TAD2A_DROME
ID TAD2A_DROME Reviewed; 562 AA.
AC Q7KSD8; Q4V6Z0; Q59DW3; Q59DW4; Q8I8U8; Q8I9F2; Q8I9F3; Q8IN85;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcriptional adapter 2A;
DE AltName: Full=dADA2a;
GN Name=Ada2a {ECO:0000303|PubMed:12482983, ECO:0000312|FlyBase:FBgn0263738};
GN Synonyms=Rpb4 {ECO:0000312|EMBL:AAS65168.1};
GN ORFNames=CG43663 {ECO:0000312|FlyBase:FBgn0263738};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN88029.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND E), INTERACTION WITH PCAF,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12482983; DOI=10.1128/mcb.23.1.306-321.2003;
RA Muratoglu S., Georgieva S., Papai G., Scheer E., Enunlu I., Komonyi O.,
RA Cserpan I., Lebedeva L., Nabirochkina E., Udvardy A., Tora L., Boros I.;
RT "Two different Drosophila ADA2 homologues are present in distinct GCN5
RT histone acetyltransferase-containing complexes.";
RL Mol. Cell. Biol. 23:306-321(2003).
RN [2] {ECO:0000312|EMBL:AAS65168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAS65168.1}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:ABF17896.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAN52144.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-562 (ISOFORMS A/B), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12697829; DOI=10.1128/mcb.23.9.3305-3319.2003;
RA Kusch T., Guelman S., Abmayr S.M., Workman J.L.;
RT "Two Drosophila Ada2 homologues function in different multiprotein
RT complexes.";
RL Mol. Cell. Biol. 23:3305-3319(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATAC COMPLEX,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18327268; DOI=10.1038/nsmb.1397;
RA Suganuma T., Gutierrez J.L., Li B., Florens L., Swanson S.K.,
RA Washburn M.P., Abmayr S.M., Workman J.L.;
RT "ATAC is a double histone acetyltransferase complex that stimulates
RT nucleosome sliding.";
RL Nat. Struct. Mol. Biol. 15:364-372(2008).
RN [7]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=19921261; DOI=10.1007/s00438-009-0499-6;
RA Pankotai T., Ujfaludi Z., Vamos E., Suri K., Boros I.M.;
RT "The dissociable RPB4 subunit of RNA Pol II has vital functions in
RT Drosophila.";
RL Mol. Genet. Genomics 283:89-97(2010).
CC -!- FUNCTION: GCN5-independent Rpb4 complexes are highly enriched in
CC decondensed chromosome puffs so may play a role in RNA polymerase II-
CC dependent transcription. {ECO:0000269|PubMed:12697829}.
CC -!- SUBUNIT: Interacts with Pcaf/GCN5 as part of a GCN5-containing ADA
CC (GNAT) multiprotein complex (PubMed:12482983, PubMed:12697829).
CC Component of the Ada2a-containing (ATAC) complex composed of at least
CC Ada2a, Atac1, Hcf, Ada3, Gcn5, Mocs2B, Charac-14, Atac3, Atac2, NC2beta
CC and wds (PubMed:18327268). {ECO:0000269|PubMed:12482983,
CC ECO:0000269|PubMed:12697829, ECO:0000269|PubMed:18327268}.
CC -!- INTERACTION:
CC Q7KSD8-4; O76216: Gcn5; NbExp=5; IntAct=EBI-1246969, EBI-867710;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482983,
CC ECO:0000269|PubMed:12697829, ECO:0000269|PubMed:18327268}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=B {ECO:0000269|PubMed:10731132};
CC IsoId=Q7KSD8-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132};
CC IsoId=Q7KSD8-2; Sequence=VSP_052368;
CC Name=C {ECO:0000269|PubMed:12482983}; Synonyms=ADA2A-SV2
CC {ECO:0000269|PubMed:12482983};
CC IsoId=Q7KSD8-3; Sequence=VSP_052368, VSP_052369;
CC Name=E {ECO:0000269|PubMed:12482983}; Synonyms=ADA2A-SV1
CC {ECO:0000269|PubMed:12482983};
CC IsoId=Q7KSD8-4; Sequence=VSP_052369;
CC Name=D {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VEA5-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development with lowest expression levels in L2 and L3
CC larvae, and highest expression levels during pupal development
CC (PubMed:12482983, PubMed:12697829). Highly expressed in all
CC developmental stages, though its abundance decreases in L2 larvae then
CC returns to high levels in pupae (PubMed:19921261).
CC {ECO:0000269|PubMed:12482983, ECO:0000269|PubMed:12697829,
CC ECO:0000269|PubMed:19921261}.
CC -!- INDUCTION: Under heat shock conditions, strongly down-regulated in L2
CC stage larvae with levels remaining low during the L3 and pupal stages.
CC In second instar larvae, down-regulated 1 hr after starvation and then
CC appears to return to normal expression levels 4 hr after nutritional
CC starvation. {ECO:0000269|PubMed:19921261}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the Rpb4 protein by alternative splicing.
