TAF4_DROME
ID TAF4_DROME Reviewed; 921 AA.
AC P47825; P49845; Q0E8E3; Q1LZ31; Q8T9E0; Q9VUY7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Transcription initiation factor TFIID subunit 4;
DE AltName: Full=110 kDa TBP-associated factor;
DE AltName: Full=Transcription initiation factor TFIID 110 kDa subunit;
DE Short=TAFII-110;
DE Short=p110;
GN Name=Taf4; Synonyms=TAF110; ORFNames=CG5444;
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] (ISOFORM A), AND PROTEIN SEQUENCE OF 519-540;
RP 597-616 AND 857-874.
RC TISSUE=Embryo;
RX PubMed=7678780; DOI=10.1016/0092-8674(93)90664-c;
RA Hoey T., Weinzierl R.O.J., Gill G., Chen J.-L., Dynlacht B.D., Tjian R.;
RT "Molecular cloning and functional analysis of Drosophila TAF110 reveal
RT properties expected of coactivators.";
RL Cell 72:247-260(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 398-406;
RP 520-540 AND 860-877, AND INTERACTION WITH TAF1.
RC TISSUE=Embryo;
RX PubMed=8327460; DOI=10.1073/pnas.90.13.5896;
RA Kokubo T., Gong D.-W., Roeder R.G., Horikoshi M., Nakatani Y.;
RT "The Drosophila 110-kDa transcription factor TFIID subunit directly
RT interacts with the N-terminal region of the 230-kDa subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5896-5900(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, AND ALTERNATIVE SPLICING.
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] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH TFIIA-L.
RC TISSUE=Embryo;
RX PubMed=8224849; DOI=10.1101/gad.7.11.2235;
RA Yokomori K., Admon A., Goodrich J.A., Chen J.-L., Tjian R.;
RT "Drosophila TFIIA-L is processed into two subunits that are associated with
RT the TBP/TAF complex.";
RL Genes Dev. 7:2235-2245(1993).
RN [8]
RP INTERACTION WITH TAF11 AND TAF12.
RX PubMed=8276241; DOI=10.1101/gad.7.12b.2587;
RA Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.;
RT "Molecular cloning and characterization of dTAFII30 alpha and dTAFII30
RT beta: two small subunits of Drosophila TFIID.";
RL Genes Dev. 7:2587-2597(1993).
RN [9]
RP INTERACTION WITH TAF5.
RC TISSUE=Embryo;
RX PubMed=8247000; DOI=10.1128/mcb.13.12.7859-7863.1993;
RA Kokubo T., Gong D.-W., Yamashita S., Takada R., Roeder R.G., Horikoshi M.,
RA Nakatani Y.;
RT "Molecular cloning, expression, and characterization of the Drosophila 85-
RT kilodalton TFIID subunit.";
RL Mol. Cell. Biol. 13:7859-7863(1993).
RN [10]
RP INTERACTION WITH TAF1.
RX PubMed=8464492; DOI=10.1038/362511a0;
RA Weinzierl R.O., Dynlacht B.D., Tjian R.;
RT "Largest subunit of Drosophila transcription factor IID directs assembly of
RT a complex containing TBP and a coactivator.";
RL Nature 362:511-517(1993).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors. May function as a coactivator by serving as a site of
CC protein-protein contact between activators like Sp1 (or btd) and TFIID
CC complex. {ECO:0000269|PubMed:8224849}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). Interacts
CC with TFIIA-L when in complex with Tbp. Interacts with Taf1, Taf5, Taf11
CC and Taf12. {ECO:0000269|PubMed:8224849, ECO:0000269|PubMed:8247000,
CC ECO:0000269|PubMed:8276241, ECO:0000269|PubMed:8327460,
CC ECO:0000269|PubMed:8464492}.
CC -!- INTERACTION:
CC P47825; Q9V9W8: pygo; NbExp=2; IntAct=EBI-277958, EBI-152653;
CC P47825; P51123: Taf1; NbExp=7; IntAct=EBI-277958, EBI-499582;
CC P47825; P03255; Xeno; NbExp=3; IntAct=EBI-277958, EBI-2603114;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=B;
CC IsoId=P47825-1; Sequence=Displayed;
CC Name=C; Synonyms=D;
CC IsoId=P47825-2; Sequence=VSP_004441;
CC -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L06861; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S63550; AAB27433.1; -; mRNA.
DR EMBL; AE014296; AAF49535.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41248.1; -; Genomic_DNA.
DR EMBL; AY069807; AAL39952.1; -; mRNA.
DR EMBL; BT025195; ABF17886.2; -; mRNA.
DR PIR; A48184; A48184.
DR RefSeq; NP_001163453.1; NM_001169982.2. [P47825-1]
DR RefSeq; NP_001287077.1; NM_001300148.1. [P47825-1]
DR RefSeq; NP_524102.1; NM_079378.4. [P47825-1]
DR RefSeq; NP_730109.1; NM_168651.3. [P47825-1]
DR RefSeq; NP_788511.1; NM_176333.3. [P47825-2]
DR RefSeq; NP_996101.1; NM_206379.3. [P47825-2]
DR AlphaFoldDB; P47825; -.
