MB3R1_ARATH
ID MB3R1_ARATH Reviewed; 776 AA.
AC Q9S7G7; O65528; Q9LDX5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Transcription factor MYB3R-1 {ECO:0000303|PubMed:11597504};
DE AltName: Full=Myb-related protein 3R-1 {ECO:0000303|PubMed:11597504};
DE AltName: Full=Plant c-MYB-like protein 1 {ECO:0000303|PubMed:10482656};
DE Short=Protein PC-MYB1 {ECO:0000303|PubMed:10482656};
GN Name=MYB3R1 {ECO:0000303|PubMed:11597504};
GN Synonyms=PC-MYB1 {ECO:0000303|PubMed:10482656};
GN OrderedLocusNames=At4g32730 {ECO:0000312|Araport:AT4G32730};
GN ORFNames=F4D11.70 {ECO:0000312|EMBL:CAA18588.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=10482656; DOI=10.1104/pp.121.1.21;
RA Braun E.L., Grotewold E.;
RT "Newly discovered plant c-myb-like genes rewrite the evolution of the plant
RT myb gene family.";
RL Plant Physiol. 121:21-24(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND VARIANTS.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=10743663; DOI=10.1046/j.1365-313x.2000.00666.x;
RA Kranz H., Scholz K., Weisshaar B.;
RT "c-MYB oncogene-like genes encoding three MYB repeats occur in all major
RT plant lineages.";
RL Plant J. 21:231-235(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [6]
RP DISRUPTION PHENOTYPE, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21862669; DOI=10.1104/pp.111.180836;
RA Haga N., Kobayashi K., Suzuki T., Maeo K., Kubo M., Ohtani M., Mitsuda N.,
RA Demura T., Nakamura K., Juergens G., Ito M.;
RT "Mutations in MYB3R1 and MYB3R4 cause pleiotropic developmental defects and
RT preferential down-regulation of multiple G2/M-specific genes in
RT Arabidopsis.";
RL Plant Physiol. 157:706-717(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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 (PubMed:21862669). Transcription activator involved in the
CC regulation of cytokinesis, probably via the activation of several G2/M
CC phase-specific genes transcription (e.g. KNOLLE) (PubMed:17287251,
CC PubMed:21862669). Transcription repressor that regulates organ growth.
CC Binds to the promoters of G2/M-specific genes and to E2F target genes
CC to prevent their expression in post-mitotic cells and to restrict the
CC time window of their expression in proliferating cells
CC (PubMed:26069325). Required for the maintenance of diploidy
CC (PubMed:21862669). {ECO:0000269|PubMed:17287251,
CC ECO:0000269|PubMed:21862669, 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. {ECO:0000250|UniProtKB:Q8H1P9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9S7G7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at low levels
CC (PubMed:10743663). Expressed in roots, cotyledons, flowers and leaves,
CC especially in vascular tissues (PubMed:17287251).
CC {ECO:0000269|PubMed:10743663, ECO:0000269|PubMed:17287251}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in the columella root cap. Also
CC present in floral organs in young flower buds. Strongly expressed in
CC vascular tissues of filaments and anthers. Weakly and uniformly present
CC in the developing embryo and maternal tissues (PubMed:17287251).
CC Expressed both in proliferating and maturing stages of leaves
CC (PubMed:26069325). {ECO:0000269|PubMed:17287251,
CC ECO:0000269|PubMed:26069325}.
CC -!- INDUCTION: Constant levels during cell cycle. Activated by CYCB1.
CC {ECO:0000269|PubMed:17287251}.
CC -!- DISRUPTION PHENOTYPE: The double mutant myb3r1 myb3r4 often fails to
CC complete cytokinesis, resulting in multinucleate cells with gapped
CC walls and cell wall stubs in diverse tissues (e.g. in embryo during the
CC first or second division after fertilization, in stomata guard mother
CC cell) and several pleiotropic developmental defects, and associated
CC with the selective reduction of several G2/M phase-specific genes
CC transcript levels (e.g. CYCB2, CDC20.1 and KNOLLE). Hypersensitivity to
CC caffeine, an inhibitor of cytokinesis (PubMed:17287251,
CC PubMed:21862669). In triple mutant myb3r1 myb3r3 myb3r5, up-regulation
CC of many G2/M-specific genes leading to larger seeds, organs and embryos
CC due to overproliferation and ectopic cell divisions (PubMed:26069325).
