETNE LPFDFHLGKK WIYASQFYQL LAEPLDIANF
410 420 430 440 450
YKNRDIKTGG HYLEGNRPKR YEVIDKWQKG VKVPEECVRS RYASTTQDTC
460 470 480 490 500
FWAKLEQAKE WLDEARKESS DPQRRSLLRE KIVPFESYAN TLVTKKEVSL
510 520 530 540
DVKAKNSSYS VWEANLKEFK CKMGYENEIE MVVDESDAME T
Length:541
Mass (Da):60,985
Last modified:May 1, 2000 - v1
Checksum:iD6D5D3EBB522C11A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188329 mRNA. Translation: AAF09479.1.
EF470727 Genomic DNA. Translation: ABR46037.1.
EF470728 Genomic DNA. Translation: ABR46038.1.
EF470729 Genomic DNA. Translation: ABR46039.1.
EF470731 Genomic DNA. Translation: ABR46041.1.
EF470733 Genomic DNA. Translation: ABR46043.1.
EF470735 Genomic DNA. Translation: ABR46045.1.
EF470736 Genomic DNA. Translation: ABR46046.1.
EF470737 Genomic DNA. Translation: ABR46047.1.
EF470741 Genomic DNA. Translation: ABR46051.1.
EF470742 Genomic DNA. Translation: ABR46052.1.
EF470743 Genomic DNA. Translation: ABR46053.1.
AL050300 Genomic DNA. Translation: CAB43438.1.
CP002686 Genomic DNA. Translation: AEE78945.1.
EU405144 Genomic DNA. Translation: ABZ02805.1.
EU405145 Genomic DNA. Translation: ABZ02806.1.
EU405146 Genomic DNA. Translation: ABZ02807.1.
EU405149 Genomic DNA. Translation: ABZ02810.1.
EU405150 Genomic DNA. Translation: ABZ02811.1.
EU405152 Genomic DNA. Translation: ABZ02813.1.
EU405153 Genomic DNA. Translation: ABZ02814.1.
EU405155 Genomic DNA. Translation: ABZ02816.1.
EU405159 Genomic DNA. Translation: ABZ02820.1.
EU405161 Genomic DNA. Translation: ABZ02822.1.
EU405162 Genomic DNA. Translation: ABZ02823.1.
EU405163 Genomic DNA. Translation: ABZ02824.1.
EU405164 Genomic DNA. Translation: ABZ02825.1.
EU405173 Genomic DNA. Translation: ABZ02834.1.
EU405174 Genomic DNA. Translation: ABZ02835.1.
EU405175 Genomic DNA. Translation: ABZ02836.1.
EU405177 Genomic DNA. Translation: ABZ02838.1.
EU405180 Genomic DNA. Translation: ABZ02841.1.
EU405181 Genomic DNA. Translation: ABZ02842.1.
EU405183 Genomic DNA. Translation: ABZ02844.1.
EU405188 Genomic DNA. Translation: ABZ02849.1.
EU405190 Genomic DNA. Translation: ABZ02851.1.
EU405192 Genomic DNA. Translation: ABZ02853.1.
EU405193 Genomic DNA. Translation: ABZ02854.1.
EU405194 Genomic DNA. Translation: ABZ02855.1.
EU405195 Genomic DNA. Translation: ABZ02856.1.
EU405197 Genomic DNA. Translation: ABZ02858.1.
EU405205 Genomic DNA. Translation: ABZ02866.1.
EU405206 Genomic DNA. Translation: ABZ02867.1.
EU405208 Genomic DNA. Translation: ABZ02869.1.
EU405209 Genomic DNA. Translation: ABZ02870.1.
EU405210 Genomic DNA. Translation: ABZ02871.1.
EU405212 Genomic DNA. Translation: ABZ02873.1.
EU405213 Genomic DNA. Translation: ABZ02874.1.
EU405214 Genomic DNA. Translation: ABZ02875.1.
EU405215 Genomic DNA. Translation: ABZ02876.1.
EU405217 Genomic DNA. Translation: ABZ02878.1.
EU405219 Genomic DNA. Translation: ABZ02880.1.
EU405223 Genomic DNA. Translation: ABZ02884.1.
EU405224 Genomic DNA. Translation: ABZ02885.1.
EU405228 Genomic DNA. Translation: ABZ02889.1.
EU405231 Genomic DNA. Translation: ABZ02892.1.
EU405232 Genomic DNA. Translation: ABZ02893.1.
EU405237 Genomic DNA. Translation: ABZ02898.1.
PIRiT08456.
RefSeqiNP_190811.1. NM_115103.4.
UniGeneiAt.22858.
At.69183.
At.69581.

