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T2AG_DROME
ID   T2AG_DROME              Reviewed;         106 AA.
AC   P52656; B5RIE5; Q8MYY8; Q9VCG7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Transcription initiation factor IIA subunit 2;
DE   AltName: Full=General transcription factor IIA subunit 2;
DE   AltName: Full=TFIIA p14 subunit;
DE            Short=TFIIA-14;
DE   AltName: Full=Transcription initiation factor IIA gamma chain;
DE            Short=TFIIA-gamma;
DE   AltName: Full=dTFIIA-S;
GN   Name=TfIIA-S; ORFNames=CG5163;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 42-59, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=Oregon-R;
RX   PubMed=7958898; DOI=10.1101/gad.8.19.2313;
RA   Yokomori K., Zeidler M.P., Chen J.-L., Verrijzer C.P., Mlodzik M.,
RA   Tjian R.;
RT   "Drosophila TFIIA directs cooperative DNA binding with TBP and mediates
RT   transcriptional activation.";
RL   Genes Dev. 8:2313-2323(1994).
RN   [2]
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   [3]
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]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, INTERACTION WITH CG12721, AND DISRUPTION PHENOTYPE.
RX   PubMed=28847004; DOI=10.1038/nature23482;
RA   Andersen P.R., Tirian L., Vunjak M., Brennecke J.;
RT   "A heterochromatin-dependent transcription machinery drives piRNA
RT   expression.";
RL   Nature 549:54-59(2017).
CC   -!- FUNCTION: TFIIA is a component of the transcription machinery of RNA
CC       polymerase II and plays an important role in transcriptional activation
CC       (PubMed:7958898). TFIIA in a complex with TBP mediates transcriptional
CC       activity (PubMed:7958898). Part of a rhi-dependent transcription
CC       machinery that enables the generation of piRNA precursors from
CC       heterochromatin while maintaining the suppression of transposon-encoded
CC       promoters and enhancers (PubMed:28847004). Forms a complex with
CC       Moonshiner/CG12721 and Trf2 which recruit transcriptional machinery to
CC       heterochromatin to initiate the bidirectional transcription of piRNA
CC       clusters, by interacting with the RDC (rhi, del and cuff) complex that
CC       binds to repressive H3K9me3 marks in the chromatin (PubMed:28847004).
CC       This mechanism allows transcription to occur in piRNA clusters despite
CC       the lack of proper promoter elements and in the presence of the
CC       repressive H3K9me3 mark (PubMed:28847004).
CC       {ECO:0000269|PubMed:28847004, ECO:0000269|PubMed:7958898}.
CC   -!- SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1 and
CC       a small subunit gamma (PubMed:7958898). It was originally believed to
CC       be a heterotrimer of an alpha (p30), a beta (p20) and a gamma (p14)
CC       subunit (PubMed:7958898). Forms a complex with Moonshiner/CG12721 and
CC       Trf2 (PubMed:28847004). {ECO:0000269|PubMed:28847004,
CC       ECO:0000269|PubMed:7958898}.
CC   -!- INTERACTION:
CC       P52656; P52654: TfIIA-L; NbExp=3; IntAct=EBI-123680, EBI-132413;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DISRUPTION PHENOTYPE: Females are sterile.
CC       {ECO:0000269|PubMed:28847004}.
CC   -!- SIMILARITY: Belongs to the TFIIA subunit 2 family. {ECO:0000305}.
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DR   EMBL; X83271; CAA58244.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF56199.1; -; Genomic_DNA.
DR   EMBL; AY113478; AAM29483.1; -; mRNA.
DR   EMBL; BT044069; ACH92134.1; -; mRNA.
DR   PIR; A54883; A55121.
DR   RefSeq; NP_524467.1; NM_079743.4.
DR   AlphaFoldDB; P52656; -.
DR   SMR; P52656; -.
DR   BioGRID; 67758; 11.
DR   DIP; DIP-23236N; -.
DR   IntAct; P52656; 1.
DR   STRING; 7227.FBpp0083912; -.
DR   PaxDb; P52656; -.
DR   DNASU; 42822; -.
DR   EnsemblMetazoa; FBtr0084526; FBpp0083912; FBgn0013347.
DR   GeneID; 42822; -.
DR   KEGG; dme:Dmel_CG5163; -.
DR   UCSC; CG5163-RA; d. melanogaster.
DR   CTD; 42822; -.
DR   FlyBase; FBgn0013347; TfIIA-S.
DR   VEuPathDB; VectorBase:FBgn0013347; -.
DR   eggNOG; KOG3463; Eukaryota.
DR   GeneTree; ENSGT00390000014572; -.
DR   HOGENOM; CLU_112964_2_1_1; -.
DR   OMA; FREVHEI; -.
DR   OrthoDB; 1589933at2759; -.
DR   PhylomeDB; P52656; -.
DR   Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
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   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   SignaLink; P52656; -.
DR   BioGRID-ORCS; 42822; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 42822; -.
DR   PRO; PR:P52656; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0013347; Expressed in oviduct (Drosophila) and 43 other tissues.
DR   ExpressionAtlas; P52656; baseline and differential.
DR   Genevisible; P52656; DM.
DR   GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005672; C:transcription factor TFIIA complex; IDA:FlyBase.
DR   GO; GO:0017025; F:TBP-class protein binding; IPI: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; cd10014; TFIIA_gamma_C; 1.
DR   CDD; cd10145; TFIIA_gamma_N; 1.
DR   Gene3D; 1.10.287.190; -; 1.
DR   Gene3D; 2.30.18.10; -; 1.
DR   InterPro; IPR009083; TFIIA_a-hlx.
DR   InterPro; IPR009088; TFIIA_b-brl.
DR   InterPro; IPR003194; TFIIA_gsu.
DR   InterPro; IPR015871; TFIIA_gsu_C.
DR   InterPro; IPR015872; TFIIA_gsu_N.
DR   PANTHER; PTHR10966; PTHR10966; 1.
DR   Pfam; PF02751; TFIIA_gamma_C; 1.
DR   Pfam; PF02268; TFIIA_gamma_N; 1.
DR   PIRSF; PIRSF009415; Hum_TFIIA_gamma; 1.
DR   SUPFAM; SSF50784; SSF50784; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..106
FT                   /note="Transcription initiation factor IIA subunit 2"
FT                   /id="PRO_0000194048"
FT   CONFLICT        40
FT                   /note="F -> L (in Ref. 4; AAM29483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   106 AA;  12193 MW;  978556B6AA8B31CA CRC64;
     MSYQLYRNTT LGNTLQESLD ELIQYGQITP GLAFKVLLQF DKSINNALNQ RVKARVTFKA
     GKLNTYRFCD NVWTLMLNDV EFREVHEIVK VDKVKIVACD GKSGEF
 
 
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