MYB30_ARATH
ID MYB30_ARATH Reviewed; 323 AA.
AC Q9SCU7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Transcription factor MYB30 {ECO:0000303|PubMed:10929106};
DE AltName: Full=Myb-related protein 30 {ECO:0000303|PubMed:10929106};
DE Short=AtMYB30 {ECO:0000303|PubMed:10929106};
GN Name=MYB30 {ECO:0000303|PubMed:10929106};
GN Synonyms=hsr1 {ECO:0000303|PubMed:10571865};
GN OrderedLocusNames=At3g28910 {ECO:0000312|Araport:AT3G28910};
GN ORFNames=MLD15.8 {ECO:0000312|EMBL:BAB02134.1};
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:CAA07433.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY
RP PATHOGEN.
RX PubMed=10571865; DOI=10.1046/j.1365-313x.1999.00578.x;
RA Daniel X., Lacomme C., Roby D., Morel J.B.;
RT "A novel myb oncogene homologue in Arabidopsis thaliana related to
RT hypersensitive cell death.";
RL Plant J. 20:57-66(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL Plant J. 23:115-122(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], INDUCTION BY JASMONIC ACID AND
RP SALICYLIC ACID, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [7]
RP FUNCTION.
RX PubMed=12119395; DOI=10.1073/pnas.152047199;
RA Vailleau F., Daniel X., Tronchet M., Montillet J.L., Triantaphylides C.,
RA Roby D.;
RT "A R2R3-MYB gene, AtMYB30, acts as a positive regulator of the
RT hypersensitive cell death program in plants in response to pathogen
RT attack.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10179-10184(2002).
RN [8]
RP FUNCTION, AND INDUCTION BY SALICYLIC ACID.
RX PubMed=16730712; DOI=10.1016/j.febslet.2006.05.027;
RA Raffaele S., Rivas S., Roby D.;
RT "An essential role for salicylic acid in AtMYB30-mediated control of the
RT hypersensitive cell death program in Arabidopsis.";
RL FEBS Lett. 580:3498-3504(2006).
RN [9]
RP FUNCTION.
RX PubMed=18326828; DOI=10.1105/tpc.107.054858;
RA Raffaele S., Vailleau F., Leger A., Joubes J., Miersch O., Huard C.,
RA Blee E., Mongrand S., Domergue F., Roby D.;
RT "A MYB transcription factor regulates very-long-chain fatty acid
RT biosynthesis for activation of the hypersensitive cell death response in
RT Arabidopsis.";
RL Plant Cell 20:752-767(2008).
RN [10]
RP FUNCTION, INDUCTION BY BZR2, INTERACTION WITH BZR2, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19170933; DOI=10.1111/j.1365-313x.2008.03778.x;
RA Li L., Yu X., Thompson A., Guo M., Yoshida S., Asami T., Chory J., Yin Y.;
RT "Arabidopsis MYB30 is a direct target of BES1 and cooperates with BES1 to
RT regulate brassinosteroid-induced gene expression.";
RL Plant J. 58:275-286(2009).
RN [11]
RP FUNCTION, INTERACTION WITH PLA2-ALPHA, INDUCTION BY PATHOGEN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20696912; DOI=10.1073/pnas.1009056107;
RA Froidure S., Canonne J., Daniel X., Jauneau A., Briere C., Roby D.,
RA Rivas S.;
RT "AtsPLA2-alpha nuclear relocalization by the Arabidopsis transcription
RT factor AtMYB30 leads to repression of the plant defense response.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15281-15286(2010).
RN [12]
RP RETRACTED PAPER.
RX PubMed=21917550; DOI=10.1105/tpc.111.088815;
RA Canonne J., Marino D., Jauneau A., Pouzet C., Briere C., Roby D., Rivas S.;
RT "The Xanthomonas type III effector XopD targets the Arabidopsis
RT transcription factor MYB30 to suppress plant defense.";
RL Plant Cell 23:3498-3511(2011).
RN [13]
RP RETRACTION NOTICE OF PUBMED:21917550.
RX PubMed=29255113; DOI=10.1105/tpc.17.00567;
RA Canonne J., Marino D., Jauneau A., Pouzet C., Briere C., Roby D., Rivas S.;
RL Plant Cell 30:253-253(2018).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, SUMOYLATION AT LYS-283, AND MUTAGENESIS OF
RP LYS-232; LYS-250 AND LYS-283.
RX PubMed=22814374; DOI=10.1073/pnas.1202630109;
RA Zheng Y., Schumaker K.S., Guo Y.;
RT "Sumoylation of transcription factor MYB30 by the small ubiquitin-like
RT modifier E3 ligase SIZ1 mediates abscisic acid response in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12822-12827(2012).
