TAF9_DROME
ID TAF9_DROME Reviewed; 278 AA.
AC Q27272; Q95RJ4; Q9VX16;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcription initiation factor TFIID subunit 9;
DE AltName: Full=Protein enhancer of yellow 1;
DE AltName: Full=TAFII40;
DE AltName: Full=Transcription initiation factor TFIID 42 kDa subunit;
DE Short=TAFII-42;
DE AltName: Full=p42;
GN Name=e(y)1; Synonyms=TAF40; ORFNames=CG6474;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7545910; DOI=10.1038/367484a0;
RA Kokubo T., Gong D.-W., Wootton J.C., Horikoshi M., Roeder R.G.,
RA Nakatani Y.;
RT "Molecular cloning of Drosophila TFIID subunits.";
RL Nature 367:484-487(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=8221891; DOI=10.1016/0092-8674(93)90386-5;
RA Goodrich J.A., Hoey T., Thut C.J., Admon A., Tjian R.;
RT "Drosophila TAFII40 interacts with both a VP16 activation domain and the
RT basal transcription factor TFIIB.";
RL Cell 75:519-530(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-278.
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH E(Y)2, AND DOMAIN.
RX PubMed=11438676; DOI=10.1128/mcb.21.15.5223-5231.2001;
RA Georgieva S., Nabirochkina E., Dilworth F.J., Eickhoff H., Becker P.,
RA Tora L., Georgiev P., Soldatov A.;
RT "The novel transcription factor e(y)2 interacts with TAF(II)40 and
RT potentiates transcription activation on chromatin templates.";
RL Mol. Cell. Biol. 21:5223-5231(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-86, AND INTERACTION WITH TAF6.
RX PubMed=8598927; DOI=10.1038/380316a0;
RA Xie X., Kokubo T., Cohen S.L., Mirza U.A., Hoffmann A., Chait B.T.,
RA Roeder R.G., Nakatani Y., Burley S.K.;
RT "Structural similarity between TAFs and the heterotetrameric core of the
RT histone octamer.";
RL Nature 380:316-322(1996).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors. {ECO:0000269|PubMed:8221891}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). E(y)1 and
CC Taf6 exist as a heterotetramer. Interacts with e(y)2.
CC {ECO:0000269|PubMed:11438676, ECO:0000269|PubMed:8598927}.
CC -!- INTERACTION:
CC Q27272; P49847: Taf6; NbExp=2; IntAct=EBI-174260, EBI-136204;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The C-terminus is important for mediating interaction with
CC e(y)2. {ECO:0000269|PubMed:11438676}.
CC -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000305}.
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DR EMBL; U06458; AAC47347.1; -; mRNA.
DR EMBL; L29540; AAA28488.1; -; mRNA.
DR EMBL; AE014298; AAF48767.3; -; Genomic_DNA.
DR EMBL; AY061338; AAL28886.2; -; mRNA.
DR PIR; A49067; A49067.
DR RefSeq; NP_523391.3; NM_078667.4.
DR PDB; 1TAF; X-ray; 2.00 A; A=19-86.
DR PDBsum; 1TAF; -.
DR AlphaFoldDB; Q27272; -.
DR SMR; Q27272; -.
DR BioGRID; 59084; 41.
DR DIP; DIP-239N; -.
DR IntAct; Q27272; 14.
DR STRING; 7227.FBpp0074237; -.
DR PaxDb; Q27272; -.
DR PRIDE; Q27272; -.
DR EnsemblMetazoa; FBtr0074463; FBpp0074237; FBgn0000617.
DR GeneID; 32762; -.
DR KEGG; dme:Dmel_CG6474; -.
DR CTD; 32762; -.
DR FlyBase; FBgn0000617; e(y)1.
DR VEuPathDB; VectorBase:FBgn0000617; -.
DR eggNOG; KOG3334; Eukaryota.
DR GeneTree; ENSGT00940000169542; -.
DR HOGENOM; CLU_068315_2_0_1; -.
DR InParanoid; Q27272; -.
DR OMA; MLEFTFR; -.
DR OrthoDB; 1429345at2759; -.
DR PhylomeDB; Q27272; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; Q27272; -.
DR BioGRID-ORCS; 32762; 1 hit in 3 CRISPR screens.
DR EvolutionaryTrace; Q27272; -.
DR GenomeRNAi; 32762; -.
DR PRO; PR:Q27272; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000617; Expressed in secondary oocyte and 23 other tissues.
DR ExpressionAtlas; Q27272; baseline and differential.
DR Genevisible; Q27272; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR CDD; cd07979; TAF9; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003162; TFIID-31.
DR Pfam; PF02291; TFIID-31kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..278
FT /note="Transcription initiation factor TFIID subunit 9"
FT /id="PRO_0000118894"
FT REGION 193..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1TAF"
FT HELIX 40..66
FT /evidence="ECO:0007829|PDB:1TAF"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1TAF"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1TAF"
SQ SEQUENCE 278 AA; 29314 MW; 0EA442C80467001F CRC64;
MSAEKSDKAK ISAQIKHVPK DAQVIMSILK ELNVQEYEPR VVNQLLEFTF RYVTCILDDA
KVYANHARKK TIDLDDVRLA TEVTLDKSFT GPLERHVLAK VADVRNSMPL PPIKPHCGLR
LPPDRYCLTG VNYKLRATNQ PKKMTKSAVE GRPLKTVVKP VSSANGPKRP HSVVAKQQVV
TIPKPVIKFT TTTTTKTVGS SGGSGGGGGQ EVKSESTGAG GDLKMEVDSD AAAVGSIAGA
SGSGAGSASG GGGGGGSSGV GVAVKREREE EEFEFVTN
