ID   TF2AA_PONAB             Reviewed;         376 AA.
AC   Q5RCU0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858178; CAH90417.1; -; mRNA.
DR   RefSeq; NP_001125209.1; NM_001131737.1.
DR   AlphaFoldDB; Q5RCU0; -.
DR   STRING; 9601.ENSPPYP00000006871; -.
DR   GeneID; 100172100; -.
DR   KEGG; pon:100172100; -.
DR   CTD; 2957; -.
DR   eggNOG; KOG2652; Eukaryota.
DR   InParanoid; Q5RCU0; -.
DR   OrthoDB; 1443035at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005672; C:transcription factor TFIIA complex; IEA:InterPro.
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   2: Evidence at transcript 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..376
FT                   /note="Transcription initiation factor IIA subunit 1"
FT                   /id="PRO_0000042598"
FT   CHAIN           2..274
FT                   /note="Transcription initiation factor IIA alpha chain"
FT                   /id="PRO_0000042599"
FT   CHAIN           275..376
FT                   /note="Transcription initiation factor IIA beta chain"
FT                   /id="PRO_0000042600"
FT   REGION          69..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..329
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        278..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            274..275
FT                   /note="Cleavage; by TASP1"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         280
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         281
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         316
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
FT   MOD_RES         321
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000250|UniProtKB:P52655"
SQ   SEQUENCE   376 AA;  41551 MW;  B419A6CAAF511249 CRC64;
     MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH
     SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA QTQQVLIPAS QQATAPQVIV
     PDSKLIQHMN ASNMSAAATA ATLALPAGVT PVQQILTNSG QLLQVVRVAN GAQYIFQPQQ
     SVVLQQQVIP QMQPGGVQAP VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV
     AAPTPAQAQI TATGHQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE
     KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK FHLKDGIMNL
     NGRDYIFSKA IGDAEW