CC {ECO:0000269|PubMed:17287251, ECO:0000269|PubMed:21862669,
CC ECO:0000269|PubMed:26069325}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18588.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF151646; AAD46772.1; -; mRNA.
DR EMBL; AF176005; AAD53110.2; -; mRNA.
DR EMBL; AF188677; AAF77637.1; -; Genomic_DNA.
DR EMBL; AF189212; AAF77638.1; -; Genomic_DNA.
DR EMBL; AF189784; AAF78886.1; -; mRNA.
DR EMBL; AL022537; CAA18588.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161582; CAB79990.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86111.1; -; Genomic_DNA.
DR PIR; E85384; E85384.
DR PIR; T04452; T04452.
DR RefSeq; NP_194999.1; NM_119426.2. [Q9S7G7-1]
DR AlphaFoldDB; Q9S7G7; -.
DR SMR; Q9S7G7; -.
DR BioGRID; 14695; 1.
DR STRING; 3702.AT4G32730.2; -.
DR iPTMnet; Q9S7G7; -.
DR PaxDb; Q9S7G7; -.
DR EnsemblPlants; AT4G32730.1; AT4G32730.1; AT4G32730. [Q9S7G7-1]
DR GeneID; 829409; -.
DR Gramene; AT4G32730.1; AT4G32730.1; AT4G32730. [Q9S7G7-1]
DR KEGG; ath:AT4G32730; -.
DR Araport; AT4G32730; -.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_016150_0_1_1; -.
DR InParanoid; Q9S7G7; -.
DR PhylomeDB; Q9S7G7; -.
DR PRO; PR:Q9S7G7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S7G7; baseline and differential.
DR Genevisible; Q9S7G7; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:1901181; P:negative regulation of cellular response to caffeine; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IGI:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; 3.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..776
FT /note="Transcription factor MYB3R-1"
FT /id="PRO_0000234361"
FT DOMAIN 30..81
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 82..137
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 138..188
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 58..81
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 110..133
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 161..184
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 648..655
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 238..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 87
FT /note="K -> R (in strain: cv. Landsberg erecta)"
FT VARIANT 223
FT /note="N -> S (in strain: cv. Landsberg erecta)"
FT VARIANT 353
FT /note="N -> S (in strain: cv. Landsberg erecta)"
FT VARIANT 586
FT /note="D -> N (in strain: cv. Landsberg erecta)"
FT VARIANT 607
FT /note="M -> V (in strain: cv. Landsberg erecta)"
SQ SEQUENCE 776 AA; 86506 MW; 9502A6A0A68FA884 CRC64;
MKREMKAPTT PLESLQGDLK GKQGRTSGPA RRSTKGQWTP EEDEVLCKAV ERFQGKNWKK
IAECFKDRTD VQCLHRWQKV LNPELVKGPW SKEEDNTIID LVEKYGPKKW STISQHLPGR
IGKQCRERWH NHLNPGINKN AWTQEEELTL IRAHQIYGNK WAELMKFLPG RSDNSIKNHW
NSSVKKKLDS YYASGLLDQC QSSPLIALQN KSIASSSSWM HSNGDEGSSR PGVDAEESEC
SQASTVFSQS TNDLQDEVQR GNEEYYMPEF HSGTEQQISN AASHAEPYYP SFKDVKIVVP
EISCETECSK KFQNLNCSHE LRTTTATEDQ LPGVSNDAKQ DRGLELLTHN MDNGGKNQAL
QQDFQSSVRL SDQPFLSNSD TDPEAQTLIT DEECCRVLFP DNMKDSSTSS GEQGRNMVDP
QNGKGSLCSQ AAETHAHETG KVPALPWHPS SSEGLAGHNC VPLLDSDLKD SLLPRNDSNA
PIQGCRLFGA TELECKTDTN DGFIDTYGHV TSHGNDDNGG FPEQQGLSYI PKDSLKLVPL
NSFSSPSRVN KIYFPIDDKP AEKDKGALCY EPPRFPSADI PFFSCDLVPS NSDLRQEYSP
FGIRQLMISS MNCTTPLRLW DSPCHDRSPD VMLNDTAKSF SGAPSILKKR HRDLLSPVLD
RRKDKKLKRA ATSSLANDFS RLDVMLDEGD DCMTSRPSES PEDKNICASP SIARDNRNCA
SARLYQEMIP IDEEPKETLE SGGVTSMQNE NGCNDGGASA KNVSPSLSLH IIWYQL
