MB3R3_ARATH
ID MB3R3_ARATH Reviewed; 505 AA.
AC Q8H1P9; F4IZX3; Q94CC4; Q9M652; Q9SR26;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcription factor MYB3R-3 {ECO:0000303|PubMed:11597504};
DE AltName: Full=Myb-related protein 3R-3 {ECO:0000303|PubMed:11597504};
GN Name=MYB3R3 {ECO:0000303|PubMed:11597504};
GN OrderedLocusNames=At3g09370 {ECO:0000312|Araport:AT3G09370};
GN ORFNames=F3L24.24 {ECO:0000312|EMBL:AAF14045.1};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (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 [6]
RP INDUCTION BY ETHYLENE; AUXIN; JASMONIC ACID AND SALICYLIC ACID, AND GENE
RP 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 GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17287251; DOI=10.1242/dev.02801;
RA Haga N., Kato K., Murase M., Araki S., Kubo M., Demura T., Suzuki K.,
RA Mueller I., Voss U., Juergens G., Ito M.;
RT "R1R2R3-Myb proteins positively regulate cytokinesis through activation of
RT KNOLLE transcription in Arabidopsis thaliana.";
RL Development 134:1101-1110(2007).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CDKA-1; RBR1 AND E2FC, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=26069325; DOI=10.15252/embj.201490899;
RA Kobayashi K., Suzuki T., Iwata E., Nakamichi N., Suzuki T., Chen P.,
RA Ohtani M., Ishida T., Hosoya H., Mueller S., Leviczky T.,
RA Pettko-Szandtner A., Darula Z., Iwamoto A., Nomoto M., Tada Y.,
RA Higashiyama T., Demura T., Doonan J.H., Hauser M.T., Sugimoto K., Umeda M.,
RA Magyar Z., Boegre L., Ito M.;
RT "Transcriptional repression by MYB3R proteins regulates plant organ
RT growth.";
RL EMBO J. 34:1992-2007(2015).
CC -!- FUNCTION: Transcription factor that binds 5'-AACGG-3' motifs in gene
CC promoters (By similarity). Transcription repressor that regulates organ
CC growth. Binds to the promoters of G2/M-specific genes and to E2F target
CC genes to prevent their expression in post-mitotic cells and to restrict
CC the time window of their expression in proliferating cells
CC (PubMed:26069325). {ECO:0000250|UniProtKB:Q94FL9,
CC ECO:0000269|PubMed:26069325}.
CC -!- SUBUNIT: Component of a DREAM-like complex which modulates a variety of
CC developmentally regulated genes and of the mitotic genes in
CC proliferating and differentiated cells. Associates with RBR1 in both
CC earlier and later stages of leaves development. Interacts with CDKA-1
CC and E2FC, but not with E2FB, at later stages of leaves development.
CC {ECO:0000269|PubMed:26069325}.
CC -!- INTERACTION:
CC Q8H1P9; P0DO23: CP2; NbExp=3; IntAct=EBI-4448936, EBI-4428219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H1P9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H1P9-2; Sequence=VSP_058759;
CC -!- DEVELOPMENTAL STAGE: Expressed both in proliferating and maturing
CC stages of leaves. {ECO:0000269|PubMed:26069325}.
CC -!- INDUCTION: Slightly induced by ethylene, auxin (IAA), jasmonic acid
CC (JA) and salicylic acid (SA). {ECO:0000269|PubMed:16463103}.
CC -!- DISRUPTION PHENOTYPE: In double mutant myb3r3 myb3r5 and triple mutant
CC myb3r1 myb3r3 myb3r5, up-regulation of many G2/M-specific genes leading
CC to larger seeds, organs and embryos due to overproliferation and
CC ectopic cell divisions. {ECO:0000269|PubMed:26069325}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY519651; AAS10121.1; -; mRNA.
DR EMBL; AF214117; AAF25950.2; -; mRNA.
DR EMBL; AC011436; AAF14045.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74757.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74758.1; -; Genomic_DNA.
DR EMBL; AY034964; AAK59470.1; -; mRNA.
DR EMBL; AY142649; AAN13107.1; -; mRNA.
DR RefSeq; NP_001078127.1; NM_001084658.2. [Q8H1P9-2]
DR RefSeq; NP_566350.1; NM_111771.4. [Q8H1P9-1]
DR AlphaFoldDB; Q8H1P9; -.
DR SMR; Q8H1P9; -.
DR IntAct; Q8H1P9; 8.
DR STRING; 3702.AT3G09370.2; -.
DR iPTMnet; Q8H1P9; -.
DR PRIDE; Q8H1P9; -.
DR ProteomicsDB; 250925; -. [Q8H1P9-1]
DR EnsemblPlants; AT3G09370.1; AT3G09370.1; AT3G09370. [Q8H1P9-1]
DR EnsemblPlants; AT3G09370.2; AT3G09370.2; AT3G09370. [Q8H1P9-2]
DR GeneID; 820094; -.
DR Gramene; AT3G09370.1; AT3G09370.1; AT3G09370. [Q8H1P9-1]
DR Gramene; AT3G09370.2; AT3G09370.2; AT3G09370. [Q8H1P9-2]
DR KEGG; ath:AT3G09370; -.
DR Araport; AT3G09370; -.
DR TAIR; locus:2083599; AT3G09370.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_016150_3_1_1; -.
DR OMA; RAVCTYN; -.
DR PhylomeDB; Q8H1P9; -.
DR PRO; PR:Q8H1P9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H1P9; baseline and differential.
DR GO; GO:0070176; C:DRM complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..505
FT /note="Transcription factor MYB3R-3"
FT /id="PRO_0000438893"
FT DOMAIN 73..124
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 125..180
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 181..231
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 101..124
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 153..176
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 204..227
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 14
FT /note="E -> EMMDLQ (in isoform 2)"
FT /id="VSP_058759"
FT CONFLICT 16
FT /note="E -> G (in Ref. 2; AAF25950)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="W -> R (in Ref. 5; AAK59470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56119 MW; 94823294CA29252C CRC64;
MSSTFNPAAS SPDEEETGEV KIEDQCVENK QSTPASCSSV SEGSAGSSHK SPTIASPATV
SPTHRYLGRT SGPIRRAKGG WTPEEDETLR QAVDTFKGKS WKNIAKSFPD RTEVQCLHRW
QKVLNPDLIK GPWTHEEDEK IVELVEKYGP AKWSIIAQSL PGRIGKQCRE RWHNHLNPDI
NKDAWTTEEE VALMNAHRSH GNKWAEIAKV LPGRTDNAIK NHWNSSLKKK SEFYLLTGRL
PPPTTTRNGV PDSVTKRSSS AQKRVFGSVA QTSSVTTDVN NLAEDGNGQI NSSVPVEEVV
AASRMTSLNE YARSPQLPNP EPLPENGGAA NNGYHLYYTP QIDYYRASEV DTQRMYGNEC
GCSPSASPVS FFTPPPCRNV HSNGSTPRSP ESYLREAGRT YPNTPSIFRK RRPRVVVQDN
NNAKKTDEAK EVDQKVNDGK DSSEIQNNGS NAYNLSPPYR IRSKRTAVFK SRQLEFISRE
EEKADDETKS SEKDMLIDGD SQLLG