TAF8_ARATH
ID TAF8_ARATH Reviewed; 353 AA.
AC Q9SYZ9; Q8LFR3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Transcription initiation factor TFIID subunit 8;
DE AltName: Full=TBP-associated factor 8;
DE Short=AtTAF8;
GN Name=TAF8; OrderedLocusNames=At4g34340;
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 TAF4B; TAF5;
RP TAF10; TAF12; TAF12B; TAF13 AND TAF14.
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=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: TAFs are components of the transcription factor IID (TFIID)
CC complex that is essential for mediating regulation of RNA polymerase
CC transcription. {ECO:0000250}.
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 TAF4B, TAF5, TAF10, TAF12, TAF12B, TAF13 and TAF14.
CC {ECO:0000269|PubMed:17340043}.
CC -!- INTERACTION:
CC Q9SYZ9; O04173: TAF10; NbExp=3; IntAct=EBI-1247615, EBI-1247479;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and inflorescences.
CC {ECO:0000269|PubMed:15527982}.
CC -!- SIMILARITY: Belongs to the TAF8 family. {ECO:0000305}.
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DR EMBL; AY463623; AAR28025.1; -; mRNA.
DR EMBL; AL035521; CAB36711.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80151.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86361.1; -; Genomic_DNA.
DR EMBL; AF360178; AAK25888.1; -; mRNA.
DR EMBL; AY039994; AAK64071.1; -; mRNA.
DR EMBL; AY084690; AAM61252.1; -; mRNA.
DR PIR; T04780; T04780.
DR RefSeq; NP_567964.1; NM_119599.1.
DR AlphaFoldDB; Q9SYZ9; -.
DR SMR; Q9SYZ9; -.
DR BioGRID; 14866; 8.
DR IntAct; Q9SYZ9; 8.
DR STRING; 3702.AT4G34340.1; -.
DR iPTMnet; Q9SYZ9; -.
DR PaxDb; Q9SYZ9; -.
DR PRIDE; Q9SYZ9; -.
DR ProteomicsDB; 234134; -.
DR EnsemblPlants; AT4G34340.1; AT4G34340.1; AT4G34340.
DR GeneID; 829584; -.
DR Gramene; AT4G34340.1; AT4G34340.1; AT4G34340.
DR KEGG; ath:AT4G34340; -.
DR Araport; AT4G34340; -.
DR TAIR; locus:2116149; AT4G34340.
DR eggNOG; KOG2389; Eukaryota.
DR HOGENOM; CLU_046212_1_0_1; -.
DR InParanoid; Q9SYZ9; -.
DR OMA; MKTGPSN; -.
DR OrthoDB; 1290064at2759; -.
DR PhylomeDB; Q9SYZ9; -.
DR PRO; PR:Q9SYZ9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SYZ9; baseline and differential.
DR Genevisible; Q9SYZ9; AT.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR CDD; cd08049; TAF8; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037818; TAF8.
DR InterPro; IPR019473; TFIID_su8_C.
DR PANTHER; PTHR46338; PTHR46338; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF10406; TAF8_C; 1.
DR SMART; SM00576; BTP; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..353
FT /note="Transcription initiation factor TFIID subunit 8"
FT /id="PRO_0000424045"
FT DOMAIN 30..103
FT /note="Histone-fold"
FT CONFLICT 129..131
FT /note="VPF -> IPS (in Ref. 6; AAM61252)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="M -> K (in Ref. 6; AAM61252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39546 MW; 261DCC7FD867C733 CRC64;
MNTERAQEGD RNDAASSSGC SESYEFSHAA AKAAVAQVCE SVGYENFKDP ALESLSGFAL
QYILQLGKTA TSFANLTGRS QCNVFDIILA LDDLTDNNGE QGISSESCSL GRSIKLREII
DFVNSSEEVP FSQPLPSFPV AISDRSRKMI PSFVEIGETP PGKHIPLWLP AFPDPHTYKE
TPMWIERVSD PRGDKIEQAR QRRKAERALL SLQRKLVCKI SSRNPVWGDM DGVKEEMRDD
ESELRSVSSG EKVESLNRDG LSVIEAFAPA MEAARDGFSS EAHTEWKKNK PVALSKLRTE
KKFLGQPLDL SLQMKGEDRP ISFVREEDRD DKRRRAEFIL RQCMENPVDL NQL
