ASR3_ARATH
ID ASR3_ARATH Reviewed; 314 AA.
AC Q8VZ20; O22805;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Trihelix transcription factor ASR3 {ECO:0000303|PubMed:25770109};
DE AltName: Full=Protein ARABIDOPSIS SH4-RELATED3 {ECO:0000303|PubMed:25770109};
GN Name=ASR3 {ECO:0000303|PubMed:25770109};
GN OrderedLocusNames=At2g33550 {ECO:0000312|Araport:AT2G33550};
GN ORFNames=F4P9.32 {ECO:0000312|EMBL:AAB80672.1};
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|EMBL:AAL38805.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=21738689; DOI=10.1371/journal.pone.0021524;
RA Castrillo G., Turck F., Leveugle M., Lecharny A., Carbonero P.,
RA Coupland G., Paz-Ares J., Onate-Sanchez L.;
RT "Speeding cis-trans regulation discovery by phylogenomic analyses coupled
RT with screenings of an arrayed library of Arabidopsis transcription
RT factors.";
RL PLoS ONE 6:E21524-E21524(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 161-LEU--LEU-165; SER-169;
RP SER-175; SER-182; THR-189; THR-196; SER-230 AND 280-LEU--LEU-284,
RP PHOSPHORYLATION AT THR-189, INTERACTION WITH MPK4, HOMODIMERIZATION,
RP SUBCELLULAR LOCATION, EAR MOTIF, AND DOMAIN.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=25770109; DOI=10.1105/tpc.114.134809;
RA Li B., Jiang S., Yu X., Cheng C., Chen S., Cheng Y., Yuan J.S., Jiang D.,
RA He P., Shan L.;
RT "Phosphorylation of trihelix transcriptional repressor ASR3 by MAP KINASE4
RT negatively regulates Arabidopsis immunity.";
RL Plant Cell 27:839-856(2015).
CC -!- FUNCTION: Transcriptional repressor that binds DNA and plays a negative
CC role in regulating microbe-associated molecular patterns-(MAMPs, e.g.
CC flg22, elf18, chitin, and LPS) triggered immunity (PTI) by negatively
CC regulating immune gene expression. {ECO:0000269|PubMed:25770109}.
CC -!- SUBUNIT: Homodimer. Interacts directly with MPK4.
CC {ECO:0000269|PubMed:25770109}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:25770109}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZ20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZ20-2; Sequence=VSP_057831;
CC -!- DOMAIN: EAR motifs are involved in transcriptional repressor activity.
CC {ECO:0000269|PubMed:25770109}.
CC -!- PTM: Phosphorylated on Thr-189 by MPK4 in response to microbe-
CC associated molecular patterns (MAMPs, e.g. flg22, elf18, chitin, and
CC LPS). This phosphorylation enhances DNA-binding and thus negatively
CC regulates immune gene expression. {ECO:0000269|PubMed:25770109}.
CC -!- DISRUPTION PHENOTYPE: Enhanced disease resistance to virulent bacterial
CC pathogen infection such as P. syringae pv tomato (Pst) DC3000 and P.
CC syringae pv maculicola (Psm) ES4326 associated with immune gene
CC activation. {ECO:0000269|PubMed:25770109}.
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DR EMBL; HQ322383; AEK67478.1; -; mRNA.
DR EMBL; AC002332; AAB80672.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08851.1; -; Genomic_DNA.
DR EMBL; AY065364; AAL38805.1; -; mRNA.
DR EMBL; AY096389; AAM20030.1; -; mRNA.
DR PIR; H84746; H84746.
DR RefSeq; NP_850213.1; NM_179882.2. [Q8VZ20-1]
DR AlphaFoldDB; Q8VZ20; -.
DR IntAct; Q8VZ20; 5.
DR STRING; 3702.AT2G33550.1; -.
DR iPTMnet; Q8VZ20; -.
DR PaxDb; Q8VZ20; -.
DR PRIDE; Q8VZ20; -.
DR ProteomicsDB; 246806; -. [Q8VZ20-1]
DR EnsemblPlants; AT2G33550.1; AT2G33550.1; AT2G33550. [Q8VZ20-1]
DR GeneID; 817920; -.
DR Gramene; AT2G33550.1; AT2G33550.1; AT2G33550. [Q8VZ20-1]
DR KEGG; ath:AT2G33550; -.
DR Araport; AT2G33550; -.
DR TAIR; locus:2051174; AT2G33550.
DR eggNOG; ENOG502QTXI; Eukaryota.
DR HOGENOM; CLU_060472_0_0_1; -.
DR InParanoid; Q8VZ20; -.
DR OMA; YDIMEAV; -.
DR PhylomeDB; Q8VZ20; -.
DR PRO; PR:Q8VZ20; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VZ20; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0050777; P:negative regulation of immune response; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..314
FT /note="Trihelix transcription factor ASR3"
FT /id="PRO_0000433633"
FT DOMAIN 38..104
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..91
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 161..165
FT /note="EAR 1"
FT /evidence="ECO:0000305|PubMed:25770109"
FT MOTIF 280..284
FT /note="EAR 2"
FT /evidence="ECO:0000305|PubMed:25770109"
FT COMPBIAS 229..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphothreonine; by MAPK4"
FT /evidence="ECO:0000269|PubMed:25770109"
FT VAR_SEQ 197..199
FT /note="Missing (in isoform 2)"
FT /id="VSP_057831"
FT MUTAGEN 161..165
FT /note="LSLGL->ASAGA: Impaired transcriptional repressor
FT activity."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 169
FT /note="S->A: Normal flg22-induced phosphorylation by MPK4."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 175
FT /note="S->A: Normal flg22-induced phosphorylation by MPK4."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 182
FT /note="S->A: Normal flg22-induced phosphorylation by MPK4."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 189
FT /note="T->A: Phospho-inactive sequence variation. Blocked
FT flg22-induced phosphorylation by MPK4 but normal
FT transcriptional repressor activity. Enhanced disease
FT resistance."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 189
FT /note="T->D: Phospho-mimetic sequence variation. Normal
FT transcriptional repressor activity but enhanced DNA-binding
FT affinity leading to compromised microbe-associated
FT molecular patterns- (MAMPs) triggered immunity (PTI)
FT responses."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 196
FT /note="T->A: Normal flg22-induced phosphorylation by MPK4."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 230
FT /note="S->A: Normal flg22-induced phosphorylation by MPK4."
FT /evidence="ECO:0000269|PubMed:25770109"
FT MUTAGEN 280..284
FT /note="LNLKL->ANAKA: Impaired transcriptional repressor
FT activity."
FT /evidence="ECO:0000269|PubMed:25770109"
SQ SEQUENCE 314 AA; 34861 MW; 4F08D028F187B413 CRC64;
MALEQLGLGV SAVDGGENSS APSNDGGDDG VKTARLPRWT RQEILVLIQG KRVAENRVRR
GRAAGMALGS GQMEPKWASV SSYCKRHGVN RGPVQCRKRW SNLAGDYKKI KEWESQIKEE
TESYWVMRND VRREKKLPGF FDKEVYDIVD GGVIPPAVPV LSLGLAPASD EGLLSDLDRR
ESPEKLNSTP VAKSVTDVID KEKQEACVAD QGRVKEKQPE AANVEGGSTS QEERKRKRTS
FGEKEEEEEE GETKKMQNQL IEILERNGQL LAAQLEVQNL NLKLDREQRK DHGDSLVAVL
NKLADAVAKI ADKM
