TADA3_RAT
ID TADA3_RAT Reviewed; 432 AA.
AC Q4V8F5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC097414; AAH97414.1; -; mRNA.
DR RefSeq; NP_001020905.1; NM_001025734.1.
DR RefSeq; XP_006237104.1; XM_006237042.1.
DR AlphaFoldDB; Q4V8F5; -.
DR SMR; Q4V8F5; -.
DR STRING; 10116.ENSRNOP00000011827; -.
DR iPTMnet; Q4V8F5; -.
DR PhosphoSitePlus; Q4V8F5; -.
DR PaxDb; Q4V8F5; -.
DR Ensembl; ENSRNOT00000011827; ENSRNOP00000011827; ENSRNOG00000008597.
DR GeneID; 362414; -.
DR KEGG; rno:362414; -.
DR UCSC; RGD:1564009; rat.
DR CTD; 10474; -.
DR RGD; 1564009; Tada3.
DR eggNOG; KOG4191; Eukaryota.
DR GeneTree; ENSGT00390000008947; -.
DR HOGENOM; CLU_038515_0_0_1; -.
DR InParanoid; Q4V8F5; -.
DR OMA; TPNKFWA; -.
DR OrthoDB; 1026409at2759; -.
DR PhylomeDB; Q4V8F5; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q4V8F5; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008597; Expressed in heart and 20 other tissues.
DR Genevisible; Q4V8F5; RN.
DR GO; GO:0140672; C:ATAC complex; ISO:RGD.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000124; C:SAGA complex; ISO:RGD.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:RGD.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; ISO:RGD.
DR GO; GO:0045995; P:regulation of embryonic development; ISO:RGD.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:RGD.
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_0000357453"
FT REGION 87..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..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 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; 48898 MW; 778A2C64AF3883AD CRC64;
MSELKDCPLQ FHDFKSVDHM KVCPRYTAVL ARSEDDGIGI EELDTLQLEL ETLLSSASRR
LRVLEAETQI LTDWQDKKGD RRILKLARDH ELGAPPKHGK PKKQKLEGKT GHGPGPGPGR
PKSKNVQPKI QEYEFTDDPI DVPRIPKNDA PNRFWASVEP YCADITSEEV RTLEELLKPP
EDEAEHYKIP PLGKHYSQRW AQEDLLEEQK DGARAAAVAD KKKGLIGPLT ELDTKDVDAL
LKKSEAQHEQ PEDGCPFGAL TQRLLQALVE ENIISPMEDS PIPDMSGKES GADGASTSPR
NQNKPFSVPH TKSLESRIKE ELIAQGLLES EDRPAEDSED EVLAELRKRQ AELKALSAHN
RTKKHDLLRL AKEEVSRQEL RQRVRMADNE VMDAFRKIMA ARQKKRTPTK KEKDQAWKTL
KERESILKLL DG
