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Transcription factor MYB30 (Myb-related protein 30) (AtMYB30)

 MYB30_ARATH             Reviewed;         323 AA.
Q9SCU7;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 159.
RecName: Full=Transcription factor MYB30 {ECO:0000303|PubMed:10929106};
AltName: Full=Myb-related protein 30 {ECO:0000303|PubMed:10929106};
Short=AtMYB30 {ECO:0000303|PubMed:10929106};
Name=MYB30 {ECO:0000303|PubMed:10929106};
Synonyms=hsr1 {ECO:0000303|PubMed:10571865};
OrderedLocusNames=At3g28910 {ECO:0000312|Araport:AT3G28910};
ORFNames=MLD15.8 {ECO:0000312|EMBL:BAB02134.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:CAA07433.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND
INDUCTION BY PATHOGEN.
PubMed=10571865; DOI=10.1046/j.1365-313X.1999.00578.x;
Daniel X., Lacomme C., Roby D., Morel J.B.;
"A novel myb oncogene homologue in Arabidopsis thaliana related to
hypersensitive cell death.";
Plant J. 20:57-66(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
"Functional identification of an Arabidopsis Snf4 ortholog by
screening for heterologous multicopy suppressors of snf4 deficiency in
yeast.";
Plant J. 23:115-122(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], INDUCTION BY JASMONIC ACID AND
SALICYLIC ACID, GENE FAMILY, AND NOMENCLATURE.
PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y.,
Wang X., Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W.,
Chen Z., Gu H., Qu L.-J.;
"The MYB transcription factor superfamily of Arabidopsis: expression
analysis and phylogenetic comparison with the rice MYB family.";
Plant Mol. Biol. 60:107-124(2006).
[7]
FUNCTION.
PubMed=12119395; DOI=10.1073/pnas.152047199;
Vailleau F., Daniel X., Tronchet M., Montillet J.L.,
Triantaphylides C., Roby D.;
"A R2R3-MYB gene, AtMYB30, acts as a positive regulator of the
hypersensitive cell death program in plants in response to pathogen
attack.";
Proc. Natl. Acad. Sci. U.S.A. 99:10179-10184(2002).
[8]
FUNCTION, AND INDUCTION BY SALICYLIC ACID.
PubMed=16730712; DOI=10.1016/j.febslet.2006.05.027;
Raffaele S., Rivas S., Roby D.;
"An essential role for salicylic acid in AtMYB30-mediated control of
the hypersensitive cell death program in Arabidopsis.";
FEBS Lett. 580:3498-3504(2006).
[9]
FUNCTION.
PubMed=18326828; DOI=10.1105/tpc.107.054858;
Raffaele S., Vailleau F., Leger A., Joubes J., Miersch O., Huard C.,
Blee E., Mongrand S., Domergue F., Roby D.;
"A MYB transcription factor regulates very-long-chain fatty acid
biosynthesis for activation of the hypersensitive cell death response
in Arabidopsis.";
Plant Cell 20:752-767(2008).
[10]
FUNCTION, INDUCTION BY BZR2, INTERACTION WITH BZR2, AND DISRUPTION
PHENOTYPE.
PubMed=19170933; DOI=10.1111/j.1365-313X.2008.03778.x;
Li L., Yu X., Thompson A., Guo M., Yoshida S., Asami T., Chory J.,
Yin Y.;
"Arabidopsis MYB30 is a direct target of BES1 and cooperates with BES1
to regulate brassinosteroid-induced gene expression.";
Plant J. 58:275-286(2009).
[11]
FUNCTION, INTERACTION WITH PLA2-ALPHA, INDUCTION BY PATHOGEN, AND
SUBCELLULAR LOCATION.
PubMed=20696912; DOI=10.1073/pnas.1009056107;
Froidure S., Canonne J., Daniel X., Jauneau A., Briere C., Roby D.,
Rivas S.;
"AtsPLA2-alpha nuclear relocalization by the Arabidopsis transcription
factor AtMYB30 leads to repression of the plant defense response.";
Proc. Natl. Acad. Sci. U.S.A. 107:15281-15286(2010).
[12]
FUNCTION, INTERACTION WITH XOPD, AND SUBCELLULAR LOCATION.
PubMed=21917550; DOI=10.1105/tpc.111.088815;
Canonne J., Marino D., Jauneau A., Pouzet C., Briere C., Roby D.,
Rivas S.;
"The Xanthomonas type III effector XopD targets the Arabidopsis
transcription factor MYB30 to suppress plant defense.";
Plant Cell 23:3498-3511(2011).
[13]
FUNCTION, DISRUPTION PHENOTYPE, SUMOYLATION AT LYS-283, AND
MUTAGENESIS OF LYS-232; LYS-250 AND LYS-283.
