TF2AA_RAT
ID TF2AA_RAT Reviewed; 377 AA.
AC O08949;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 a unprocessed large subunit 1 and a
CC small subunit gamma. It was originally believed to be a heterotrimer of
CC an alpha, a beta and a gamma subunit. TFIIA forms a complex with TBP
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: The alpha and beta subunits are postranslationally produced from
CC the precursor formby TASP1. The cleavage promotes proteasomal
CC degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
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DR EMBL; AF000943; AAB58716.1; -; mRNA.
DR RefSeq; NP_071544.1; NM_022208.1.
DR AlphaFoldDB; O08949; -.
DR SMR; O08949; -.
DR STRING; 10116.ENSRNOP00000005873; -.
DR iPTMnet; O08949; -.
DR PhosphoSitePlus; O08949; -.
DR jPOST; O08949; -.
DR PaxDb; O08949; -.
DR PRIDE; O08949; -.
DR Ensembl; ENSRNOT00000005873; ENSRNOP00000005873; ENSRNOG00000004300.
DR GeneID; 83830; -.
DR KEGG; rno:83830; -.
DR UCSC; RGD:69246; rat.
DR CTD; 2957; -.
DR RGD; 69246; Gtf2a1.
DR eggNOG; KOG2652; Eukaryota.
DR GeneTree; ENSGT00940000156726; -.
DR HOGENOM; CLU_030027_5_0_1; -.
DR InParanoid; O08949; -.
DR OMA; EVCDASQ; -.
DR OrthoDB; 1443035at2759; -.
DR PhylomeDB; O08949; -.
DR TreeFam; TF350445; -.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O08949; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004300; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; O08949; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005672; C:transcription factor TFIIA complex; ISO:RGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:RGD.
DR GO; GO:0097550; C:transcription preinitiation complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:RGD.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
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 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..377
FT /note="Transcription initiation factor IIA subunit 1"
FT /id="PRO_0000042601"
FT CHAIN 2..275
FT /note="Transcription initiation factor IIA alpha chain"
FT /id="PRO_0000042602"
FT CHAIN 276..377
FT /note="Transcription initiation factor IIA beta chain"
FT /id="PRO_0000042603"
FT REGION 69..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 275..276
FT /note="Cleavage; by TASP1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 281
FT /note="Phosphoserine; by TAF1"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 282
FT /note="Phosphoserine; by TAF1"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 377 AA; 41563 MW; 205FEEB2B24E8D71 CRC64;
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH
SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA QTQQVLIPAS QQATAPQVIV
PDSKLIQHMN ASSITSAAAT AATLALPAGV TPVQQILTNS GQLLQVVRAA NGAQYIFQPQ
QSVVLQQQVI PQMQPGGVQA PVIQQVLAPL PGGISPQTGV IIQPQQILFT GNKTQVIPTT
VAAPTPAQAQ IPAAGQQQPQ AQPAQQQAPL VLQVDGTGDT SSEEDEDEEE DYDDDEEEDK
EKDGAEDGQV EEEPLNSEDD VSDEEGQELF DTENVVVCQY DKIHRSKNKW KFHLKDGIMN
LNGRDYIFSK AIGDAEW
