ID   TADA3_PONAB             Reviewed;         432 AA.
AC   Q5R5V0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Transcriptional adapter 3;
DE   AltName: Full=ADA3 homolog;
DE   AltName: Full=Transcriptional adapter 3-like;
DE            Short=ADA3-like protein;
GN   Name=TADA3; Synonyms=ADA3, TADA3L;
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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a component of the PCAF complex. The PCAF
CC       complex is capable of efficiently acetylating histones in a nucleosomal
CC       context. The PCAF complex could be considered as the human version of
CC       the yeast SAGA complex. Also known as a coactivator for p53/TP53-
CC       dependent transcriptional activation (By similarity). Component of the
CC       ATAC complex, a complex with histone acetyltransferase activity on
CC       histones H3 and H4 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The PCAF complex is composed of a number of TBP-associated
CC       factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and
CC       TAF12, PCAF, and also PCAF-associated factors (PAFs), such as
CC       TADA2L/ADA2, TADA3L/ADA3 and SPT3. Interacts directly with TADA2L and
CC       PCAF and also with the high-risk HPV oncoprotein E6. Component of the
CC       STAGA transcription coactivator-HAT complex, at least composed of
CC       SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12,
CC       TRRAP and TAF9. Component of the TFTC-HAT complex (By similarity).
CC       Component of the ADA2A-containing complex (ATAC), composed of KAT14,
CC       KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NGG1 family. {ECO:0000305}.
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DR   EMBL; CR860753; CAH92866.1; -; mRNA.
DR   RefSeq; NP_001127599.1; NM_001134127.1.
DR   AlphaFoldDB; Q5R5V0; -.
DR   SMR; Q5R5V0; -.
DR   STRING; 9601.ENSPPYP00000015293; -.
DR   GeneID; 100174678; -.
DR   KEGG; pon:100174678; -.
DR   CTD; 10474; -.
DR   eggNOG; KOG4191; Eukaryota.
DR   InParanoid; Q5R5V0; -.
DR   OrthoDB; 1026409at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019340; Histone_AcTrfase_su3.
DR   PANTHER; PTHR13556; PTHR13556; 2.
DR   Pfam; PF10198; Ada3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..432
FT                   /note="Transcriptional adapter 3"
FT                   /id="PRO_0000357452"
FT   REGION          87..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          40..69
FT                   /evidence="ECO:0000255"
FT   COILED          367..407
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        87..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75528"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75528"
FT   MOD_RES         418
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75528"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75528"
FT   CROSSLNK        129
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75528"
SQ   SEQUENCE   432 AA;  48872 MW;  59993E2CF9C14B5D CRC64;
     MSELKDCPLQ FHDFKSVDHL KVCPRYTAVL ARSEDDGIGI EELDTLQLEL ETLLSSASRR
     LRVLEAETQI LTDWQDKKGD RRFLKLGRDH ELGAPPKHGK PKKQKLEGKA GHGPGPGPGR
     PKSKNLQPKV QEYEFTDDPI DVPRIPKNDA PNRFWASVEP YCADITSEEV RTLEELLKPP
     EDEAEHYKIP PLGKHYSQRW AQEDLLEEQK DGARAAAVAD KKKGLMGPLT ELDTKDVDAL
     PKKSEAQHEQ PEDGCPFGAL TQRLLQALVE ENIISPMEDS PIPDMSGKES GADGASTSPR
     NQNKPFSVPH TKSLESRIKE ELIAQGLLES EDRPAEDSED EVLAELRKRQ AELKALSAHN
     RTKKHDLLRL AKEEVSRQEL RQRVRMADNE VMDAFRKIMA ARQKKRTPTK KEKDQAWKTL
     KERESILKLL DG