EXA1_ARATH
ID EXA1_ARATH Reviewed; 1714 AA.
AC Q9FMM3;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1 {ECO:0000303|PubMed:27402258};
DE AltName: Full=Plant SMY2-type ILE-GYF domain-containing protein 1 {ECO:0000303|PubMed:29073135};
DE AltName: Full=Protein MUTANT, SNC1-ENHANCING 11 {ECO:0000303|PubMed:28362261};
GN Name=EXA1 {ECO:0000303|PubMed:27402258};
GN Synonyms=MUSE11 {ECO:0000303|PubMed:28362261},
GN PSIG1 {ECO:0000303|PubMed:29073135};
GN OrderedLocusNames=At5g42950 {ECO:0000312|Araport:AT5G42950};
GN ORFNames=MBD2.15 {ECO:0000312|EMBL:BAB09197.1};
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=27402258; DOI=10.1111/tpj.13265;
RA Hashimoto M., Neriya Y., Keima T., Iwabuchi N., Koinuma H.,
RA Hagiwara-Komoda Y., Ishikawa K., Himeno M., Maejima K., Yamaji Y.,
RA Namba S.;
RT "EXA1, a GYF domain protein, is responsible for loss-of-susceptibility to
RT plantago asiatica mosaic virus in Arabidopsis thaliana.";
RL Plant J. 88:120-131(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION WITH RPL18B AND
RP EIF4E1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28362261; DOI=10.7554/elife.23684;
RA Wu Z., Huang S., Zhang X., Wu D., Xia S., Li X.;
RT "Regulation of plant immune receptor accumulation through translational
RT repression by a glycine-tyrosine-phenylalanine (GYF) domain protein.";
RL Elife 6:0-0(2017).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF TYR-575, INTERACTION WITH
RP SMG7, PHOSPHORYLATION AT SER-39, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Col-8, and cv. Columbia;
RX PubMed=29073135; DOI=10.1371/journal.pgen.1007037;
RA Matsui H., Nomura Y., Egusa M., Hamada T., Hyon G.-S., Kaminaka H.,
RA Watanabe Y., Ueda T., Trujillo M., Shirasu K., Nakagami H.;
RT "The GYF domain protein PSIG1 dampens the induction of cell death during
RT plant-pathogen interactions.";
RL PLoS Genet. 13:E1007037-E1007037(2017).
CC -!- FUNCTION: Translational repressor involved in the negative regulation
CC of immune receptor accumulation via the inhibition of nucleotide-
CC binding leucine-rich repeat (NLR) receptor mediated defense
CC (PubMed:28362261). Represses NLR protein accumulation (e.g. SNC1, RPS4,
CC RPM1 and RPS2) (PubMed:28362261). Together with SMG7, helps to restrict
CC effector-triggered immunity (ETI) cell death induction during pathogen
CC infection in a salicylic acid- (SA) and reactive oxygen species- (ROS)
CC independent manner (PubMed:29073135). Required for pathogen-associated
CC molecular pattern (PAMP)-induced suppression of necrotrophic fungal
CC (e.g. F.moniliforme) pathogen-derived mycotoxin-triggered (e.g.
CC fumonisin B1) cell death (PubMed:29073135).
CC {ECO:0000269|PubMed:28362261, ECO:0000269|PubMed:29073135}.
CC -!- FUNCTION: (Microbial infection) Required for early steps of plantago
CC asiatica mosaic virus (PlAMV, genus Potexvirus) infection
CC (PubMed:27402258). Facilitates pathogenic growth of avirulent hemi-
CC biotrophic bacteria P.syringae pv. tomato (Pst) DC3000 (e.g. AvrRps4
CC and AvrRpm1) and of the compatible oomycete H.arabidopsidis Noco2
CC (PubMed:28362261, PubMed:29073135). {ECO:0000269|PubMed:27402258,
CC ECO:0000269|PubMed:28362261, ECO:0000269|PubMed:29073135}.
CC -!- SUBUNIT: Associates with eIF4E initiation factors and the ribosome
CC complex, thus likely contributing to the proper translation of target
CC proteins (PubMed:28362261). Interacts directly with RPL18B and eIF4E1
CC (PubMed:28362261). Binds to SMG7 (PubMed:29073135).
