ID   TF2AA_MOUSE             Reviewed;         378 AA.
AC   Q99PM3; Q8C812;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Transcription initiation factor IIA subunit 1;
DE   AltName: Full=General transcription factor IIA subunit 1;
DE   Contains:
DE     RecName: Full=Transcription initiation factor IIA alpha chain;
DE     AltName: Full=TFIIA p35 subunit;
DE   Contains:
DE     RecName: Full=Transcription initiation factor IIA beta chain;
DE     AltName: Full=TFIIA p19 subunit;
GN   Name=Gtf2a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11159353; DOI=10.1095/biolreprod64.2.507;
RA   Han S., Zhou L., Upadhyaya A.B., Lee S.H., Parker K.L., DeJong J.;
RT   "TFIIAalpha/beta-like factor is encoded by a germ cell-specific gene whose
RT   expression is up-regulated with other general transcription factors during
RT   spermatogenesis in the mouse.";
RL   Biol. Reprod. 64:507-517(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-378.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1 and
CC       a small subunit gamma. It was originally believed to be a heterotrimer
CC       of an alpha (p35), a beta (p19) and a gamma subunit (p12). TFIIA forms
CC       a complex with TBP. Part of TBP-based Pol II pre-initiation complex
CC       (PIC), in which Pol II core assembles with general transcription
CC       factors and other specific initiation factors including GTF2E1, GTF2E2,
CC       GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5,
CC       GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit PIC complex
CC       mediates DNA unwinding and targets Pol II core to the transcription
CC       start site where the first phosphodiester bond forms.
CC       {ECO:0000250|UniProtKB:P52655}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in pachytene spermatocytes and
CC       spermatids. {ECO:0000269|PubMed:11159353}.
CC   -!- INDUCTION: Up-regulated during germ cell differentiation in testis.
CC       {ECO:0000269|PubMed:11159353}.
CC   -!- PTM: The alpha and beta subunits are postranslationally produced from
CC       the precursor form by TASP1. The cleavage promotes proteasomal
CC       degradation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF250834; AAG50431.1; -; mRNA.
DR   EMBL; AK048711; BAC33430.1; ALT_INIT; mRNA.
DR   CCDS; CCDS26089.1; -.
DR   RefSeq; NP_113568.2; NM_031391.2.
DR   RefSeq; NP_780544.1; NM_175335.3.
DR   AlphaFoldDB; Q99PM3; -.
DR   BioGRID; 219952; 25.
DR   ComplexPortal; CPX-743; Transcription factor complex TFIIA.
DR   IntAct; Q99PM3; 12.
DR   MINT; Q99PM3; -.
DR   STRING; 10090.ENSMUSP00000021345; -.
DR   iPTMnet; Q99PM3; -.
DR   PhosphoSitePlus; Q99PM3; -.
DR   EPD; Q99PM3; -.
DR   MaxQB; Q99PM3; -.
DR   PaxDb; 10090-ENSMUSP00000021345; -.
DR   ProteomicsDB; 263289; -.
DR   Pumba; Q99PM3; -.
DR   Antibodypedia; 76; 347 antibodies from 32 providers.
DR   DNASU; 83602; -.
DR   Ensembl; ENSMUST00000021345.14; ENSMUSP00000021345.7; ENSMUSG00000020962.15.
DR   GeneID; 83602; -.
DR   KEGG; mmu:83602; -.
DR   UCSC; uc007okr.2; mouse.
DR   AGR; MGI:1933277; -.
DR   CTD; 2957; -.
DR   MGI; MGI:1933277; Gtf2a1.
DR   VEuPathDB; HostDB:ENSMUSG00000020962; -.
DR   eggNOG; KOG2652; Eukaryota.
DR   GeneTree; ENSGT00940000156726; -.
DR   HOGENOM; CLU_030027_5_0_1; -.
DR   InParanoid; Q99PM3; -.
DR   OMA; EVCDASQ; -.
DR   OrthoDB; 9955at2759; -.
DR   PhylomeDB; Q99PM3; -.
DR   TreeFam; TF350445; -.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 83602; 15 hits in 75 CRISPR screens.
DR   ChiTaRS; Gtf2a1; mouse.
DR   PRO; PR:Q99PM3; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q99PM3; Protein.
DR   Bgee; ENSMUSG00000020962; Expressed in animal zygote and 267 other cell types or tissues.
DR   ExpressionAtlas; Q99PM3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005672; C:transcription factor TFIIA complex; IDA:MGI.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR   GO; GO:0097550; C:transcription preinitiation complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR   GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR   GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; NAS:ComplexPortal.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR   CDD; cd07976; TFIIA_alpha_beta_like; 2.
DR   Gene3D; 1.10.287.100; -; 1.
DR   Gene3D; 2.30.18.10; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   InterPro; IPR004855; TFIIA_asu/bsu.
DR   InterPro; IPR009088; TFIIA_b-brl.
DR   PANTHER; PTHR12694; TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT 1; 1.
DR   PANTHER; PTHR12694:SF7; TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT 1; 1.
DR   Pfam; PF03153; TFIIA; 2.
DR   SMART; SM01371; TFIIA; 1.
DR   SUPFAM; SSF47396; Transcription factor IIA (TFIIA), alpha-helical domain; 1.
DR   SUPFAM; SSF50784; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   Genevisible; Q99PM3; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   CHAIN           2..378
FT                   /note="Transcription initiation factor IIA subunit 1"
FT                   /id="PRO_0000042595"
FT   CHAIN           2..276
FT                   /note="Transcription initiation factor IIA alpha chain"
FT                   /id="PRO_0000042596"
FT   CHAIN           277..378
FT                   /note="Transcription initiation factor IIA beta chain"
FT                   /id="PRO_0000042597"
FT   REGION          69..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..331
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         345
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   BINDING         346
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   SITE            276..277
FT                   /note="Cleavage; by TASP1"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         282
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         283
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         318
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         323
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   CONFLICT        121
FT                   /note="V -> G (in Ref. 1; AAG50431)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="D -> G (in Ref. 1; AAG50431)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333
FT                   /note="T -> A (in Ref. 1; AAG50431)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  41614 MW;  FE28AA688662457E CRC64;
     MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH
     SEEQQLLLQV QQQHQPQQQQ HHHHHHQHQQ AQPQQTVPQQ AQTQQVLIPA SQQATAPQVI
     VPDSKLLQHM NASSITSAAA TAATLALPAG VTPVQQLLTN SGQLLQVVRA ANGAQYILQP
     QQSVVLQQQV IPQMQPGGVQ APVIQQVLAP LPGGISPQTG VIIQPQQILF TGNKTQVIPT
     TVAAPAPAQA PMPAAGQQQP QAQPAQQQAP LVLQVDGTGD TSSEEDEDEE EDYDDDEEED
     KEKDGAEDGQ VEEEPLNSED DVSDEEGQEL FDTENVVVCQ YDKIHRSKNK WKFHLKDGIM
     NLNGRDYIFS KAIGDAEW
//