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TF2AA_DROME
ID   TF2AA_DROME             Reviewed;         366 AA.
AC   P52654; Q8IMN7; Q8IMN8; Q95RK0; Q9VB56;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Transcription initiation factor IIA subunit 1;
DE   AltName: Full=General transcription factor IIA subunit 1;
DE   AltName: Full=dTFIIA-L;
DE   Contains:
DE     RecName: Full=Transcription initiation factor IIA alpha chain;
DE     AltName: Full=TFIIA p30 subunit;
DE   Contains:
DE     RecName: Full=Transcription initiation factor IIA beta chain;
DE     AltName: Full=TFIIA p20 subunit;
GN   Name=TfIIA-L; ORFNames=CG5930;
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), PARTIAL PROTEIN SEQUENCE,
RP   INTERACTION WITH TBP AND TAF4, AND CLEAVAGE.
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   [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, 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   [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).
CC   -!- FUNCTION: TFIIA is a component of the transcription machinery of RNA
CC       polymerase II and plays an important role in transcriptional
CC       activation. TFIIA in a complex with TBP mediates transcriptional
CC       activity.
CC   -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC       protein (Tbp) and a number of TBP-associated factors (Tafs). TFIIA is a
CC       heterodimer of a unprocessed large subunit 1 and a small subunit gamma.
CC       It was originally believed to be a heterotrimer of an alpha (p30), a
CC       beta (p20) and a gamma subunit (p14). Interacts with Tbp. Taf4
CC       interacts with TFIIA-L when TFIIA-L is in complex with Tbp.
CC       {ECO:0000269|PubMed:8224849}.
CC   -!- INTERACTION:
CC       P52654; P52656: TfIIA-S; NbExp=3; IntAct=EBI-132413, EBI-123680;
CC       P52654; Q9W5B9: TfIIA-S-2; NbExp=5; IntAct=EBI-132413, EBI-181168;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=P52654-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P52654-2; Sequence=VSP_014785;
CC       Name=C;
CC         IsoId=P52654-3; Sequence=VSP_014784, VSP_014785;
CC   -!- PTM: The precursor form (48 kDa) is cleaved to give rise to the alpha
CC       (30 kDa) and beta (20 kDa) subunits. {ECO:0000269|PubMed:8224849}.
CC   -!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
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DR   EMBL; S66759; AAB28821.1; -; mRNA.
DR   EMBL; AE014297; AAF56687.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14105.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14106.1; -; Genomic_DNA.
DR   EMBL; AY061325; AAL28873.1; -; mRNA.
DR   PIR; A49076; A49076.
DR   RefSeq; NP_476995.1; NM_057647.4. [P52654-1]
DR   RefSeq; NP_476996.1; NM_057648.4. [P52654-2]
DR   RefSeq; NP_733208.1; NM_170329.2. [P52654-3]
DR   AlphaFoldDB; P52654; -.
DR   SMR; P52654; -.
DR   BioGRID; 68171; 26.
DR   IntAct; P52654; 17.
DR   STRING; 7227.FBpp0084525; -.
DR   PaxDb; P52654; -.
DR   DNASU; 43284; -.
DR   EnsemblMetazoa; FBtr0085154; FBpp0084524; FBgn0011289. [P52654-3]
DR   EnsemblMetazoa; FBtr0085155; FBpp0084525; FBgn0011289. [P52654-1]
DR   EnsemblMetazoa; FBtr0085156; FBpp0084526; FBgn0011289. [P52654-2]
DR   GeneID; 43284; -.
DR   KEGG; dme:Dmel_CG5930; -.
DR   CTD; 43284; -.
DR   FlyBase; FBgn0011289; TfIIA-L.
DR   VEuPathDB; VectorBase:FBgn0011289; -.
DR   eggNOG; KOG2652; Eukaryota.
DR   GeneTree; ENSGT00940000169791; -.
DR   InParanoid; P52654; -.
DR   OMA; EVCDASQ; -.
DR   PhylomeDB; P52654; -.
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   BioGRID-ORCS; 43284; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; TfIIA-L; fly.
DR   GenomeRNAi; 43284; -.
DR   PRO; PR:P52654; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0011289; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR   ExpressionAtlas; P52654; baseline and differential.
DR   Genevisible; P52654; DM.
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:0001094; F:TFIID-class transcription factor complex binding; IPI:FlyBase.
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   Gene3D; 2.30.18.10; -; 1.
DR   InterPro; IPR004855; TFIIA_asu/bsu.
DR   InterPro; IPR009088; TFIIA_b-brl.
DR   PANTHER; PTHR12694; PTHR12694; 1.
DR   Pfam; PF03153; TFIIA; 2.
DR   SMART; SM01371; TFIIA; 1.
DR   SUPFAM; SSF50784; SSF50784; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..366
FT                   /note="Transcription initiation factor IIA subunit 1"
FT                   /id="PRO_0000042590"
FT   CHAIN           1..262
FT                   /note="Transcription initiation factor IIA alpha chain"
FT                   /id="PRO_0000042591"
FT   CHAIN           263..366
FT                   /note="Transcription initiation factor IIA beta chain"
FT                   /id="PRO_0000042592"
FT   REGION          56..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..317
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         265
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         306
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..39
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014784"
FT   VAR_SEQ         75..77
FT                   /note="Missing (in isoform B and isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014785"
FT   CONFLICT        26
FT                   /note="A -> G (in Ref. 1; AAB28821)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="A -> G (in Ref. 1; AAB28821)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  39268 MW;  73A3100332739643 CRC64;
     MALCQTSVLK VYHAVIEDVI TNVRDAFLDE GVDEQVLQEM KQVWRNKLLA SKAVELSPDS
     GDGSHPPPIV ANNPKSHKAA NAKAKKAAAA TAVTSHQHIG GNSSMSSLVG LKSSAGMAAG
     SGIRNGLVPI KQEVNSQNPP PLHPTSAASM MQKQQQAASS GQGSIPIVAT LDPNRIMPVN
     ITLPSPAGSA SSESRVLTIQ VPASALQENQ LTQILTAHLI SSIMSLPTTL ASSVLQQHVN
     AALSSANHQK TLAAAKQLDG ALDSSDEDES EESDDNIDND DDDDLDKDDD EDAEHEDAAE
     EEPLNSEDDV TDEDSAEMFD TDNVIVCQYD KITRSRNKWK FYLKDGIMNM RGKDYVFQKS
     NGDAEW
 
 
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