MB3R2_ARATH
ID MB3R2_ARATH Reviewed; 437 AA.
AC Q9SPN3; O65263;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Transcription factor MYB3R-2 {ECO:0000303|PubMed:11597504};
DE AltName: Full=Myb-related protein 3R-2 {ECO:0000303|PubMed:11597504};
DE AltName: Full=Plant c-MYB-like protein 2 {ECO:0000303|PubMed:10482656};
DE Short=Protein PC-MYB2 {ECO:0000303|PubMed:10482656};
GN Name=MYB3R2 {ECO:0000303|PubMed:11597504};
GN Synonyms=PC-MYB2 {ECO:0000303|PubMed:10482656};
GN OrderedLocusNames=At4g00540 {ECO:0000312|Araport:AT4G00540};
GN ORFNames=F6N23.19 {ECO:0000312|EMBL:AAC13637.1};
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 [MRNA], 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=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.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18426557; DOI=10.1186/1471-2164-9-182;
RA Hanano S., Stracke R., Jakoby M., Merkle T., Domagalska M.A., Weisshaar B.,
RA Davis S.J.;
RT "A systematic survey in Arabidopsis thaliana of transcription factors that
RT modulate circadian parameters.";
RL BMC Genomics 9:182-182(2008).
CC -!- FUNCTION: Transcription factor that binds 5'-AACGG-3' motifs in gene
CC promoters (By similarity). Required for proper circadian rhythm
CC (PubMed:18426557). {ECO:0000250|UniProtKB:Q94FL9,
CC ECO:0000269|PubMed:18426557}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SPN3-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Aberrant circadian rhythms.
CC {ECO:0000269|PubMed:18426557}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13637.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80863.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF151647; AAD46773.1; -; mRNA.
DR EMBL; AF218054; AAF26415.1; -; mRNA.
DR EMBL; AF058919; AAC13637.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81896.1; -; Genomic_DNA.
DR PIR; T01218; T01218.
DR RefSeq; NP_567179.1; NM_116278.1. [Q9SPN3-1]
DR AlphaFoldDB; Q9SPN3; -.
DR SMR; Q9SPN3; -.
DR STRING; 3702.AT4G00540.1; -.
DR iPTMnet; Q9SPN3; -.
DR PaxDb; Q9SPN3; -.
DR PRIDE; Q9SPN3; -.
DR EnsemblPlants; AT4G00540.1; AT4G00540.1; AT4G00540. [Q9SPN3-1]
DR GeneID; 827977; -.
DR Gramene; AT4G00540.1; AT4G00540.1; AT4G00540. [Q9SPN3-1]
DR KEGG; ath:AT4G00540; -.
DR Araport; AT4G00540; -.
DR TAIR; locus:2127108; AT4G00540.
DR eggNOG; KOG0048; Eukaryota.
DR InParanoid; Q9SPN3; -.
DR OMA; ENDSPFH; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9SPN3; -.
DR PRO; PR:Q9SPN3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SPN3; baseline and differential.
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:0042752; P:regulation of circadian rhythm; IMP: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; 1.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..437
FT /note="Transcription factor MYB3R-2"
FT /id="PRO_0000438892"
FT DOMAIN 39..95
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 96..154
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 155..205
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 67..95
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 127..150
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 178..201
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 50032 MW; 904D98D39ACF9291 CRC64;
MTESIDLNRS ESESDNNTDD VTPIFAIDDS SKGRVSGPTR RSTKGGWTAE EDQILTNVVK
KYQGRNWKRI AECLPGSEEN RRNDVQCQHR WLKVLDPSLQ KGAWKKEEDE LLSELVKDYM
ENDRPPWSKI SKELPGRIGK QCRERWHNHL NPTIIKSPWT REEELILVQA QRGNGNKWAE
IAKLLPGRTE NNIKNHWNCS VKKRLEQFPS NLFSGVVYGS KPSSGFEYNF FNQRNTMVES
CITSQIKEAA KSPQRDFLDL TLGLNWRSIS SSTSSLRGEE SVSSSVDSVC ARLNACLETP
QNSNNDTVCV KEVREMKERL RMAARTFDTP SIISKTSSPA SGLKRLRQKY DTPFPTDARS
HMSSEEDHSV SASPSSKYRF VKRNTCSGSK PLERRLDFDF LLWDEHGRRN GIVNFSVRIL
PQKSDLKSGL VRPFWLR