CC {ECO:0000269|PubMed:28362261, ECO:0000269|PubMed:29073135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28362261}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:29073135}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, mostly in flowers, leaves
CC and stems, and, to a lower extent, in roots (at protein level).
CC {ECO:0000269|PubMed:27402258}.
CC -!- PTM: Quickly phosphorylated at Ser-39 after treatment of seedlings with
CC the pathogen-associated molecular pattern (PAMP) flg22.
CC {ECO:0000269|PubMed:29073135}.
CC -!- DISRUPTION PHENOTYPE: Reduced size with a curly leaf phenotype
CC associated with an abnormal constitutive PR1 expression
CC (PubMed:28362261, PubMed:29073135). No spontaneous lesions, but
CC enhanced cell death independent of salicylic acid (SA) biosynthesis or
CC reactive oxygen species (ROS) production during pathogen infection
CC (e.g. P.syringae and F.moniliforme) (PubMed:29073135). Heightened
CC nucleotide-binding leucine-rich repeat protein (NLR, e.g. SNC1, RPS4,
CC RPM1 and RPS2) accumulation and enhanced resistance against virulent
CC pathogens (PubMed:28362261). Enhanced snc1-mediated autoimmunity
CC including stunted growth, increased expression of pathogenesis related
CC (PR, e.g. PR1 and PR2) genes and enhanced disease resistance against
CC the virulent oomycete pathogen H.arabidopsidis Noco2, and reduced hemi-
CC biotrophic bacterial growth of P.syringae pv. tomato (Pst) DC3000
CC expressing avirulent effectors AvrRps4 and AvrRpm1 (PubMed:28362261,
CC PubMed:29073135). Abnormal resistance to plantago asiatica mosaic virus
CC (PlAMV, genus Potexvirus) with the absence of infection foci prior to
CC cell-to-cell movement (PubMed:27402258). Increased oxidative bursts,
CC mitogen-activated protein kinase activation and callose deposition in
CC response to the pathogen-associated molecular pattern (PAMP) flg22
CC (PubMed:29073135). {ECO:0000269|PubMed:27402258,
CC ECO:0000269|PubMed:28362261, ECO:0000269|PubMed:29073135}.
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DR EMBL; LC130495; BAX09292.1; -; mRNA.
DR EMBL; AB008264; BAB09197.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94891.1; -; Genomic_DNA.
DR RefSeq; NP_199109.1; NM_123660.3.
DR AlphaFoldDB; Q9FMM3; -.
DR SMR; Q9FMM3; -.
DR IntAct; Q9FMM3; 5.
DR STRING; 3702.AT5G42950.1; -.
DR iPTMnet; Q9FMM3; -.
DR MetOSite; Q9FMM3; -.
DR PaxDb; Q9FMM3; -.
DR PRIDE; Q9FMM3; -.
DR ProMEX; Q9FMM3; -.
DR ProteomicsDB; 177756; -.
DR EnsemblPlants; AT5G42950.1; AT5G42950.1; AT5G42950.
DR GeneID; 834307; -.
DR Gramene; AT5G42950.1; AT5G42950.1; AT5G42950.
DR KEGG; ath:AT5G42950; -.
DR Araport; AT5G42950; -.
DR TAIR; locus:2160041; AT5G42950.
DR eggNOG; KOG1862; Eukaryota.
DR HOGENOM; CLU_002948_0_0_1; -.
DR InParanoid; Q9FMM3; -.
DR OMA; DGDHYRP; -.
DR OrthoDB; 46953at2759; -.
DR PhylomeDB; Q9FMM3; -.
DR PRO; PR:Q9FMM3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMM3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0030371; F:translation repressor activity; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Necrosis; Phosphoprotein; Plant defense; Reference proteome;
KW Repressor; Translation regulation.
FT CHAIN 1..1714
FT /note="Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1"
FT /id="PRO_0000447893"
FT DOMAIN 546..597
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 1..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29073135"
FT MUTAGEN 575
FT /note="Y->A: Enhanced cell death phenotype triggered by
FT P.syringae pv. tomato (Pst) DC3000. Abolished interaction
FT with SMG7."