PubMed=22814374; DOI=10.1073/pnas.1202630109;
Zheng Y., Schumaker K.S., Guo Y.;
"Sumoylation of transcription factor MYB30 by the small ubiquitin-like
modifier E3 ligase SIZ1 mediates abscisic acid response in Arabidopsis
thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 109:12822-12827(2012).
[14]
INTERACTION WITH MIEL1, AND UBIQUITINATION.
PubMed=23403577; DOI=10.1038/ncomms2479;
Marino D., Froidure S., Canonne J., Ben Khaled S., Khafif M.,
Pouzet C., Jauneau A., Roby D., Rivas S.;
"Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the
transcription factor MYB30 weakening plant defence.";
Nat. Commun. 4:1476-1476(2013).
[15]
REVIEW.
PubMed=23596456; DOI=10.3389/fpls.2013.00098;
Raffaele S., Rivas S.;
"Regulate and be regulated: integration of defense and other signals
by the AtMYB30 transcription factor.";
Front. Plant Sci. 4:98-98(2013).
[16]
DOMAIN, S-NITROSYLATION AT CYS-49 AND CYS-53, AND MUTAGENESIS OF
CYS-49 AND CYS-53.
PubMed=24583075; DOI=10.1016/j.bbapap.2014.02.015;
Tavares C.P., Vernal J., Delena R.A., Lamattina L., Cassia R.,
Terenzi H.;
"S-nitrosylation influences the structure and DNA binding activity of
AtMYB30 transcription factor from Arabidopsis thaliana.";
Biochim. Biophys. Acta 1844:810-817(2014).
[17]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24587042; DOI=10.1371/journal.pone.0089799;
Liu L., Zhang J., Adrian J., Gissot L., Coupland G., Yu D., Turck F.;
"Elevated levels of MYB30 in the phloem accelerate flowering in
Arabidopsis through the regulation of FLOWERING LOCUS T.";
PLoS ONE 9:E89799-E89799(2014).
-!- FUNCTION: Transcription factor that binds specifically to the DNA
sequence 5'-AACAAAC-3' (PubMed:19170933). Acts as a positive
regulator of hypersensitive cell death (PubMed:10571865,
PubMed:12119395). Acts as a positive regulator of salicylic acid
synthesis (PubMed:16730712). Regulates very-long-chain fatty acid
biosynthesis (PubMed:18326828). Acts cooperatively with BZR2 to
promote expression of a subset of brassinosteroids target genes
(PubMed:19170933). Transcriptional activity and hypersensitive
response control negatively regulated by PLA2-ALPHA and by the
Xanthomonas type III effector XopD (AC G9L9K6) (PubMed:20696912,
PubMed:21917550). Involved in the regulation of abscisic acid
(ABA) signaling (PubMed:22814374). Increased levels of MYB30 can
accelerate flowering both in long and short days through the
regulation of FT (PubMed:24587042). {ECO:0000269|PubMed:10571865,
ECO:0000269|PubMed:12119395, ECO:0000269|PubMed:16730712,
ECO:0000269|PubMed:18326828, ECO:0000269|PubMed:19170933,
ECO:0000269|PubMed:20696912, ECO:0000269|PubMed:21917550,
ECO:0000269|PubMed:22814374, ECO:0000269|PubMed:24587042}.
-!- SUBUNIT: Interacts with MIEL1 (PubMed:23403577). Interacts with
BZR2 (PubMed:19170933). Interacts with PLA2-ALPHA
(PubMed:20696912). Interacts with the Xanthomonas type III
effector XopD (AC G9L9K6) (via HLH domain) (PubMed:21917550).
{ECO:0000269|PubMed:19170933, ECO:0000269|PubMed:20696912,
ECO:0000269|PubMed:21917550, ECO:0000269|PubMed:23403577}.
-!- INTERACTION:
Q8S8N6:PLA2-ALPHA; NbExp=4; IntAct=EBI-4466599, EBI-15869996;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20696912,
ECO:0000269|PubMed:21917550}. Note=Relocalized to nuclear bodies
by XopD. {ECO:0000269|PubMed:21917550}.
-!- TISSUE SPECIFICITY: Expressed in vascular tissues of leaves,
hypocotyl and roots. {ECO:0000269|PubMed:24587042}.
-!- DEVELOPMENTAL STAGE: Expressed in 2-week-old seedlings, in the
early stages of development. {ECO:0000269|PubMed:10571865}.
