MYB56_ARATH
ID MYB56_ARATH Reviewed; 323 AA.
AC Q6R053; Q9FN72; Q9ZTD6;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transcription factor MYB56 {ECO:0000303|PubMed:9839469};
DE AltName: Full=Myb-related protein 56 {ECO:0000303|PubMed:9839469};
DE Short=AtMYB56 {ECO:0000303|PubMed:9839469};
DE AltName: Full=Protein BRASSINOSTEROIDS AT VASCULAR AND ORGANIZING CENTER {ECO:0000303|PubMed:24981610};
GN Name=MYB56 {ECO:0000303|PubMed:9839469};
GN Synonyms=BRAVO {ECO:0000303|PubMed:24981610};
GN OrderedLocusNames=At5g17800 {ECO:0000312|Araport:AT5G17800};
GN ORFNames=MVA3.16 {ECO:0000312|EMBL:BAB09579.1};
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 143-323, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9839469; DOI=10.1046/j.1365-313x.1998.00278.x;
RA Kranz H.D., Denekamp M., Greco R., Jin H.-L., Leyva A., Meissner R.C.,
RA Petroni K., Urzainqui A., Bevan M., Martin C., Smeekens S., Tonelli C.,
RA Paz-Ares J., Weisshaar B.;
RT "Towards functional characterisation of the members of the R2R3-MYB gene
RT family from Arabidopsis thaliana.";
RL Plant J. 16:263-276(1998).
RN [6]
RP GENE FAMILY.
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 TISSUE SPECIFICITY.
RX PubMed=16581911; DOI=10.1073/pnas.0510607103;
RA Lee J.-Y., Colinas J., Wang J.Y., Mace D., Ohler U., Benfey P.N.;
RT "Transcriptional and posttranscriptional regulation of transcription factor
RT expression in Arabidopsis roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6055-6060(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23911125; DOI=10.1111/jipb.12094;
RA Zhang Y., Liang W., Shi J., Xu J., Zhang D.;
RT "MYB56 encoding a R2R3 MYB transcription factor regulates seed size in
RT Arabidopsis thaliana.";
RL J. Integr. Plant Biol. 55:1166-1178(2013).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP BES1, REPRESSION BY BES1, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=24981610; DOI=10.1016/j.devcel.2014.05.020;
RA Vilarrasa-Blasi J., Gonzalez-Garcia M.P., Frigola D., Fabregas N.,
RA Alexiou K.G., Lopez-Bigas N., Rivas S., Jauneau A., Lohmann J.U.,
RA Benfey P.N., Ibanes M., Cano-Delgado A.I.;
RT "Regulation of plant stem cell quiescence by a brassinosteroid signaling
RT module.";
RL Dev. Cell 30:36-47(2014).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, REGULATION BY CRL3(BPMS), INDUCTION,
RP INTERACTION WITH BPM1; BPM2; BPM3; BPM4; BPM5 AND BPM6, HOMODIMERIZATION,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25343985; DOI=10.1093/mp/ssu120;
RA Chen L., Bernhardt A., Lee J., Hellmann H.;
RT "Identification of Arabidopsis MYB56 as a novel substrate for CRL3BPM E3
RT ligases.";
RL Mol. Plant 0:0-0(2014).
CC -!- FUNCTION: Acts as a cell-specific local repressor of quiescent center
CC (QC) self-renewal by cell divisions in the primary root. Counteracts
CC brassinosteroid (BR)-mediated cell division in the QC cells
CC (PubMed:24981610). Regulates maternally seed size, especially before
CC the heart stage, promoting both endothelial cells expansion and cell
CC number in the outer integument layer of the seed coat
CC (PubMed:23911125). Modulates the expression of genes involved in cell
CC wall metabolism such as cell division and expansion (PubMed:23911125,
CC PubMed:24981610). Negative regulator of flowering via the repression of
CC FT transcription (PubMed:25343985). {ECO:0000269|PubMed:23911125,
CC ECO:0000269|PubMed:24981610, ECO:0000269|PubMed:25343985}.