FT /evidence="ECO:0000269|PubMed:29073135"
SQ SEQUENCE 1714 AA; 187619 MW; 38E850BC82164840 CRC64;
MANSSAGSAA DHRNKHLSVN PPHQIFKDIQ GSDNAIPLSP QWLLSKPGEN KTGMGTGDPN
QYGNHSDVVR TTGNGEETLD NLKKKDVFRP SLLDAESGRR DRWRDEERDT LSSVRNDRWR
NGDKDSGDNK KVDRWDNVAP KFGEQRRGPN DRWTDSGNKD AAPEQRRESK WNSRWGPDDK
EAEIPRNKWD EPGKDGEIIR EKGPSLPTSD GDHYRPWRPS QGRGRGEALH NQSTPNKQVT
SFSHSRGRGE NTAIFSAGRG RMSPGGSIFT SAPNQSHPPG SASDKGESGP GEPPHLRYSR
MKLLDVYRMA DTECYEKFPD GFIEVPSLTS EEPTDPLALC APSSDEVNVL DAIEKGKIVS
SGAPQTSKDG PTGRNPVEFS QPRRIRPAGS REDMTFGAEE SKDESGETRN YPDDKFRPEA
SHEGYAPFRR GNEAPVRELK EPSMQGNAHV QSASPWRQSS GGERSNRNSH DWNDPSADSR
LKSSDSVWSH PKDSINHLGG NNMMLPQSKG ESRWQISEDP SLRRQPSLVF DREQEVRKLL
PSSPEELSLY YKDPQGLIQG PFSGSDIIGW FEAGYFGIDL LVRLASAPND SPFSLLGDVM
PHLRAKSGPP PGFTGAKQNE FVDAAGTSAF PGVGKVHSGM GETDMLQNDM RYKHVAGTVA
ENRFIESLMS GGLTNSAQGV QGYGVNSSGG LSLPVTDGGA DMYLLAKKLE LERQRSIPSP
YSYWPGRESA NLMPGSENVS ENAQQPTRSP SSDLLSILQG VTDRSSPAVS GPLPAWSQPI
QKESDLHHAK TFQTQIPFGV QQQRLPEQNL PLSGLLGQPM ENNPGGMLSP DMMLAAGLSQ
EHQSLNLLQQ QQLLLQLNAQ TPLSAQHQRL LVEKMLLLKH QHKQEEQQQL LRQQQQLYSQ
VFADQQRSQQ RFGDPSYGQL QASLDALRLQ PSKDMSQVNQ QVQVPVSHEE RGINLADLLP
VTHATNQTVA SFETPSLHLQ NQLFGNVDPR MVLPDQIDDT HKKESKSEYE RTVSADYVNS
LYSEKPVLSP GYHATHNVEE PVSYPNNESS TATMTAPEIV ESKLLEEQSK DMYAGKGEVS
IELSGETPAT EVKNNDVSVA RKTSEKKSRK QRAKQAADLA KSTSRAPLQE TKKPQPGSAD
DSEIKGKTKK SADTLIDNDT HLIKSSTATA SNTSQMSSEV DSVRGEESSL QNTRTQPGRA
WKPAPGFKPK SLLEIQMEEQ RVAQAEALAP KISSTVNSVG SAAPWAGIVT NSDSNILRET
HGESAITQTG VVKPESVPTL KAKKSHLHDL LADDVFAKSS DKEREVMEII SNNDAFMQVT
TTNAESFDDD NFIDARETKK SRKKSARAKT SGAKIAAHVP AVDTSLQTNS VEKGKSSRIL
QQQEKEVLPA IPSGPSLGDF VLWKGESVNN PPPAAAWSSG PKKSTKPSSL RDIVKEQEKM
TTSSHPPPSP VPTTQKAIPP QAHQGGASWS RSASSPSQAV SQSSSQSKSK GDDDLFWGPV
EQSTQDTKQG DFPHLTSQNS WGTKNTPGKV NAGTSLNRQK SVSMGSADRV LSSPVVTQAS
HKGKKEAVTK LTEANGFRDW CKSECLRLLG SEDTSVLEFC LKLSRSEAET LLIENLGSRD
PDHKFIDKFL NYKDLLPSEV VEIAFQSKGS GVGTRNNTGE DYYYNTTAAN DGFSKVGGKK
KAKKGKKVSL SASVLGFNVV SNRIMMGEIQ TIED
