Q9FMM3 · EXA1_ARATH

Function

function

Translational repressor involved in the negative regulation of immune receptor accumulation via the inhibition of nucleotide-binding leucine-rich repeat (NLR) receptor mediated defense (PubMed:28362261).
Represses NLR protein accumulation (e.g. SNC1, RPS4, RPM1 and RPS2) (PubMed:28362261).
Together with SMG7, helps to restrict effector-triggered immunity (ETI) cell death induction during pathogen infection in a salicylic acid- (SA) and reactive oxygen species- (ROS) independent manner (PubMed:29073135).
Required for pathogen-associated molecular pattern (PAMP)-induced suppression of necrotrophic fungal (e.g. F.moniliforme) pathogen-derived mycotoxin-triggered (e.g. fumonisin B1) cell death (PubMed:29073135).
(Microbial infection) Required for early steps of plantago asiatica mosaic virus (PlAMV, genus Potexvirus) infection (PubMed:27402258).
Facilitates pathogenic growth of avirulent hemi-biotrophic bacteria P.syringae pv. tomato (Pst) DC3000 (e.g. AvrRps4 and AvrRpm1) and of the compatible oomycete H.arabidopsidis Noco2 (PubMed:28362261, PubMed:29073135).

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular ComponentP-body
Cellular Componentplastid
Molecular FunctionmRNA binding
Molecular Functiontranslation repressor activity
Biological Processdefense response to bacterium
Biological Processdefense response to fungus
Biological Processdefense response to oomycetes
Biological Processdefense response to virus
Biological Processprogrammed cell death
Biological Processregulation of defense response
Biological Processresponse to molecule of bacterial origin

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1
  • Alternative names
    • Plant SMY2-type ILE-GYF domain-containing protein 1
    • Protein MUTANT, SNC1-ENHANCING 11

Gene names

    • Name
      EXA1
    • Synonyms
      MUSE11
      , PSIG1
    • ORF names
      MBD2.15
    • Ordered locus names
      At5g42950

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Columbia
    • cv. Landsberg erecta
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FMM3

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Reduced size with a curly leaf phenotype associated with an abnormal constitutive PR1 expression (PubMed:28362261, PubMed:29073135).
No spontaneous lesions, but enhanced cell death independent of salicylic acid (SA) biosynthesis or reactive oxygen species (ROS) production during pathogen infection (e.g. P.syringae and F.moniliforme) (PubMed:29073135).
Heightened nucleotide-binding leucine-rich repeat protein (NLR, e.g. SNC1, RPS4, RPM1 and RPS2) accumulation and enhanced resistance against virulent pathogens (PubMed:28362261).
Enhanced snc1-mediated autoimmunity including stunted growth, increased expression of pathogenesis related (PR, e.g. PR1 and PR2) genes and enhanced disease resistance against the virulent oomycete pathogen H.arabidopsidis Noco2, and reduced hemi-biotrophic bacterial growth of P.syringae pv. tomato (Pst) DC3000 expressing avirulent effectors AvrRps4 and AvrRpm1 (PubMed:28362261, PubMed:29073135).
Abnormal resistance to plantago asiatica mosaic virus (PlAMV, genus Potexvirus) with the absence of infection foci prior to cell-to-cell movement (PubMed:27402258).
Increased oxidative bursts, mitogen-activated protein kinase activation and callose deposition in response to the pathogen-associated molecular pattern (PAMP) flg22 (PubMed:29073135).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis575Enhanced cell death phenotype triggered by P.syringae pv. tomato (Pst) DC3000. Abolished interaction with SMG7.

Variants

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The viewer provides 204 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004478931-1714Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1
Modified residue39Phosphoserine

Post-translational modification

Quickly phosphorylated at Ser-39 after treatment of seedlings with the pathogen-associated molecular pattern (PAMP) flg22.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all tissues, mostly in flowers, leaves and stems, and, to a lower extent, in roots (at protein level).