CC -!- SUBUNIT: Forms homodimer (PubMed:25343985). Interacts with the
CC dephosphorylated active form of BES1 in the nucleus of quiescent center
CC (QC) cells (PubMed:24981610). Interacts with BPM1, BPM2, BPM3, BPM4,
CC BPM5 and BPM6 at the promoter of FLOWERING LOCUS T (FT)
CC (PubMed:25343985). {ECO:0000269|PubMed:24981610,
CC ECO:0000269|PubMed:25343985}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:24981610, ECO:0000269|PubMed:25343985}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:25343985}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers (at protein level) and
CC siliques, and, to a lower extent, in roots, stems and leaves
CC (PubMed:25343985). Expressed in embryos (e.g. heart and torpedo stages)
CC and cotyledons, and, at low levels, in roots and inflorescence
CC (PubMed:23911125). Accumulates specifically in root apical meristem
CC quiescent center (QC) and vascular initial cells (PubMed:16581911,
CC PubMed:24981610). {ECO:0000269|PubMed:16581911,
CC ECO:0000269|PubMed:23911125, ECO:0000269|PubMed:24981610,
CC ECO:0000269|PubMed:25343985}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds.
CC {ECO:0000269|PubMed:23911125}.
CC -!- INDUCTION: Levels follow a circadian cycle with a progressive decrease
CC during the day time (at protein level) (PubMed:25343985). Down-
CC regulated by brassinosteroids (BRs) in a dose- and time-dependent
CC manner. Repressed by BES1. Auto-activation of expression
CC (PubMed:24981610). Targeted to 26S proteasomal degradation by the
CC CULLIN3 (CUL3)-based E3 ligases CRL3(BPMs) (PubMed:25343985).
CC {ECO:0000269|PubMed:24981610, ECO:0000269|PubMed:25343985}.
CC -!- DISRUPTION PHENOTYPE: Smaller seeds and embryos associated with smaller
CC contracted endothelial cells and reduced cell number in the outer
CC integument layer of the seed coat during the seed development
CC (PubMed:23911125). Increased quiescent center (QC) cell divisions
CC (PubMed:24981610). Early flowering under long-day (LD) associated with
CC FT accumulation (PubMed:25343985). {ECO:0000269|PubMed:23911125,
CC ECO:0000269|PubMed:24981610, ECO:0000269|PubMed:25343985}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09579.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY519627; AAS10097.1; -; mRNA.
DR EMBL; AB006706; BAB09579.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED92471.1; -; Genomic_DNA.
DR EMBL; AK176193; BAD43956.1; -; mRNA.
DR EMBL; AK176277; BAD44040.1; -; mRNA.
DR EMBL; AF062891; AAC83613.1; -; mRNA.
DR PIR; T51663; T51663.
DR RefSeq; NP_197282.1; NM_121786.4.
DR AlphaFoldDB; Q6R053; -.
DR SMR; Q6R053; -.
DR IntAct; Q6R053; 62.
DR STRING; 3702.AT5G17800.1; -.
DR PaxDb; Q6R053; -.
DR PRIDE; Q6R053; -.
DR EnsemblPlants; AT5G17800.1; AT5G17800.1; AT5G17800.
DR GeneID; 831648; -.
DR Gramene; AT5G17800.1; AT5G17800.1; AT5G17800.
DR KEGG; ath:AT5G17800; -.
DR Araport; AT5G17800; -.
DR TAIR; locus:2175931; AT5G17800.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_18_1_1; -.
DR InParanoid; Q6R053; -.
DR OMA; HGNERGE; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q6R053; -.
DR PRO; PR:Q6R053; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6R053; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071367; P:cellular response to brassinosteroid stimulus; IEP:TAIR.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0080060; P:integument development; IMP:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:TAIR.
DR GO; GO:0048579; P:negative regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:1904961; P:quiescent center organization; IMP:UniProtKB.
DR GO; GO:0080113; P:regulation of seed growth; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 Brassinosteroid signaling pathway; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..323
FT /note="Transcription factor MYB56"
FT /id="PRO_0000438812"
FT DOMAIN 88..139
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 140..194
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 116..138
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 167..190
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 186
FT /note="W -> R (in Ref. 5; AAC83613)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> T (in Ref. 5; AAC83613)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="M -> T (in Ref. 5; AAC83613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36892 MW; 62B3D99038388D1B CRC64;
MNPNLLEKDL RGKETTNGSI RYKEANNFRS LPNSHTAACK TSLNNPSISR NHPHNKSASV
LESEDEHGNE RGENEKSLRM RGKSGINTKV CSRGHWRPTE DAKLKELVAQ FGPQNWNLIS
NHLLGRSGKS CRLRWFNQLD PRINKRAFTE EEEFRLLAAH RAYGNKWALI SRLFPGRTDN
AVKNHWHVIM ARRTRESQRQ RQQPPPTLSR DAEMTVSSSC RYNQGKFINE EDDDDDVSAV
STCTTELSLT PPSSAYQPRF FNYDSTLASG KDGQCVQRAE VNGIYGKKMD HQNHHTISVS
ERKVEMKMRS GYYYFDFLGV GAS
