TA12B_ARATH
ID TA12B_ARATH Reviewed; 683 AA.
AC Q940A7; Q9LQJ7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 138.
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; OrderedLocusNames=At1g17440;
GN ORFNames=F28G4.8;
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], IDENTIFICATION, NOMENCLATURE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15527982; DOI=10.1016/j.gene.2004.08.023;
RA Lago C., Clerici E., Mizzi L., Colombo L., Kater M.M.;
RT "TBP-associated factors in Arabidopsis.";
RL Gene 342:231-241(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND INTERACTION WITH TAF4; TAF4B;
RP TAF5; TAF8; TAF10; TAF11; TAF12; TAF13; TAF14; TAF14B; TAF15 AND TAF15B.
RC STRAIN=cv. Columbia;
RX PubMed=17340043; DOI=10.1007/s11103-007-9135-1;
RA Lawit S.J., O'Grady K., Gurley W.B., Czarnecka-Verner E.;
RT "Yeast two-hybrid map of Arabidopsis TFIID.";
RL Plant Mol. Biol. 64:73-87(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ETHYLENE, SUBCELLULAR LOCATION,
RP SUBUNIT, AND INTERACTION WITH ERF1B; EIN3; PP2A1 AND PP2A5.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17526916; DOI=10.1093/jxb/erm080;
RA Robles L.M., Wampole J.S., Christians M.J., Larsen P.B.;
RT "Arabidopsis enhanced ethylene response 4 encodes an EIN3-interacting TFIID
RT transcription factor required for proper ethylene response, including ERF1
RT induction.";
RL J. Exp. Bot. 58:2627-2639(2007).
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. Probably involved in the negative regulation of
CC cytokinin sensitivity. {ECO:0000269|PubMed:17526916}.
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.
CC {ECO:0000269|PubMed:17340043, ECO:0000269|PubMed:17526916}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17526916}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, inflorescences
CC and flowers. {ECO:0000269|PubMed:15527982,
CC ECO:0000269|PubMed:17526916}.
CC -!- INDUCTION: Not up-regulated by ethylene. {ECO:0000269|PubMed:17526916}.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
CC -!- CAUTION: TAF12B in cv. Lansberg erecta (AC B2C6R6) is 2 amino acids
CC shorter and has been shown to be involved in the negative regulation of
CC cytokinin sensitivity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY463614; AAR28016.1; -; mRNA.
DR EMBL; AC007843; AAF97312.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29587.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29588.1; -; Genomic_DNA.
DR EMBL; AY056144; AAL07223.1; -; mRNA.
DR EMBL; AY091423; AAM14362.1; -; mRNA.
DR RefSeq; NP_564023.1; NM_101605.5.
DR RefSeq; NP_849680.1; NM_179349.1.
DR AlphaFoldDB; Q940A7; -.
DR SMR; Q940A7; -.
DR BioGRID; 23556; 14.
DR IntAct; Q940A7; 16.
DR STRING; 3702.AT1G17440.1; -.
DR iPTMnet; Q940A7; -.
DR PaxDb; Q940A7; -.
DR PRIDE; Q940A7; -.
DR ProteomicsDB; 232997; -.
DR EnsemblPlants; AT1G17440.1; AT1G17440.1; AT1G17440.
DR EnsemblPlants; AT1G17440.2; AT1G17440.2; AT1G17440.
DR GeneID; 838316; -.
DR Gramene; AT1G17440.1; AT1G17440.1; AT1G17440.
DR Gramene; AT1G17440.2; AT1G17440.2; AT1G17440.
DR KEGG; ath:AT1G17440; -.
DR Araport; AT1G17440; -.
DR TAIR; locus:2018861; AT1G17440.
DR eggNOG; KOG1142; Eukaryota.
DR HOGENOM; CLU_033120_1_0_1; -.
DR InParanoid; Q940A7; -.
DR OMA; GSQKSMN; -.
DR OrthoDB; 1227642at2759; -.
DR PhylomeDB; Q940A7; -.
DR PRO; PR:Q940A7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940A7; baseline and differential.
DR Genevisible; Q940A7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010104; P:regulation of ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
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; Initiation factor; Nucleus; Protein biosynthesis;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..683
FT /note="Transcription initiation factor TFIID subunit 12b"
FT /id="PRO_0000424051"
FT DOMAIN 525..598
FT /note="Histone-fold"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..683
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..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 74805 MW; CA53B057BE2D9EB8 CRC64;
MAEPIPSSSL SPKSLQSPNP MEPSPASSTP LPSSSSQQQQ LMTAPISNSV NSAASPAMTV
TTTEGIVIQN NSQPNISSPN PTSSNPPIGA QIPSPSPLSH PSSSLDQQTQ TQQLVQQTQQ
LPQQQQQIMQ QISSSPIPQL SPQQQQILQQ QHMTSQQIPM SSYQIAQSLQ RSPSLSRLSQ
IQQQQQQQHQ GQYGNVLRQQ AGLYGTMNFG GSGSVQQSQQ NQQMVNPNMS RAGLVGQSGH
LPMLNGAAGA AQMNIQPQLL AASPRQKSGM VQGSQFHPGS SGQQLQGMQA MGMMGSLNLT
SQMRGNPALY AQQRINPGQM RQQLSQQNAL TSPQVQNLQR TSSLAFMNPQ LSGLAQNGQA
GMMQNSLSQQ QWLKQMSGIT SPNSFRLQPS QRQALLLQQQ QQQQQQLSSP QLHQSSMSLN
QQQISQIIQQ QQQQSQLGQS QMNQSHSQQQ LQQMQQQLQQ QPQQQMQQQQ QQQQQMQINQ
QQPSPRMLSH AGQKSVSLTG SQPEATQSGT TTPGGSSSQG TEATNQLLGK RKIQDLVSQV
DVHAKLDPDV EDLLLEVADD FIDSVTSFAC SLAKHRKSSV LEPKDILLHL EKNLHLTIPG
FSSEDKRQTK TVPTDLHKKR LAMVRALLES SKPETNASNS KETMRQAMVN PNGPNHLLRP
SQSSEQLVSQ TSGPHILQHM TRY
