TF2B1_ARATH
ID TF2B1_ARATH Reviewed; 312 AA.
AC P48512; Q53YU0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Transcription initiation factor IIB-1;
DE AltName: Full=General transcription factor TFIIB-1;
DE Short=AtTFIIB1;
GN Name=TFIIB1; OrderedLocusNames=At2g41630; ORFNames=T32G6.15;
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; TISSUE=Leaf, and Stem;
RX PubMed=8811869; DOI=10.1046/j.1365-313x.1996.10030561.x;
RA Baldwin D.A., Gurley W.B.;
RT "Isolation and characterization of cDNAs encoding transcription factor IIB
RT from Arabidopsis and soybean.";
RL Plant J. 10:561-568(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lawit S.J., Gurley W.B.;
RT "Binary protein-protein interactions of Arabidopsis thaliana general
RT transcription factors TFIIa, TFIIb, TFIId, TFIIe, and TFIIf.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH TBP2.
RX PubMed=10634912; DOI=10.2307/3871034;
RA Pan S., Czarnecka-Verner E., Gurley W.B.;
RT "Role of the TATA binding protein-transcription factor IIB interaction in
RT supporting basal and activated transcription in plant cells.";
RL Plant Cell 12:125-136(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23547107; DOI=10.1093/jxb/ert078;
RA Zhou J.J., Liang Y., Niu Q.K., Chen L.Q., Zhang X.Q., Ye D.;
RT "The Arabidopsis general transcription factor TFIIB1 (AtTFIIB1) is required
RT for pollen tube growth and endosperm development.";
RL J. Exp. Bot. 64:2205-2218(2013).
RN [10]
RP INTERACTION WITH ATHB-7 AND ATHB-12.
RX PubMed=24531799; DOI=10.1007/s00299-014-1576-9;
RA Capella M., Re D.A., Arce A.L., Chan R.L.;
RT "Plant homeodomain-leucine zipper I transcription factors exhibit different
RT functional AHA motifs that selectively interact with TBP or/and TFIIB.";
RL Plant Cell Rep. 33:955-967(2014).
CC -!- FUNCTION: General factor that plays a major role in the activation of
CC eukaryotic genes transcribed by RNA polymerase II (By similarity).
CC Interacts with TBP2 and is required for activated transcription and
CC possibly basal transcription (PubMed:10634912). Plays important roles
CC in pollen tube growth, guidance, and reception as well as endosperm
CC development. Is partially functionally different from TFIIB2 and PBRP2
CC (PubMed:23547107). {ECO:0000250|UniProtKB:Q8W0W3,
CC ECO:0000269|PubMed:10634912, ECO:0000269|PubMed:23547107}.
CC -!- SUBUNIT: Associates with TFIID-IIA (DA complex) to form TFIID-IIA-IIB
CC (DAB-complex) which is then recognized by polymerase II (By
CC similarity). Interacts with TBP2 (PubMed:19376835). Interacts with
CC ATHB-7 and ATHB-12 (PubMed:24531799). {ECO:0000250|UniProtKB:Q00403,
CC ECO:0000269|PubMed:24531799}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality and aborted seed when
CC homozygous. {ECO:0000269|PubMed:23547107}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {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; U31096; AAB09755.1; -; mRNA.
DR EMBL; AY463600; AAR28002.1; -; mRNA.
DR EMBL; AC002510; AAB84344.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10009.1; -; Genomic_DNA.
DR EMBL; AY093060; AAM13059.1; -; mRNA.
DR EMBL; AY128769; AAM91169.1; -; mRNA.
DR EMBL; AY086647; AAM63705.1; -; mRNA.
DR PIR; T00819; T00819.
DR RefSeq; NP_181694.1; NM_129726.4.
DR AlphaFoldDB; P48512; -.
DR SMR; P48512; -.
DR BioGRID; 4098; 13.
DR IntAct; P48512; 1.
DR STRING; 3702.AT2G41630.1; -.
DR iPTMnet; P48512; -.
DR PaxDb; P48512; -.
DR PRIDE; P48512; -.
DR ProteomicsDB; 234170; -.
DR EnsemblPlants; AT2G41630.1; AT2G41630.1; AT2G41630.
DR GeneID; 818761; -.
DR Gramene; AT2G41630.1; AT2G41630.1; AT2G41630.
DR KEGG; ath:AT2G41630; -.
DR Araport; AT2G41630; -.
DR TAIR; locus:2062703; AT2G41630.
DR eggNOG; KOG1597; Eukaryota.
DR HOGENOM; CLU_043736_1_1_1; -.
DR InParanoid; P48512; -.
DR OMA; RMWQRRM; -.
DR OrthoDB; 729732at2759; -.
DR PhylomeDB; P48512; -.
DR PRO; PR:P48512; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P48512; baseline and differential.
DR Genevisible; P48512; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:TAIR.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR023486; TFIIB_CS.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR Pfam; PF00382; TFIIB; 2.
DR PRINTS; PR00685; TIFACTORIIB.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00782; TFIIB; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..312
FT /note="Transcription initiation factor IIB-1"
FT /id="PRO_0000119301"
FT REPEAT 115..192
FT /note="1"
FT REPEAT 216..290
FT /note="2"
FT ZN_FING 2..34
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 312 AA; 34272 MW; D731D2FAE60484EA CRC64;
MSDAYCTDCK KETELVVDHS AGDTLCSECG LVLESHSIDE TSEWRTFANE SSNSDPNRVG
GPTNPLLADS ALTTVIAKPN GSSGDFLSSS LGRWQNRNSN SDRGLIQAFK TIATMSERLG
LVATIKDRAN ELYKRLEDQK SSRGRNQDAL YAACLYIACR QEDKPRTIKE ICVIANGATK
KEIGRAKDYI VKTLGLEPGQ SVDLGTIHAG DFMRRFCSNL AMSNHAVKAA QEAVQKSEEF
DIRRSPISIA AVVIYIITQL SDDKKTLKDI SHATGVAEGT IRNSYKDLYP HLSKIAPSWY
AKEEDLKNLS SP