Genome annotation databases

EnsemblPlantsiAT3G52430.1; AT3G52430.1; AT3G52430.
GeneIDi824408.
GrameneiAT3G52430.1; AT3G52430.1; AT3G52430.
KEGGiath:AT3G52430.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188329 mRNA. Translation: AAF09479.1.
EF470727 Genomic DNA. Translation: ABR46037.1.
EF470728 Genomic DNA. Translation: ABR46038.1.
EF470729 Genomic DNA. Translation: ABR46039.1.
EF470731 Genomic DNA. Translation: ABR46041.1.
EF470733 Genomic DNA. Translation: ABR46043.1.
EF470735 Genomic DNA. Translation: ABR46045.1.
EF470736 Genomic DNA. Translation: ABR46046.1.
EF470737 Genomic DNA. Translation: ABR46047.1.
EF470741 Genomic DNA. Translation: ABR46051.1.
EF470742 Genomic DNA. Translation: ABR46052.1.
EF470743 Genomic DNA. Translation: ABR46053.1.
AL050300 Genomic DNA. Translation: CAB43438.1.
CP002686 Genomic DNA. Translation: AEE78945.1.
EU405144 Genomic DNA. Translation: ABZ02805.1.
EU405145 Genomic DNA. Translation: ABZ02806.1.
EU405146 Genomic DNA. Translation: ABZ02807.1.
EU405149 Genomic DNA. Translation: ABZ02810.1.
EU405150 Genomic DNA. Translation: ABZ02811.1.
EU405152 Genomic DNA. Translation: ABZ02813.1.
EU405153 Genomic DNA. Translation: ABZ02814.1.
EU405155 Genomic DNA. Translation: ABZ02816.1.
EU405159 Genomic DNA. Translation: ABZ02820.1.
EU405161 Genomic DNA. Translation: ABZ02822.1.
EU405162 Genomic DNA. Translation: ABZ02823.1.
EU405163 Genomic DNA. Translation: ABZ02824.1.
EU405164 Genomic DNA. Translation: ABZ02825.1.
EU405173 Genomic DNA. Translation: ABZ02834.1.
EU405174 Genomic DNA. Translation: ABZ02835.1.
EU405175 Genomic DNA. Translation: ABZ02836.1.
EU405177 Genomic DNA. Translation: ABZ02838.1.
EU405180 Genomic DNA. Translation: ABZ02841.1.
EU405181 Genomic DNA. Translation: ABZ02842.1.
EU405183 Genomic DNA. Translation: ABZ02844.1.
EU405188 Genomic DNA. Translation: ABZ02849.1.
EU405190 Genomic DNA. Translation: ABZ02851.1.
EU405192 Genomic DNA. Translation: ABZ02853.1.
EU405193 Genomic DNA. Translation: ABZ02854.1.
EU405194 Genomic DNA. Translation: ABZ02855.1.
EU405195 Genomic DNA. Translation: ABZ02856.1.
EU405197 Genomic DNA. Translation: ABZ02858.1.
EU405205 Genomic DNA. Translation: ABZ02866.1.
EU405206 Genomic DNA. Translation: ABZ02867.1.
EU405208 Genomic DNA. Translation: ABZ02869.1.
EU405209 Genomic DNA. Translation: ABZ02870.1.
EU405210 Genomic DNA. Translation: ABZ02871.1.
EU405212 Genomic DNA. Translation: ABZ02873.1.
EU405213 Genomic DNA. Translation: ABZ02874.1.
EU405214 Genomic DNA. Translation: ABZ02875.1.
EU405215 Genomic DNA. Translation: ABZ02876.1.
EU405217 Genomic DNA. Translation: ABZ02878.1.
EU405219 Genomic DNA. Translation: ABZ02880.1.
EU405223 Genomic DNA. Translation: ABZ02884.1.
EU405224 Genomic DNA. Translation: ABZ02885.1.
EU405228 Genomic DNA. Translation: ABZ02889.1.
EU405231 Genomic DNA. Translation: ABZ02892.1.
EU405232 Genomic DNA. Translation: ABZ02893.1.
EU405237 Genomic DNA. Translation: ABZ02898.1.
PIRiT08456.
RefSeqiNP_190811.1. NM_115103.4.
UniGeneiAt.22858.
At.69183.
At.69581.

3D structure databases

ProteinModelPortaliQ9S745.
SMRiQ9S745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9726. 2 interactors.
IntActiQ9S745. 1 interactor.
STRINGi3702.AT3G52430.1.

Protein family/group databases

ESTHERiarath-PAD4. Plant_lipase_EDS1-like.

Proteomic databases

PaxDbiQ9S745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G52430.1; AT3G52430.1; AT3G52430.
GeneIDi824408.
GrameneiAT3G52430.1; AT3G52430.1; AT3G52430.
KEGGiath:AT3G52430.

Organism-specific databases

TAIRiAT3G52430.

Phylogenomic databases

eggNOGiENOG410IJZD. Eukaryota.
ENOG410Y7YA. LUCA.
InParanoidiQ9S745.
OMAiRTKGHYM.
OrthoDBiEOG093606VH.
PhylomeDBiQ9S745.

Miscellaneous databases

PROiQ9S745.

Gene expression databases

GenevisibleiQ9S745. AT.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
[Graphical view]
PfamiPF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAD4_ARATH
AccessioniPrimary (citable) accession number: Q9S745
Secondary accession number(s): B0ZUC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.