Gene expression databases

Interaction

Subunit

Associates with eIF4E initiation factors and the ribosome complex, thus likely contributing to the proper translation of target proteins (PubMed:28362261).
Interacts directly with RPL18B and eIF4E1 (PubMed:28362261).
Binds to SMG7 (PubMed:29073135).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-296Disordered
Compositional bias54-76Polar residues
Compositional bias77-201Basic and acidic residues
Compositional bias226-250Polar residues
Compositional bias267-282Polar residues
Region358-511Disordered
Compositional bias360-374Polar residues
Compositional bias385-426Basic and acidic residues
Compositional bias445-466Polar residues
Domain546-597GYF
Region728-753Disordered
Compositional bias733-753Polar residues
Region1092-1205Disordered
Compositional bias1098-1116Basic and acidic residues
Compositional bias1136-1157Basic and acidic residues
Compositional bias1158-1198Polar residues
Region1437-1566Disordered
Compositional bias1456-1491Polar residues
Compositional bias1500-1559Polar residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,714
  • Mass (Da)
    187,619
  • Last updated
    2001-03-01 v1
  • Checksum
    38E850BC82164840
MANSSAGSAADHRNKHLSVNPPHQIFKDIQGSDNAIPLSPQWLLSKPGENKTGMGTGDPNQYGNHSDVVRTTGNGEETLDNLKKKDVFRPSLLDAESGRRDRWRDEERDTLSSVRNDRWRNGDKDSGDNKKVDRWDNVAPKFGEQRRGPNDRWTDSGNKDAAPEQRRESKWNSRWGPDDKEAEIPRNKWDEPGKDGEIIREKGPSLPTSDGDHYRPWRPSQGRGRGEALHNQSTPNKQVTSFSHSRGRGENTAIFSAGRGRMSPGGSIFTSAPNQSHPPGSASDKGESGPGEPPHLRYSRMKLLDVYRMADTECYEKFPDGFIEVPSLTSEEPTDPLALCAPSSDEVNVLDAIEKGKIVSSGAPQTSKDGPTGRNPVEFSQPRRIRPAGSREDMTFGAEESKDESGETRNYPDDKFRPEASHEGYAPFRRGNEAPVRELKEPSMQGNAHVQSASPWRQSSGGERSNRNSHDWNDPSADSRLKSSDSVWSHPKDSINHLGGNNMMLPQSKGESRWQISEDPSLRRQPSLVFDREQEVRKLLPSSPEELSLYYKDPQGLIQGPFSGSDIIGWFEAGYFGIDLLVRLASAPNDSPFSLLGDVMPHLRAKSGPPPGFTGAKQNEFVDAAGTSAFPGVGKVHSGMGETDMLQNDMRYKHVAGTVAENRFIESLMSGGLTNSAQGVQGYGVNSSGGLSLPVTDGGADMYLLAKKLELERQRSIPSPYSYWPGRESANLMPGSENVSENAQQPTRSPSSDLLSILQGVTDRSSPAVSGPLPAWSQPIQKESDLHHAKTFQTQIPFGVQQQRLPEQNLPLSGLLGQPMENNPGGMLSPDMMLAAGLSQEHQSLNLLQQQQLLLQLNAQTPLSAQHQRLLVEKMLLLKHQHKQEEQQQLLRQQQQLYSQVFADQQRSQQRFGDPSYGQLQASLDALRLQPSKDMSQVNQQVQVPVSHEERGINLADLLPVTHATNQTVASFETPSLHLQNQLFGNVDPRMVLPDQIDDTHKKESKSEYERTVSADYVNSLYSEKPVLSPGYHATHNVEEPVSYPNNESSTATMTAPEIVESKLLEEQSKDMYAGKGEVSIELSGETPATEVKNNDVSVARKTSEKKSRKQRAKQAADLAKSTSRAPLQETKKPQPGSADDSEIKGKTKKSADTLIDNDTHLIKSSTATASNTSQMSSEVDSVRGEESSLQNTRTQPGRAWKPAPGFKPKSLLEIQMEEQRVAQAEALAPKISSTVNSVGSAAPWAGIVTNSDSNILRETHGESAITQTGVVKPESVPTLKAKKSHLHDLLADDVFAKSSDKEREVMEIISNNDAFMQVTTTNAESFDDDNFIDARETKKSRKKSARAKTSGAKIAAHVPAVDTSLQTNSVEKGKSSRILQQQEKEVLPAIPSGPSLGDFVLWKGESVNNPPPAAAWSSGPKKSTKPSSLRDIVKEQEKMTTSSHPPPSPVPTTQKAIPPQAHQGGASWSRSASSPSQAVSQSSSQSKSKGDDDLFWGPVEQSTQDTKQGDFPHLTSQNSWGTKNTPGKVNAGTSLNRQKSVSMGSADRVLSSPVVTQASHKGKKEAVTKLTEANGFRDWCKSECLRLLGSEDTSVLEFCLKLSRSEAETLLIENLGSRDPDHKFIDKFLNYKDLLPSEVVEIAFQSKGSGVGTRNNTGEDYYYNTTAANDGFSKVGGKKKAKKGKKVSLSASVLGFNVVSNRIMMGEIQTIED

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias54-76Polar residues
Compositional bias77-201Basic and acidic residues
Compositional bias226-250Polar residues
Compositional bias267-282Polar residues
Compositional bias360-374Polar residues
Compositional bias385-426Basic and acidic residues
Compositional bias445-466Polar residues
Compositional bias733-753Polar residues
Compositional bias1098-1116Basic and acidic residues
Compositional bias1136-1157Basic and acidic residues
Compositional bias1158-1198Polar residues
Compositional bias1456-1491Polar residues
Compositional bias1500-1559Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LC130495
EMBL· GenBank· DDBJ
BAX09292.1
EMBL· GenBank· DDBJ
mRNA
AB008264
EMBL· GenBank· DDBJ
BAB09197.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED94891.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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