MYB96_ARATH
ID MYB96_ARATH Reviewed; 352 AA.
AC Q24JK1; Q6R036; Q9SPG0; Q9ZRY6;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Transcription factor MYB96 {ECO:0000303|PubMed:11597504};
DE AltName: Full=Myb-related protein 96 {ECO:0000303|PubMed:11597504};
DE Short=AtMYB96 {ECO:0000303|PubMed:11597504};
GN Name=MYB96 {ECO:0000303|PubMed:11597504};
GN Synonyms=MYBCOV1 {ECO:0000312|EMBL:AED97611.1};
GN OrderedLocusNames=At5g62470 {ECO:0000312|Araport:AT5G62470};
GN ORFNames=K19B1.8 {ECO:0000312|EMBL:BAB11497.1};
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] (ISOFORM 2), GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11597504; DOI=10.1016/s1369-5266(00)00199-0;
RA Stracke R., Werber M., Weisshaar B.;
RT "The R2R3-MYB gene family in Arabidopsis thaliana.";
RL Curr. Opin. Plant Biol. 4:447-456(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Qu L., Gu H.;
RT "The MYB transcription factor family in Arabidopsis: A genome-wide cloning
RT and expression pattern Analysis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-352 (ISOFORM 1), AND INDUCTION BY THE
RP CAULIFLOWER MOSAIC VIRUS.
RX PubMed=10226370; DOI=10.1094/mpmi.1999.12.5.377;
RA Geri C.E., Cecchini E., Giannakou M.E., Covey S.N., Milner J.J.;
RT "Altered patterns of gene expression in Arabidopsis elicited by cauliflower
RT mosaic virus (CaMV) infection and by a CaMV gene VI transgene.";
RL Mol. Plant Microbe Interact. 12:377-384(1999).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19625633; DOI=10.1104/pp.109.144220;
RA Seo P.J., Xiang F., Qiao M., Park J.Y., Lee Y.N., Kim S.G., Lee Y.H.,
RA Park W.J., Park C.M.;
RT "The MYB96 transcription factor mediates abscisic acid signaling during
RT drought stress response in Arabidopsis.";
RL Plant Physiol. 151:275-289(2009).
RN [9]
RP FUNCTION.
RX PubMed=20149112; DOI=10.1111/j.1469-8137.2010.03183.x;
RA Seo P.J., Park C.M.;
RT "MYB96-mediated abscisic acid signals induce pathogen resistance response
RT by promoting salicylic acid biosynthesis in Arabidopsis.";
RL New Phytol. 186:471-483(2010).
RN [10]
RP FUNCTION.
RX PubMed=21398568; DOI=10.1105/tpc.111.083485;
RA Seo P.J., Lee S.B., Suh M.C., Park M.J., Go Y.S., Park C.M.;
RT "The MYB96 transcription factor regulates cuticular wax biosynthesis under
RT drought conditions in Arabidopsis.";
RL Plant Cell 23:1138-1152(2011).
RN [11]
RP FUNCTION.
RX PubMed=23404903; DOI=10.1093/jxb/ert040;
RA Guo L., Yang H., Zhang X., Yang S.;
RT "Lipid transfer protein 3 as a target of MYB96 mediates freezing and
RT drought stress in Arabidopsis.";
RL J. Exp. Bot. 64:1755-1767(2013).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=25912720; DOI=10.1111/tpj.12866;
RA Lee H.G., Seo P.J.;
RT "The MYB96-HHP module integrates cold and abscisic acid signaling to
RT activate the CBF-COR pathway in Arabidopsis.";
RL Plant J. 82:962-977(2015).
RN [13]
RP FUNCTION.
RX PubMed=25616734; DOI=10.1007/s11103-015-0283-4;
RA Lee H.G., Lee K., Seo P.J.;
RT "The Arabidopsis MYB96 transcription factor plays a role in seed
RT dormancy.";
RL Plant Mol. Biol. 87:371-381(2015).
RN [14]
RP FUNCTION.
RX PubMed=25869652; DOI=10.1104/pp.15.00162;
RA Lee K., Lee H.G., Yoon S., Kim H.U., Seo P.J.;
RT "The Arabidopsis MYB96 transcription factor is a positive regulator of
RT ABSCISIC ACID-INSENSITIVE4 in the control of seed germination.";
RL Plant Physiol. 168:677-689(2015).
RN [15]
RP FUNCTION.
