ID MBF1C_ARATH Reviewed; 148 AA.
AC Q9LV58; Q8LE67;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=Multiprotein-bridging factor 1c;
GN Name=MBF1C; OrderedLocusNames=At3g24500; ORFNames=MOB24.13;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ABSCISIC ACID.
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 [7]
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 [8]
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 [9]
RP FUNCTION, INDUCTION BY HEAT STRESS, AND INDUCTION BY DEHYDRATION.
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).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS, INTERACTION WITH
RP TPS5, AND DISRUPTION PHENOTYPE.
RX PubMed=18201973; DOI=10.1074/jbc.m709187200;
RA Suzuki N., Bajad S., Shuman J., Shulaev V., Mittler R.;
RT "The transcriptional co-activator MBF1c is a key regulator of
RT thermotolerance in Arabidopsis thaliana.";
RL J. Biol. Chem. 283:9269-9275(2008).
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. Involved in the
CC tolerance to heat and osmotic stress by partially activating the
CC ethylene-response signal transduction pathway.
CC {ECO:0000269|PubMed:14988493, ECO:0000269|PubMed:16244138,
CC ECO:0000269|PubMed:18201973}.
CC -!- SUBUNIT: Binds to TPS5.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm.
CC Note=PubMed:16283071 shows a localization restricted to the nucleus and
CC not altered by heat or ABA treatment, while PubMed:18201973 describes a
CC transport from the cytoplasm to the nucleus induced by heat stress.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LV58-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers,
CC siliques and shoots. Not detected in seeds.
CC {ECO:0000269|PubMed:14988493, ECO:0000269|PubMed:15451167}.
CC -!- DEVELOPMENTAL STAGE: Scarcely expressed in early stages, restricted to
CC the shoot apical meristem in 14-day-old seedlings and detected in all
CC tissues in 28-day-old seedlings. {ECO:0000269|PubMed:15451167}.
CC -!- INDUCTION: By abscisic acid, H(2)O(2), heat treatment, dehydration and
CC high salt, but not by cold treatment, 2,4-D, ACC, methyl jasmonate or
CC salicylic acid. {ECO:0000269|PubMed:14988493,
CC ECO:0000269|PubMed:15451167, ECO:0000269|PubMed:16244138,
CC ECO:0000269|PubMed:18201973}.
CC -!- DISRUPTION PHENOTYPE: Plants are deficient in basal thermotolerance.
CC {ECO:0000269|PubMed:18201973}.
CC -!- SIMILARITY: Belongs to the MBF1 family. {ECO:0000305}.
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DR EMBL; AB020746; BAB01997.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76905.1; -; Genomic_DNA.
DR EMBL; BT004761; AAO44027.1; -; mRNA.
DR EMBL; AY085593; AAM62814.1; -; mRNA.
DR EMBL; AK227957; BAE99925.1; -; mRNA.
DR RefSeq; NP_189093.1; NM_113358.3. [Q9LV58-1]
DR AlphaFoldDB; Q9LV58; -.
DR SMR; Q9LV58; -.
DR BioGRID; 7372; 7.
DR IntAct; Q9LV58; 6.
DR STRING; 3702.Q9LV58; -.
DR PaxDb; 3702-AT3G24500-1; -.
DR ProteomicsDB; 238692; -. [Q9LV58-1]
DR EnsemblPlants; AT3G24500.1; AT3G24500.1; AT3G24500. [Q9LV58-1]
DR GeneID; 822041; -.
DR Gramene; AT3G24500.1; AT3G24500.1; AT3G24500. [Q9LV58-1]
DR KEGG; ath:AT3G24500; -.
DR Araport; AT3G24500; -.
DR TAIR; AT3G24500; MBF1C.
DR eggNOG; KOG3398; Eukaryota.
DR HOGENOM; CLU_112609_1_0_1; -.
DR InParanoid; Q9LV58; -.
DR OMA; DWDPIVL; -.
DR OrthoDB; 120438at2759; -.
DR PhylomeDB; Q9LV58; -.
DR PRO; PR:Q9LV58; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV58; baseline and differential.
DR Genevisible; Q9LV58; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:TAIR.
DR GO; GO:0003713; F:transcription coactivator activity; IGI:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; TAS:TAIR.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013729; MBF1_N.
DR PANTHER; PTHR10245:SF15; ENDOTHELIAL DIFFERENTIATION-RELATED FACTOR 1; 1.
DR PANTHER; PTHR10245; ENDOTHELIAL DIFFERENTIATION-RELATED FACTOR 1 MULTIPROTEIN BRIDGING FACTOR 1; 1.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF08523; MBF1; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..148
FT /note="Multiprotein-bridging factor 1c"
FT /id="PRO_0000325905"
FT DOMAIN 91..145
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 102..121
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT CONFLICT 7
FT /note="G -> E (in Ref. 4; AAM62814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16403 MW; 2133CFDACF068837 CRC64;
MPSRYPGAVT QDWEPVVLHK SKQKSQDLRD PKAVNAALRN GVAVQTVKKF DAGSNKKGKS
TAVPVINTKK LEEETEPAAM DRVKAEVRLM IQKARLEKKM SQADLAKQIN ERTQVVQEYE
NGKAVPNQAV LAKMEKVLGV KLRGKIGK
//