CC {ECO:0000269|PubMed:19921261}.
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DR EMBL; AF544017; AAN88029.1; -; mRNA.
DR EMBL; AF544018; AAN88030.1; -; mRNA.
DR EMBL; AE014297; AAN13767.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65168.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52962.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52963.1; -; Genomic_DNA.
DR EMBL; BT022166; AAY51560.1; -; mRNA.
DR EMBL; BT025205; ABF17896.1; -; mRNA.
DR EMBL; AY142216; AAN52144.1; -; mRNA.
DR RefSeq; NP_001014634.1; NM_001014634.3. [Q7KSD8-4]
DR RefSeq; NP_001014635.1; NM_001014635.3. [Q7KSD8-2]
DR RefSeq; NP_001014636.1; NM_001014636.3. [Q7KSD8-1]
DR RefSeq; NP_001014637.1; NM_001014637.3. [Q7KSD8-3]
DR RefSeq; NP_001163645.1; NM_001170174.2. [Q7KSD8-3]
DR AlphaFoldDB; Q7KSD8; -.
DR SMR; Q7KSD8; -.
DR BioGRID; 77382; 19.
DR IntAct; Q7KSD8; 17.
DR STRING; 7227.FBpp0302532; -.
DR PaxDb; Q7KSD8; -.
DR EnsemblMetazoa; FBtr0310380; FBpp0302531; FBgn0263738. [Q7KSD8-2]
DR EnsemblMetazoa; FBtr0310381; FBpp0302532; FBgn0263738. [Q7KSD8-1]
DR EnsemblMetazoa; FBtr0310382; FBpp0302533; FBgn0263738. [Q7KSD8-3]
DR EnsemblMetazoa; FBtr0310383; FBpp0302534; FBgn0263738. [Q7KSD8-4]
DR EnsemblMetazoa; FBtr0310384; FBpp0302535; FBgn0263738. [Q7KSD8-3]
DR GeneID; 326128; -.
DR KEGG; dme:Dmel_CG43663; -.
DR UCSC; CG33520-RA; d. melanogaster. [Q7KSD8-1]
DR CTD; 373884; -.
DR FlyBase; FBgn0263738; Ada2a.
DR VEuPathDB; VectorBase:FBgn0263738; -.
DR eggNOG; KOG0457; Eukaryota.
DR GeneTree; ENSGT00940000156751; -.
DR HOGENOM; CLU_018273_3_0_1; -.
DR InParanoid; Q7KSD8; -.
DR OMA; WITKYVS; -.
DR PhylomeDB; Q7KSD8; -.
DR SignaLink; Q7KSD8; -.
DR BioGRID-ORCS; 326128; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 326128; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0263738; Expressed in wing disc and 17 other tissues.
DR ExpressionAtlas; Q7KSD8; baseline and differential.
DR Genevisible; Q7KSD8; DM.
DR GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..562
FT /note="Transcriptional adapter 2A"
FT /id="PRO_0000283733"
FT DOMAIN 154..198
FT /note="SANT"
FT /evidence="ECO:0000255"
FT DOMAIN 471..562
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 91..146
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT VAR_SEQ 23..37
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12482983, ECO:0000303|Ref.4"
FT /id="VSP_052368"
FT VAR_SEQ 464..483
FT /note="Missing (in isoform C and isoform E)"
FT /evidence="ECO:0000303|PubMed:12482983, ECO:0000303|Ref.4"
FT /id="VSP_052369"
FT CONFLICT 229
FT /note="S -> T (in Ref. 1; AAN88029/AAN88030)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> P (in Ref. 4; AAY51560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 65625 MW; 0AE29DCC8AE4251C CRC64;
MSFMNPVDMV DEDAADLQFP KVALLHIFTT LNCLFAVEPL GPQVKRFIHA HQNEHTRNSM
VLYNPHTLHR YLEEMEEKTR DQNSSVPSAT KDANRCATCR CSLTEPYIKC SECLDTLLCL
QCFSRGKEAF SHRNNHAYII VRDNIQVFAD EPHWTARDER ILLKTLRTHG YGNWEAVSQA
LDQRHEPAEV RRHYHDCYFG GIFERLLNLK HARDSYVPER MPYVFKMRSL DPPRHDDIAS
MQFRLSAGYR CARGDFDTPY DTSAESLLSI MVDHRGRDDD NEASESEFER EVTEELQLGL
VRAYNNRLRE RQRRYKIMRQ HGLIMPNRTV SWISKYVHAF GSDASCMRFL GFMQICPDPI
KFDMLLESLR YYRELHSQLH KLYDLREHGV RTLSGAKLYA RLSKERQQAQ RDYSRLKQTD
AFDWQQLVQH YESNRSGDPG PLAINSKLYV MNTRRKASPI EIGGGKHFTH CLTPTEYNFS
LIPDLPGYSK LDDGERKLCS VARLVPQSYL DYKNQLVTEQ AKLGYLRLAD ARRLIKIDVN
KTRQIYDFLL EHGHISRPPS YG