-!- INDUCTION: Up-regulated during hypersensitive response, but no
expression detected during compatible interaction with pathogens
(PubMed:10571865). Specifically induced in the inoculated zone 4
hours post pathogen infection (PubMed:20696912). Up-regulated by
jasmonic acid and salicylic acid (PubMed:16463103,
PubMed:16730712). Transcriptionally regulated by BZR2
(PubMed:19170933). {ECO:0000269|PubMed:10571865,
ECO:0000269|PubMed:16463103, ECO:0000269|PubMed:16730712,
ECO:0000269|PubMed:19170933, ECO:0000269|PubMed:20696912}.
-!- DOMAIN: The N-terminus (11-116) contains a fully active minimal
DNA-binding domain. {ECO:0000269|PubMed:24583075}.
-!- PTM: Ubiquitinated by MIEL1. {ECO:0000269|PubMed:23403577}.
-!- PTM: Sumoylated at Lys-283 by SIZ1. Stabilizes MYB30 and is
required for its function in ABA signaling.
{ECO:0000269|PubMed:22814374}.
-!- PTM: Simultaneous S-nitrosylation at Cys-49 and CYS-53 negatively
regulates DNA-binding activity. {ECO:0000269|PubMed:24583075}.
-!- DISRUPTION PHENOTYPE: Altered brassinosteroids response phenotypes
(PubMed:19170933). Hypersensitivity to ABA during germination and
seedling growth (PubMed:22814374). {ECO:0000269|PubMed:19170933,
ECO:0000269|PubMed:22814374}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ007289; CAA07433.1; -; mRNA.
EMBL; AF250339; AAG10145.1; -; mRNA.
EMBL; AP000386; BAB02134.1; -; Genomic_DNA.
EMBL; CP002686; AEE77505.1; -; Genomic_DNA.
EMBL; AY081278; AAL91167.1; -; mRNA.
EMBL; AY114560; AAM47879.1; -; mRNA.
EMBL; AY519592; AAS10062.1; -; mRNA.
PIR; T51621; T51621.
RefSeq; NP_189533.1; NM_113812.5.
UniGene; At.10902; -.
UniGene; At.67623; -.
ProteinModelPortal; Q9SCU7; -.
SMR; Q9SCU7; -.
DIP; DIP-59548N; -.
IntAct; Q9SCU7; 3.
STRING; 3702.AT3G28910.1; -.
PaxDb; Q9SCU7; -.
EnsemblPlants; AT3G28910.1; AT3G28910.1; AT3G28910.
GeneID; 822525; -.
Gramene; AT3G28910.1; AT3G28910.1; AT3G28910.
KEGG; ath:AT3G28910; -.
Araport; AT3G28910; -.
TAIR; locus:2090764; AT3G28910.
eggNOG; KOG0048; Eukaryota.
eggNOG; COG5147; LUCA.
KO; K09422; -.
OMA; ADINMAK; -.
OrthoDB; EOG09360JGU; -.
PhylomeDB; Q9SCU7; -.
PRO; PR:Q9SCU7; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9SCU7; baseline and differential.
Genevisible; Q9SCU7; AT.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:TAIR.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001135; F:transcription factor activity, RNA polymerase II transcription factor recruiting; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0009626; P:plant-type hypersensitive response; IEP:TAIR.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0009733; P:response to auxin; IEP:TAIR.
GO; GO:0009617; P:response to bacterium; IEP:TAIR.
GO; GO:0009723; P:response to ethylene; IEP:TAIR.
GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:TAIR.
CDD; cd00167; SANT; 2.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017930; Myb_dom.
InterPro; IPR001005; SANT/Myb.
Pfam; PF00249; Myb_DNA-binding; 2.
SMART; SM00717; SANT; 2.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS51294; HTH_MYB; 2.
1: Evidence at protein level;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Plant defense; Reference proteome; Repeat; S-nitrosylation;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 323 Transcription factor MYB30.
/FTId=PRO_0000434021.
DOMAIN 9 61 HTH myb-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DOMAIN 62 116 HTH myb-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 37 61 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 89 112 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
COMPBIAS 130 200 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
MOD_RES 49 49 S-nitrosocysteine.
{ECO:0000269|PubMed:24583075}.
MOD_RES 53 53 S-nitrosocysteine.
{ECO:0000269|PubMed:24583075}.
CROSSLNK 283 283 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:22814374}.
MUTAGEN 49 49 C->A: No effect on DNA-binding. Loss of
DNA-binding; when associated with A-53.
{ECO:0000269|PubMed:24583075}.
MUTAGEN 53 53 C->A: No effect on DNA-binding. Loss of
DNA-binding; when associated with A-49.
{ECO:0000269|PubMed:24583075}.
MUTAGEN 232 232 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:22814374}.
MUTAGEN 250 250 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:22814374}.
MUTAGEN 283 283 K->R: Loss of sumoylation.
{ECO:0000269|PubMed:22814374}.
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


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