RX PubMed=27577115; DOI=10.1093/pcp/pcw147;
RA Lee S.B., Kim H.U., Suh M.C.;
RT "MYB94 and MYB96 additively activate cuticular wax biosynthesis in
RT Arabidopsis.";
RL Plant Cell Physiol. 57:2300-2311(2016).
RN [16]
RP FUNCTION.
RX PubMed=26725725; DOI=10.1038/srep17754;
RA Lee H.G., Mas P., Seo P.J.;
RT "MYB96 shapes the circadian gating of ABA signaling in Arabidopsis.";
RL Sci. Rep. 6:17754-17754(2016).
RN [17]
RP FUNCTION, AND INTERACTION WITH HDA15.
RX PubMed=30979883; DOI=10.1038/s41467-019-09417-1;
RA Lee H.G., Seo P.J.;
RT "MYB96 recruits the HDA15 protein to suppress negative regulators of ABA
RT signaling in Arabidopsis.";
RL Nat. Commun. 10:1713-1713(2019).
CC -!- FUNCTION: Transcription activator involved in the activation of
CC cuticular wax biosynthesis under drought stress. Binds directly to DNA
CC consensus sequences found in the promoters of genes encoding very-long-
CC chain fatty acid-condensing enzymes involved in cuticular wax
CC biosynthesis (PubMed:21398568). Functions together with MYB94 in the
CC activation of cuticular wax biosynthesis (PubMed:27577115). Involved in
CC drought stress response through abscisic acid (ABA) signaling. Mediates
CC ABA signals that enhance plant resistance to drought by reducing
CC stomatal opening. Mediates ABA-auxin cross-talk to regulate lateral
CC root growth under drought stress conditions (PubMed:19625633). Involved
CC in the regulation of ABA biosynthesis and ABA-dependent seed dormancy
CC state. Binds to the promoters of NCED2 and NCED6, which are enzymes
CC catalyzing the first step of ABA biosynthesis (PubMed:25616734).
CC Regulates seed germination by controlling the expression of ABI4, a
CC repressor of lipid breakdown during seed germination (PubMed:25869652).
CC Binds to the promoter of LTP3 and transactivates LTP3 gene in response
CC to drought stress and freezing (PubMed:23404903). Involved in cold
CC stress response. Binds directly to the promoters of heptahelical
CC protein (HHP) genes in response to cold stress. HHPs modulate the
CC expression of SCRM/ICE1, SCRM2/ICE2 and CAMTA3, which are upstream
CC regulators of cold-responsive C-repeat-binding factors (CBFs)
CC (PubMed:25912720). Involved in defense responses against the bacterial
CC pathogen Pseudomonas syringae. May act as a molecular link that
CC mediates cross-talks between ABA and salicylate (PubMed:20149112).
CC Involved in a crosstalk between the circadian clock and ABA signaling.
CC Binds directly to the promoter of APRR1/TOC1 to activate its expression
CC (PubMed:26725725). Promotes ABA signaling (PubMed:30979883). Recruits
CC the histone deacetylase HDA15 to the promoters of a subset of Rho
CC GTPase (ROP) genes, which repress ABA signaling at the early stages of
CC signal transduction (PubMed:30979883). HDA15 represses ROP expression
CC by removing acetyl groups of histone H3 and H4 from the cognate
CC regions, particularly in the presence of ABA (PubMed:30979883).
CC {ECO:0000269|PubMed:19625633, ECO:0000269|PubMed:20149112,
CC ECO:0000269|PubMed:21398568, ECO:0000269|PubMed:23404903,
CC ECO:0000269|PubMed:25616734, ECO:0000269|PubMed:25869652,
CC ECO:0000269|PubMed:25912720, ECO:0000269|PubMed:26725725,
CC ECO:0000269|PubMed:27577115, ECO:0000269|PubMed:30979883}.
CC -!- SUBUNIT: Interacts with HDA15. {ECO:0000269|PubMed:30979883}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:19625633}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q24JK1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q24JK1-2; Sequence=VSP_059283;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, guard cells and
CC lateral root primordia. {ECO:0000269|PubMed:19625633}.
CC -!- INDUCTION: Induced by drought stress, salt stress and abscisic acid
CC (ABA) (PubMed:19625633). Induced by infection with the cauliflower
CC mosaic virus (CaMV) (PubMed:10226370). Induced by cold stress
CC (PubMed:25912720). {ECO:0000269|PubMed:10226370,
CC ECO:0000269|PubMed:19625633, ECO:0000269|PubMed:25912720}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased susceptibility to
CC drought stress. {ECO:0000269|PubMed:19625633}.