RN [15]
RP INTERACTION WITH MIEL1, AND UBIQUITINATION.
RX PubMed=23403577; DOI=10.1038/ncomms2479;
RA Marino D., Froidure S., Canonne J., Ben Khaled S., Khafif M., Pouzet C.,
RA Jauneau A., Roby D., Rivas S.;
RT "Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the
RT transcription factor MYB30 weakening plant defence.";
RL Nat. Commun. 4:1476-1476(2013).
RN [16]
RP REVIEW.
RX PubMed=23596456; DOI=10.3389/fpls.2013.00098;
RA Raffaele S., Rivas S.;
RT "Regulate and be regulated: integration of defense and other signals by the
RT AtMYB30 transcription factor.";
RL Front. Plant Sci. 4:98-98(2013).
RN [17]
RP DOMAIN, S-NITROSYLATION AT CYS-49 AND CYS-53, AND MUTAGENESIS OF CYS-49 AND
RP CYS-53.
RX PubMed=24583075; DOI=10.1016/j.bbapap.2014.02.015;
RA Tavares C.P., Vernal J., Delena R.A., Lamattina L., Cassia R., Terenzi H.;
RT "S-nitrosylation influences the structure and DNA binding activity of
RT AtMYB30 transcription factor from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1844:810-817(2014).
RN [18]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24587042; DOI=10.1371/journal.pone.0089799;
RA Liu L., Zhang J., Adrian J., Gissot L., Coupland G., Yu D., Turck F.;
RT "Elevated levels of MYB30 in the phloem accelerate flowering in Arabidopsis
RT through the regulation of FLOWERING LOCUS T.";
RL PLoS ONE 9:E89799-E89799(2014).
CC -!- FUNCTION: Transcription factor that binds specifically to the DNA
CC sequence 5'-AACAAAC-3' (PubMed:19170933). Acts as a positive regulator
CC of hypersensitive cell death (PubMed:10571865, PubMed:12119395). Acts
CC as a positive regulator of salicylic acid synthesis (PubMed:16730712).
CC Regulates very-long-chain fatty acid biosynthesis (PubMed:18326828).
CC Acts cooperatively with BZR2 to promote expression of a subset of
CC brassinosteroids target genes (PubMed:19170933). Transcriptional
CC activity and hypersensitive response control negatively regulated by
CC PLA2-ALPHA (PubMed:20696912). Involved in the regulation of abscisic
CC acid (ABA) signaling (PubMed:22814374). Increased levels of MYB30 can
CC accelerate flowering both in long and short days through the regulation
CC of FT (PubMed:24587042). {ECO:0000269|PubMed:10571865,
CC ECO:0000269|PubMed:12119395, ECO:0000269|PubMed:16730712,
CC ECO:0000269|PubMed:18326828, ECO:0000269|PubMed:19170933,
CC ECO:0000269|PubMed:20696912, ECO:0000269|PubMed:22814374,
CC ECO:0000269|PubMed:24587042}.
CC -!- SUBUNIT: Interacts with MIEL1 (PubMed:23403577). Interacts with BZR2
CC (PubMed:19170933). Interacts with PLA2-ALPHA (PubMed:20696912).
CC {ECO:0000269|PubMed:19170933, ECO:0000269|PubMed:20696912,
CC ECO:0000269|PubMed:23403577}.
CC -!- INTERACTION:
CC Q9SCU7; Q8S8N6: PLA2-ALPHA; NbExp=4; IntAct=EBI-4466599, EBI-15869996;
CC Q9SCU7; Q9M8Y0: SEC; NbExp=3; IntAct=EBI-4466599, EBI-4426966;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20696912}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues of leaves, hypocotyl
CC and roots. {ECO:0000269|PubMed:24587042}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 2-week-old seedlings, in the early
CC stages of development. {ECO:0000269|PubMed:10571865}.
CC -!- INDUCTION: Up-regulated during hypersensitive response, but no
CC expression detected during compatible interaction with pathogens
CC (PubMed:10571865). Specifically induced in the inoculated zone 4 hours
CC post pathogen infection (PubMed:20696912). Up-regulated by jasmonic
CC acid and salicylic acid (PubMed:16463103, PubMed:16730712).
CC Transcriptionally regulated by BZR2 (PubMed:19170933).
CC {ECO:0000269|PubMed:10571865, ECO:0000269|PubMed:16463103,
CC ECO:0000269|PubMed:16730712, ECO:0000269|PubMed:19170933,
CC ECO:0000269|PubMed:20696912}.
