TAF8_DROME
ID TAF8_DROME Reviewed; 328 AA.
AC Q9VWY6; O18398; Q8SYE2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transcription initiation factor TFIID subunit 8;
DE AltName: Full=Protein prodos;
GN Name=Taf8 {ECO:0000312|EMBL:AAF48800.1};
GN Synonyms=pds {ECO:0000303|PubMed:11134347},
GN prod {ECO:0000312|EMBL:CAA75667.1}; ORFNames=CG7128;
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] {ECO:0000312|EMBL:CAA75667.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S {ECO:0000312|EMBL:CAA75667.1};
RA Ortuno-Sahagun D.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAF48800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF48800.1}
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 [4] {ECO:0000312|EMBL:AAL49226.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL49226.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TAF10B.
RX PubMed=11134347; DOI=10.1128/mcb.21.2.614-623.2001;
RA Hernandez-Hernandez A., Ferrus A.;
RT "Prodos is a conserved transcriptional regulator that interacts with
RT dTAF(II)16 in Drosophila melanogaster.";
RL Mol. Cell. Biol. 21:614-623(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-245 AND SER-255, AND
RP 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: 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:11134347}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). Histone
CC fold interacts with N-terminus of Taf10b.
CC {ECO:0000269|PubMed:11134347}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF8 family. {ECO:0000255}.
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DR EMBL; Y15513; CAA75667.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48800.1; -; Genomic_DNA.
DR EMBL; AY071604; AAL49226.1; -; mRNA.
DR RefSeq; NP_523397.1; NM_078673.4.
DR AlphaFoldDB; Q9VWY6; -.
DR SMR; Q9VWY6; -.
DR BioGRID; 59112; 8.
DR IntAct; Q9VWY6; 6.
DR STRING; 7227.FBpp0074288; -.
DR iPTMnet; Q9VWY6; -.
DR PaxDb; Q9VWY6; -.
DR DNASU; 32792; -.
DR EnsemblMetazoa; FBtr0074514; FBpp0074288; FBgn0022724.
DR GeneID; 32792; -.
DR KEGG; dme:Dmel_CG7128; -.
DR CTD; 129685; -.
DR FlyBase; FBgn0022724; Taf8.
DR VEuPathDB; VectorBase:FBgn0022724; -.
DR eggNOG; KOG4336; Eukaryota.
DR GeneTree; ENSGT00390000017567; -.
DR HOGENOM; CLU_070829_0_0_1; -.
DR InParanoid; Q9VWY6; -.
DR OMA; SAHNYCE; -.
DR OrthoDB; 1290064at2759; -.
DR PhylomeDB; Q9VWY6; -.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 32792; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 32792; -.
DR PRO; PR:Q9VWY6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0022724; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; Q9VWY6; baseline and differential.
DR Genevisible; Q9VWY6; DM.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
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; PTHR46469; PTHR46469; 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 Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..328
FT /note="Transcription initiation factor TFIID subunit 8"
FT /id="PRO_0000118886"
FT DOMAIN 16..83
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 229..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 164
FT /note="Q -> H (in Ref. 1; CAA75667)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="M -> I (in Ref. 4; AAL49226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 36649 MW; A3CD62A4BC2EDC7C CRC64;
MEKVEAVTVS NVDPYRRILN KVVSQLLLDK GAGQASNHSL ETLTQMLQAL IWEIGNSAHN
YCELSGRTMP TVGDVSLALI NMGISISNLD PYMRKETHVP IPLPPQQTQQ RPLSLLQAGI
KAPHPHYVPS YFPPMPDPHA YIRTPTHKQP VTEYEAIREK AACQKRDIEK ALTKFLCKTT
ETNNLFPTED NMFPLIACKP AFPPYAAALN PTDQVFDFEE LEYHYLVANR TEDEPSKDDG
EEGDSENEEM DGDKSKEEKP ELDIKPNSNT NKAILENPNI DNPYLRAATL PKRSKNCPTP
GTMPSRSLAT TAPTIRTPST LEITKTNL