CC -!- MISCELLANEOUS: Plants overexpressing MYB96 exhibit a dwarf growth,
CC altered leaf morphology, reduced lateral roots, and enhanced drought
CC resistance (PubMed:19625633). The gain-of-function mutant myb96-1D
CC (activation tagging) plants exhibit deposition of epicuticuar wax
CC crystals on leaf surface (PubMed:21398568). The gain-of-function mutant
CC myb96-1D (activation tagging) plants accumulate high levels of
CC anthocyanins and salicylate (SA), express pathogenesis-related (PR)
CC genes constitutively, and exhibit enhanced resistance to Pseudomonas
CC syringae infection (PubMed:20149112). {ECO:0000269|PubMed:19625633,
CC ECO:0000269|PubMed:20149112, ECO:0000269|PubMed:21398568}.
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DR EMBL; AF176001; AAD53106.1; -; mRNA.
DR EMBL; AY519645; AAS10115.1; -; mRNA.
DR EMBL; AB015469; BAB11497.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97610.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97611.1; -; Genomic_DNA.
DR EMBL; BT024888; ABD85159.1; -; mRNA.
DR EMBL; AK228977; BAF00865.1; -; mRNA.
DR EMBL; AJ011669; CAA09728.1; -; mRNA.
DR PIR; T52590; T52590.
DR RefSeq; NP_201053.2; NM_125641.4. [Q24JK1-1]
DR RefSeq; NP_851248.1; NM_180917.1. [Q24JK1-2]
DR AlphaFoldDB; Q24JK1; -.
DR SMR; Q24JK1; -.
DR STRING; 3702.AT5G62470.2; -.
DR PaxDb; Q24JK1; -.
DR PRIDE; Q24JK1; -.
DR ProteomicsDB; 248914; -. [Q24JK1-1]
DR EnsemblPlants; AT5G62470.1; AT5G62470.1; AT5G62470. [Q24JK1-2]
DR EnsemblPlants; AT5G62470.2; AT5G62470.2; AT5G62470. [Q24JK1-1]
DR GeneID; 836367; -.
DR Gramene; AT5G62470.1; AT5G62470.1; AT5G62470. [Q24JK1-2]
DR Gramene; AT5G62470.2; AT5G62470.2; AT5G62470. [Q24JK1-1]
DR KEGG; ath:AT5G62470; -.
DR Araport; AT5G62470; -.
DR TAIR; locus:2154119; AT5G62470.
DR eggNOG; KOG0048; Eukaryota.
DR InParanoid; Q24JK1; -.
DR OMA; ENMIGIM; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q24JK1; -.
DR PRO; PR:Q24JK1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q24JK1; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1904278; P:positive regulation of wax biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:2000033; P:regulation of seed dormancy process; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; 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 Abscisic acid signaling pathway; Activator; Alternative splicing;
KW DNA-binding; Nucleus; Plant defense; Reference proteome; Repeat;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..352
FT /note="Transcription factor MYB96"
FT /id="PRO_0000442919"
FT DOMAIN 9..65
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 66..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..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 47
FT /note="Missing (in isoform 2)"
FT /id="VSP_059283"
FT CONFLICT 134
FT /note="N -> S (in Ref. 7; CAA09728)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="I -> V (in Ref. 2; AAS10115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39188 MW; 3554956483EEDFEE CRC64;
MGRPPCCEKI GVKKGPWTPE EDIILVSYIQ EHGPGNWRSV PTHTGLRRCS KSCRLRWTNY
LRPGIKRGNF TEHEEKTIVH LQALLGNRWA AIASYLPERT DNDIKNYWNT HLKKKLKKIN
ESGEEDNDGV SSSNTSSQKN HQSTNKGQWE RRLQTDINMA KQALCEALSL DKPSSTLSSS
SSLPTPVITQ QNIRNFSSAL LDRCYDPSSS SSSTTTTTTS NTTNPYPSGV YASSAENIAR
LLQDFMKDTP KALTLSSSSP VSETGPLTAA VSEEGGEGFE QSFFSFNSMD ETQNLTQETS
FFHDQVIKPE ITMDQDHGLI SQGSLSLFEK WLFDEQSHEM VGMALAGQEG MF
