T2AG_ARATH
ID T2AG_ARATH Reviewed; 106 AA.
AC Q39236; O49348;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Transcription initiation factor IIA subunit 2;
DE AltName: Full=General transcription factor IIA subunit 2;
DE AltName: Full=Transcription initiation factor IIA gamma chain;
DE Short=TFIIA-gamma;
GN Name=TFIIA-S; OrderedLocusNames=At4g24440; ORFNames=T22A6.270;
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;
RA Schwechheimer C.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10092179; DOI=10.1023/a:1006139724849;
RA Li Y.F., Le Gourierrec J., Torki M., Kim Y.J., Guerineau F., Zhou D.X.;
RT "Characterization and functional analysis of Arabidopsis TFIIA reveal that
RT the evolutionarily unconserved region of the large subunit has a
RT transcription activation domain.";
RL Plant Mol. Biol. 39:515-525(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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.
CC -!- FUNCTION: TFIIA is a component of the transcription machinery of RNA
CC polymerase II and plays an important role in transcriptional
CC activation. TFIIA in a complex with TBP mediates transcriptional
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1 and
CC a small subunit gamma. It was originally believed to be a heterotrimer
CC of an alpha, a beta and a gamma subunit (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIA subunit 2 family. {ECO:0000305}.
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DR EMBL; X98862; CAA67369.1; -; mRNA.
DR EMBL; AJ223634; CAA11524.1; -; mRNA.
DR EMBL; AL078637; CAB45079.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79354.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84904.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84905.1; -; Genomic_DNA.
DR EMBL; AY072192; AAL60014.1; -; mRNA.
DR EMBL; AY096423; AAM20063.1; -; mRNA.
DR EMBL; AY085740; AAM62958.1; -; mRNA.
DR PIR; T09907; T09907.
DR RefSeq; NP_194175.1; NM_118577.5.
DR RefSeq; NP_849434.1; NM_179103.3.
DR AlphaFoldDB; Q39236; -.
DR SMR; Q39236; -.
DR BioGRID; 13835; 1.
DR IntAct; Q39236; 1.
DR STRING; 3702.AT4G24440.1; -.
DR iPTMnet; Q39236; -.
DR PaxDb; Q39236; -.
DR PRIDE; Q39236; -.
DR ProteomicsDB; 245274; -.
DR EnsemblPlants; AT4G24440.1; AT4G24440.1; AT4G24440.
DR EnsemblPlants; AT4G24440.2; AT4G24440.2; AT4G24440.
DR GeneID; 828546; -.
DR Gramene; AT4G24440.1; AT4G24440.1; AT4G24440.
DR Gramene; AT4G24440.2; AT4G24440.2; AT4G24440.
DR KEGG; ath:AT4G24440; -.
DR Araport; AT4G24440; -.
DR TAIR; locus:2136017; AT4G24440.
DR eggNOG; KOG3463; Eukaryota.
DR HOGENOM; CLU_112964_3_1_1; -.
DR InParanoid; Q39236; -.
DR OMA; QYYELYR; -.
DR OrthoDB; 1589933at2759; -.
DR PhylomeDB; Q39236; -.
DR PRO; PR:Q39236; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39236; baseline and differential.
DR Genevisible; Q39236; AT.
DR GO; GO:0005672; C:transcription factor TFIIA complex; IBA:GO_Central.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR CDD; cd10014; TFIIA_gamma_C; 1.
DR CDD; cd10145; TFIIA_gamma_N; 1.
DR Gene3D; 1.10.287.190; -; 1.
DR Gene3D; 2.30.18.10; -; 1.
DR InterPro; IPR009083; TFIIA_a-hlx.
DR InterPro; IPR009088; TFIIA_b-brl.
DR InterPro; IPR003194; TFIIA_gsu.
DR InterPro; IPR015871; TFIIA_gsu_C.
DR InterPro; IPR015872; TFIIA_gsu_N.
DR PANTHER; PTHR10966; PTHR10966; 1.
DR Pfam; PF02751; TFIIA_gamma_C; 1.
DR Pfam; PF02268; TFIIA_gamma_N; 1.
DR PIRSF; PIRSF009415; Hum_TFIIA_gamma; 1.
DR SUPFAM; SSF50784; SSF50784; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..106
FT /note="Transcription initiation factor IIA subunit 2"
FT /id="PRO_0000194050"
FT CONFLICT 29
FT /note="L -> V (in Ref. 1; CAA67369)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..69
FT /note="TYRFC -> HLQVR (in Ref. 1; CAA67369)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="D -> Y (in Ref. 1; CAA67369)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="R -> P (in Ref. 1; CAA67369)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="C -> S (in Ref. 1; CAA67369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 12140 MW; FB466F2E1EC68534 CRC64;
MATFELYRRS TIGMCLTETL DEMVQSGTLS PELAIQVLVQ FDKSMTEALE SQVKTKVSIK
GHLHTYRFCD NVWTFILQDA MFKSDDRQEN VSRVKIVACD SKLLTQ
