TAFCL_ARATH
ID TAFCL_ARATH Reviewed; 681 AA.
AC B2C6R6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Transcription initiation factor TFIID subunit 12b;
DE AltName: Full=Protein CYTOKININ-HYPERSENSITIVE 1;
DE AltName: Full=Protein ENHANCED ETHYLENE RESPONSE 4;
DE AltName: Full=TBP-associated factor 12b;
DE Short=AtTAF12b;
GN Name=TAF12B; Synonyms=CKH1, EER4;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY CYTOKININS.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=21357579; DOI=10.1093/pcp/pcr021;
RA Kubo M., Furuta K., Demura T., Fukuda H., Liu Y.G., Shibata D.,
RA Kakimoto T.;
RT "The CKH1/EER4 gene encoding a TAF12-like protein negatively regulates
RT cytokinin sensitivity in Arabidopsis thaliana.";
RL Plant Cell Physiol. 52:629-637(2011).
RN [2]
RP INTERACTION WITH PKL.
RX PubMed=21357580; DOI=10.1093/pcp/pcr022;
RA Furuta K., Kubo M., Sano K., Demura T., Fukuda H., Liu Y.G., Shibata D.,
RA Kakimoto T.;
RT "The CKH2/PKL chromatin remodeling factor negatively regulates cytokinin
RT responses in Arabidopsis calli.";
RL Plant Cell Physiol. 52:618-628(2011).
CC -!- FUNCTION: TAFs are components of the transcription factor IID (TFIID)
CC complex that is essential for mediating regulation of RNA polymerase
CC transcription. Required for the expression of a subset of ethylene-
CC responsive genes (By similarity). Involved in the negative regulation
CC of cytokinin sensitivity. {ECO:0000250, ECO:0000269|PubMed:21357579}.
CC -!- SUBUNIT: Component of the TFIID complex. TFIID is composed of TATA
CC binding protein (TBP) and a number of TBP-associated factors (TAFs)
CC whose MWs range from 14-217 kDa. Can homodimerize. Interacts with
CC PP2A1, PP2A5, ERF1B, EIN3, TAF4, TAF4B, TAF5, TAF8, TAF10, TAF11,
CC TAF12, TAF13, TAF14, TAF14B, TAF15 and TAF15B (By similarity).
CC Interacts with PKL. {ECO:0000250, ECO:0000269|PubMed:21357580}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21357579}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:21357579}.
CC -!- INDUCTION: Not up-regulated by cytokinins.
CC {ECO:0000269|PubMed:21357579}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to cytokinins.
CC {ECO:0000269|PubMed:21357579}.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
CC -!- CAUTION: TAF12B in cv. Columbia (AC Q940A7) is 2 amino acids longer.
CC {ECO:0000305}.
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DR EMBL; EU293889; ACA50283.1; -; mRNA.
DR AlphaFoldDB; B2C6R6; -.
DR SMR; B2C6R6; -.
DR IntAct; B2C6R6; 2.
DR ExpressionAtlas; B2C6R6; baseline and differential.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 2.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..681
FT /note="Transcription initiation factor TFIID subunit 12b"
FT /id="PRO_0000424052"
FT DOMAIN 523..596
FT /note="Histone-fold"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 74563 MW; 458295D372BF0A6F CRC64;
MAEPIPSSSL SPKSLQSPNP MEPSPASSTP LPSSSSQQQQ LMTAPISNSV NSAASPAMTV
TTTEGIVIQN NSQPNISSPN PTSSNPPIGA QIPSPSPLSH PSSSLDQQTQ TQQLVQQTQQ
LPQQQQQIMQ QISSSPIPQL SPQQQQILQQ QHMTSQQIPM SSYQIAQSLQ RSPSLSRLSQ
IQQQQQQQQH QGQYGNVLRQ QAGLYGTMNF GGSGSVQQSQ QNQQMVNPNM SRAALVGQSG
HLPMLNGAAG AAQMNIQPQL LAASPRQKSG MVQGSQFHPG SSGQQLQGMQ AMGMMGSLNL
TSQMRGNPAL YAQQRINPGQ MRQQLSQQNA LTSPQVQNLQ RTSSLAFMNP QLSGLAQNGQ
AGMMQNSLSQ QQWLKQMSGI TSPNSFRLQP SQRQALLLQQ QQQQLSSPQL HQSSMSLNQQ
QISQIIQQQQ QQSQLGQSQM NQSHSQQQLQ QMQQQLQQQP QQQMQQQQQQ QQQMQINQQQ
PSPRMLSHAG QKSVSLTGSQ PEATQSGTTT PGGSSSQGTE ATNQLLGKRK IQDLVSQVDV
HAKLDPDVED LLLEVADDFI DSVTSFACSL AKHRKSSVLE PKDILLHLEK NLHLTIPGFS
SEDKRQTKTV PTDLHKKRLA MVRALLESSK PETNASNSKE TMRQAMVNPN GPNHLLRPSQ
SSEQLVSQTS GPHILQHMTR Y
