MBF1B_ARATH
ID MBF1B_ARATH Reviewed; 142 AA.
AC Q9LXT3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Multiprotein-bridging factor 1b;
GN Name=MBF1B; OrderedLocusNames=At3g58680; ORFNames=T20N10.30;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14988493; DOI=10.1093/pcp/pch017;
RA Tsuda K., Tsuji T., Hirose S., Yamazaki K.;
RT "Three Arabidopsis MBF1 homologs with distinct expression profiles play
RT roles as transcriptional co-activators.";
RL Plant Cell Physiol. 45:225-231(2004).
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15451167; DOI=10.1016/j.bbaexp.2004.08.004;
RA Tsuda K., Yamazaki K.;
RT "Structure and expression analysis of three subtypes of Arabidopsis MBF1
RT genes.";
RL Biochim. Biophys. Acta 1680:1-10(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16283071; DOI=10.1007/s10265-005-0238-y;
RA Sugikawa Y., Ebihara S., Tsuda K., Niwa Y., Yamazaki K.;
RT "Transcriptional coactivator MBF1s from Arabidopsis predominantly localize
RT in nucleolus.";
RL J. Plant Res. 118:431-437(2005).
RN [8]
RP INDUCTION.
RX PubMed=16244138; DOI=10.1104/pp.105.070110;
RA Suzuki N., Rizhsky L., Liang H., Shuman J., Shulaev V., Mittler R.;
RT "Enhanced tolerance to environmental stress in transgenic plants expressing
RT the transcriptional coactivator multiprotein bridging factor 1c.";
RL Plant Physiol. 139:1313-1322(2005).
CC -!- FUNCTION: Transcriptional coactivator that stimulates transcriptional
CC activity by bridging regulatory proteins and TBP, thereby recruiting
CC TBP to promoters occupied by DNA-binding regulators. {ECO:0000250,
CC ECO:0000269|PubMed:14988493}.
CC -!- INTERACTION:
CC Q9LXT3; Q84JU4: IBR5; NbExp=3; IntAct=EBI-15217346, EBI-604555;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16283071}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, petioles and
CC shoots. Higher expression in flowers and siliques. Detected in leaf
CC veins through development. {ECO:0000269|PubMed:14988493,
CC ECO:0000269|PubMed:15451167}.
CC -!- DEVELOPMENTAL STAGE: Detected only in seeds of 2-3 days after
CC pollination (dap) siliques. {ECO:0000269|PubMed:15451167}.
CC -!- INDUCTION: Not induced by heat or cold treatments, H(2)O(2),
CC dehydration, high salt, abscisic acid, 2,4-D, ACC, methyl jasmonate or
CC salicylic acid. {ECO:0000269|PubMed:14988493,
CC ECO:0000269|PubMed:15451167, ECO:0000269|PubMed:16244138}.
CC -!- SIMILARITY: Belongs to the MBF1 family. {ECO:0000305}.
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DR EMBL; AL353032; CAB88285.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79817.1; -; Genomic_DNA.
DR EMBL; AF324717; AAG40068.1; -; mRNA.
DR EMBL; AF326909; AAG41491.1; -; mRNA.
DR EMBL; AF339728; AAK00410.1; -; mRNA.
DR EMBL; AY042850; AAK68790.1; -; mRNA.
DR EMBL; AY081487; AAM10049.1; -; mRNA.
DR EMBL; AY084597; AAM61162.1; -; mRNA.
DR PIR; T49151; T49151.
DR RefSeq; NP_191427.1; NM_115730.4.
DR AlphaFoldDB; Q9LXT3; -.
DR SMR; Q9LXT3; -.
DR BioGRID; 10352; 9.
DR IntAct; Q9LXT3; 9.
DR STRING; 3702.AT3G58680.1; -.
DR iPTMnet; Q9LXT3; -.
DR MetOSite; Q9LXT3; -.
DR PaxDb; Q9LXT3; -.
DR PRIDE; Q9LXT3; -.
DR ProteomicsDB; 238374; -.
DR EnsemblPlants; AT3G58680.1; AT3G58680.1; AT3G58680.
DR GeneID; 825037; -.
DR Gramene; AT3G58680.1; AT3G58680.1; AT3G58680.
DR KEGG; ath:AT3G58680; -.
DR Araport; AT3G58680; -.
DR TAIR; locus:2098994; AT3G58680.
DR eggNOG; KOG3398; Eukaryota.
DR HOGENOM; CLU_112609_1_0_1; -.
DR InParanoid; Q9LXT3; -.
DR OMA; IMHARTE; -.
DR OrthoDB; 1571466at2759; -.
DR PhylomeDB; Q9LXT3; -.
DR PRO; PR:Q9LXT3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXT3; baseline and differential.
DR Genevisible; Q9LXT3; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003713; F:transcription coactivator activity; IGI:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:TAIR.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013729; MBF1_N.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF08523; MBF1; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..142
FT /note="Multiprotein-bridging factor 1b"
FT /id="PRO_0000325904"
FT DOMAIN 87..141
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 98..117
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT REGION 49..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 142 AA; 15582 MW; D39DA199C813236F CRC64;
MAGIGPITQD WEPVVIRKRA PNAAAKRDEK TVNAARRSGA DIETVRKFNA GSNKAASSGT
SLNTKKLDDD TENLSHDRVP TELKKAIMQA RGEKKLTQSQ LAHLINEKPQ VIQEYESGKA
IPNQQILSKL ERALGAKLRG KK