CC -!- DOMAIN: The N-terminus (11-116) contains a fully active minimal DNA-
CC binding domain. {ECO:0000269|PubMed:24583075}.
CC -!- PTM: Ubiquitinated by MIEL1. {ECO:0000269|PubMed:23403577}.
CC -!- PTM: Sumoylated at Lys-283 by SIZ1. Stabilizes MYB30 and is required
CC for its function in ABA signaling. {ECO:0000269|PubMed:22814374}.
CC -!- PTM: Simultaneous S-nitrosylation at Cys-49 and CYS-53 negatively
CC regulates DNA-binding activity. {ECO:0000269|PubMed:24583075}.
CC -!- DISRUPTION PHENOTYPE: Altered brassinosteroids response phenotypes
CC (PubMed:19170933). Hypersensitivity to ABA during germination and
CC seedling growth (PubMed:22814374). {ECO:0000269|PubMed:19170933,
CC ECO:0000269|PubMed:22814374}.
CC -!- CAUTION: An article reported regulation of transcriptional activity and
CC hypersensitive response control by Xanthomonas type III effector XopD;
CC however, this paper was later retracted. {ECO:0000305|PubMed:21917550,
CC ECO:0000305|PubMed:29255113}.
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DR EMBL; AJ007289; CAA07433.1; -; mRNA.
DR EMBL; AF250339; AAG10145.1; -; mRNA.
DR EMBL; AP000386; BAB02134.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77505.1; -; Genomic_DNA.
DR EMBL; AY081278; AAL91167.1; -; mRNA.
DR EMBL; AY114560; AAM47879.1; -; mRNA.
DR EMBL; AY519592; AAS10062.1; -; mRNA.
DR PIR; T51621; T51621.
DR RefSeq; NP_189533.1; NM_113812.5.
DR AlphaFoldDB; Q9SCU7; -.
DR SMR; Q9SCU7; -.
DR DIP; DIP-59548N; -.
DR IntAct; Q9SCU7; 6.
DR STRING; 3702.AT3G28910.1; -.
DR PaxDb; Q9SCU7; -.
DR PRIDE; Q9SCU7; -.
DR ProteomicsDB; 251211; -.
DR EnsemblPlants; AT3G28910.1; AT3G28910.1; AT3G28910.
DR GeneID; 822525; -.
DR Gramene; AT3G28910.1; AT3G28910.1; AT3G28910.
DR KEGG; ath:AT3G28910; -.
DR Araport; AT3G28910; -.
DR TAIR; locus:2090764; AT3G28910.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_6_0_1; -.
DR InParanoid; Q9SCU7; -.
DR OMA; EECAGAF; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9SCU7; -.
DR PRO; PR:Q9SCU7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCU7; baseline and differential.
DR Genevisible; Q9SCU7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IMP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:TAIR.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Nucleus; Plant defense; Reference proteome;
KW Repeat; S-nitrosylation; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..323
FT /note="Transcription factor MYB30"
FT /id="PRO_0000434021"
FT DOMAIN 9..61
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 62..116
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 37..61
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 89..112
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 119..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:24583075"
FT MOD_RES 53
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:24583075"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:22814374"
FT MUTAGEN 49
FT /note="C->A: No effect on DNA-binding. Loss of DNA-binding;
FT when associated with A-53."
FT /evidence="ECO:0000269|PubMed:24583075"
FT MUTAGEN 53
FT /note="C->A: No effect on DNA-binding. Loss of DNA-binding;
FT when associated with A-49."
FT /evidence="ECO:0000269|PubMed:24583075"
FT MUTAGEN 232
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:22814374"
FT MUTAGEN 250
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:22814374"
FT MUTAGEN 283
FT /note="K->R: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:22814374"
SQ SEQUENCE 323 AA; 35919 MW; 2114F9760C8D8238 CRC64;
MVRPPCCDKG GVKKGPWTPE EDIILVTYIQ EHGPGNWRAV PTNTGLLRCS KSCRLRWTNY
LRPGIKRGNF TEHEEKMIVH LQALLGNRWA AIASYLPQRT DNDIKNYWNT HLKKKLNKVN
QDSHQELDRS SLSSSPSSSS ANSNSNISRG QWERRLQTDI HLAKKALSEA LSPAVAPIIT
STVTTTSSSA ESRRSTSSAS GFLRTQETST TYASSTENIA KLLKGWVKNS PKTQNSADQI
ASTEVKEVIK SDDGKECAGA FQSFSEFDHS YQQAGVSPDH ETKPDITGCC SNQSQWSLFE
KWLFEDSGGQ IGDILLDENT NFF