DR SMR; P47825; -.
DR BioGRID; 65074; 33.
DR DIP; DIP-237N; -.
DR IntAct; P47825; 16.
DR MINT; P47825; -.
DR PaxDb; P47825; -.
DR PRIDE; P47825; -.
DR DNASU; 39765; -.
DR EnsemblMetazoa; FBtr0075448; FBpp0075205; FBgn0010280. [P47825-1]
DR EnsemblMetazoa; FBtr0075449; FBpp0075206; FBgn0010280. [P47825-1]
DR EnsemblMetazoa; FBtr0075450; FBpp0075207; FBgn0010280. [P47825-2]
DR EnsemblMetazoa; FBtr0075451; FBpp0089259; FBgn0010280. [P47825-2]
DR EnsemblMetazoa; FBtr0301911; FBpp0291125; FBgn0010280. [P47825-1]
DR EnsemblMetazoa; FBtr0345951; FBpp0311865; FBgn0010280. [P47825-1]
DR GeneID; 39765; -.
DR KEGG; dme:Dmel_CG5444; -.
DR CTD; 6874; -.
DR FlyBase; FBgn0010280; Taf4.
DR VEuPathDB; VectorBase:FBgn0010280; -.
DR eggNOG; KOG2341; Eukaryota.
DR GeneTree; ENSGT00390000011620; -.
DR InParanoid; P47825; -.
DR PhylomeDB; P47825; -.
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-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; P47825; -.
DR BioGRID-ORCS; 39765; 2 hits in 3 CRISPR screens.
DR ChiTaRS; Taf4; fly.
DR GenomeRNAi; 39765; -.
DR PRO; PR:P47825; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010280; Expressed in wing disc and 28 other tissues.
DR ExpressionAtlas; P47825; baseline and differential.
DR Genevisible; P47825; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0001092; F:TFIIA-class transcription factor complex binding; IPI:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IPI:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:FlyBase.
DR CDD; cd08045; TAF4; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.20.120.1110; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR045144; TAF4.
DR InterPro; IPR007900; TAF4_C.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR PANTHER; PTHR15138; PTHR15138; 1.
DR Pfam; PF05236; TAF4; 1.
DR Pfam; PF07531; TAFH; 1.
DR SMART; SM00549; TAFH; 1.
DR SUPFAM; SSF158553; SSF158553; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS51119; TAFH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..921
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000118870"
FT DOMAIN 290..386
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT REGION 66..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 138..207
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.6"
FT /id="VSP_004441"
FT CONFLICT 114
FT /note="V -> M (in Ref. 5; AAL39952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 99338 MW; 27E6852859872767 CRC64;
MNTSQTAAGN RITFTSQPLP NGTISIAGNP GAVISTAQLP NTTTIKTIQA GIGGQHQGLQ
QVHHVQQQQQ SQQQQQQQQQ TQSAGQPLLN SMLPAGVVVG MRQQAPSQQQ QKNVPTNPLS
RVVINSHMAG VRPQSPSITL STLNTGQTPA LLVKTDNGFQ LLRVGTTTGP PTVTQTITNT
SNNSNTTSTT NHPTTTQIRL QTVPAAASMT NTTATSNIIV NSVASSGYAN SSQPPHLTQL
NAQAPQLPQI TQIQTIPAQQ SQQQQVNNVS SAGGTATAVS STTAATTTQQ GNTKEKCRKF
LANLIELSTR EPKPVEKNVR TLIQELVNAN VEPEEFCDRL ERLLNASPQP CLIGFLKKSL
PLLRQALYTK ELVIEGIKPP PQHVLGLAGL SQQLPKIQAQ IRPIGPSQTT TIGQTQVRMI
TPNALGTPRP TIGHTTISKQ PPNIRLPTAP RLVNTGGIRT QIPSLQVPGQ ANIVQIRGPQ
HAQLQRTGSV QIRATTRPPN SVPTANKLTA VKVGQTQIKA ITPSLHPPSL AAISGGPPPT
PTLSVLSTLN SASTTTLPIP SLPTVHLPPE ALRAREQMQN SLNHNSNHFD AKLVEIKAPS
LHPPHMERIN ASLTPIGAKT MARPPPAINK AIGKKKRDAM EMDAKLNTSS GGAASAANSF
FQQSSMSSMY GDDDINDVAA MGGVNLAEES QRILGCTENI GTQIRSCKDE VFLNLPSLQA
RIRAITSEAG LDEPSQDVAV LISHACQERL KNIVEKLAVI AEHRIDVIKL DPRYEPAKDV
RGQIKFLEEL DKAEQKRHEE LEREMLLRAA KSRSRVEDPE QAKMKARAKE MQRAEMEELR
QRDANLTALQ AIGPRKKLKL DGETVSSGAG SSGGGVLSSS GSAPTTLRPR IKRVNLRDML
FYMEQEREFC RSSMLFKTYL K
