T2FA_DROME
ID T2FA_DROME Reviewed; 577 AA.
AC Q05913; Q9VI19;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=General transcription factor IIF subunit 1;
DE AltName: Full=Transcription factor 5 large chain;
DE Short=TF5A;
DE AltName: Full=Transcription initiation factor IIF subunit alpha;
DE Short=TFIIF-alpha;
GN Name=TfIIFalpha {ECO:0000303|PubMed:8464745,
GN ECO:0000312|FlyBase:FBgn0010282};
GN ORFNames=CG10281 {ECO:0000312|FlyBase:FBgn0010282};
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=8464745; DOI=10.1093/nar/21.6.1492;
RA Gong D.-W., Horikoshi M., Nakatani Y.;
RT "Analysis of cDNA encoding Drosophila transcription initiation factor TFIIF
RT alpha (RAP74).";
RL Nucleic Acids Res. 21:1492-1492(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8464716; DOI=10.1093/nar/21.5.1319;
RA Kephart D., Price M.P., Burton Z.F., Finkelstein A., Greenblalt J.,
RA Price D.H.;
RT "Cloning of a Drosophila cDNA with sequence similarity to human
RT transcription factor RAP74.";
RL Nucleic Acids Res. 21:1319-1319(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].
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 FUNCTION.
RX PubMed=8175788; DOI=10.1016/s0021-9258(17)36864-3;
RA Kephart D., Wang B.Q., Burton Z.F., Price D.H.;
RT "Functional analysis of Drosophila factor 5 (TFIIF), a general
RT transcription factor.";
RL J. Biol. Chem. 269:13536-13543(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-246; SER-250;
RP SER-252; THR-341; SER-342; SER-352; SER-355; SER-453; SER-455; THR-457;
RP SER-482; SER-484 AND THR-488, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC to RNA polymerase II and helps to recruit it to the initiation complex
CC in collaboration with TFIIB. It promotes transcription elongation.
CC {ECO:0000269|PubMed:8175788}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000250|UniProtKB:P35269}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:8175788}.
CC -!- PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase
CC II-like kinases. {ECO:0000250|UniProtKB:P35269}.
CC -!- SIMILARITY: Belongs to the TFIIF alpha subunit family. {ECO:0000305}.
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DR EMBL; L10331; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X66982; CAA47391.1; -; mRNA.
DR EMBL; AE014297; AAF54125.1; -; Genomic_DNA.
DR EMBL; AY051733; AAK93157.1; -; mRNA.
DR PIR; S30237; S30237.
DR RefSeq; NP_524246.1; NM_079522.4.
DR AlphaFoldDB; Q05913; -.
DR SMR; Q05913; -.
DR BioGRID; 65991; 6.
DR DIP; DIP-17887N; -.
DR IntAct; Q05913; 5.
DR STRING; 7227.FBpp0081216; -.
DR iPTMnet; Q05913; -.
DR PaxDb; Q05913; -.
DR PRIDE; Q05913; -.
DR DNASU; 40790; -.
DR EnsemblMetazoa; FBtr0081719; FBpp0081216; FBgn0010282.
DR GeneID; 40790; -.
DR KEGG; dme:Dmel_CG10281; -.
DR CTD; 40790; -.
DR FlyBase; FBgn0010282; TfIIFalpha.
DR VEuPathDB; VectorBase:FBgn0010282; -.
DR eggNOG; KOG2393; Eukaryota.
DR GeneTree; ENSGT00440000038032; -.
DR HOGENOM; CLU_027572_2_0_1; -.
DR InParanoid; Q05913; -.
DR OMA; NNMKEFR; -.
DR OrthoDB; 893557at2759; -.
DR PhylomeDB; Q05913; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DME-6803529; FGFR2 alternative splicing.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-72086; mRNA Capping.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA.
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-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-DME-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q05913; -.
DR BioGRID-ORCS; 40790; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40790; -.
DR PRO; PR:Q05913; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010282; Expressed in anlage and 56 other tissues.
DR Genevisible; Q05913; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005674; C:transcription factor TFIIF complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001096; F:TFIIF-class transcription factor complex binding; IPI:FlyBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR008851; TFIIF-alpha.
DR InterPro; IPR011039; TFIIF_interaction.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13011; PTHR13011; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50916; SSF50916; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..577
FT /note="General transcription factor IIF subunit 1"
FT /id="PRO_0000211233"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 20
FT /note="A -> R (in Ref. 1; L10331)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> G (in Ref. 1; L10331)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="P -> A (in Ref. 1; L10331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 64467 MW; 1E3DF88E3C833761 CRC64;
MSSASKSTPS AASGSSTSAA AAAAASVASG SASSSANVQE FKIRVPKMPK KHHVMRFNAT
LNVDFAQWRN VKLERENNMK EFRGMEEDQP KFGAGSEYNR DQREEARRKK FGIIARKYRP
EAQPWILKVG GKTGKKFKGI REGGVGENAA FYVFTHAPDG AIEAYPLTEW YNFQPIQRYK
SLSAEEAEQE FGRRKKVMNY FSLMLRKRLR GDEEEEQDPE EAKLIKAATK KSKELKITDM
DEWIDSEDES DSEDEEDKKK KEQEDSDDGK AKGKGKKGAD KKKKKRDVDD EAFEESDDGD
EEGREMDYDT SSSEDEPDPE AKVDKDMKGV AEEDALRKLL TSDEEEDDEK KSDESDKEDA
DGEKKKKDKG KDEVSKDKKK KKPTKDDKKG KSNGSGDSST DFSSDSTDSE DDLSNGPPKK
KVVVKDKDKE KEKEKESAAS SKVIASSSNA NKSRSATPTL STDASKRKMN SLPSDLTASD
TSNSPTSTPA KRPKNEISTS LPTSFSGGKV EDYGITEEAV RRYLKRKPLT ATELLTKFKN
KKTPVSSDRL VETMTKILKK INPVKHTIQG KMYLWIK
