TAD2A_ARATH
ID TAD2A_ARATH Reviewed; 548 AA.
AC Q9SFD5; Q9SSE2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcriptional adapter ADA2a;
DE Short=AtADA2a;
GN Name=ADA2A; Synonyms=HAC10, HXA02, HXA2; OrderedLocusNames=At3g07740;
GN ORFNames=F17A17.8, MLP3.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH GCN5 AND DREB1B/CBF1.
RX PubMed=11266554; DOI=10.1093/nar/29.7.1524;
RA Stockinger E.J., Mao Y., Regier M.K., Triezenberg S.J., Thomashow M.F.;
RT "Transcriptional adaptor and histone acetyltransferase proteins in
RT Arabidopsis and their interactions with CBF1, a transcriptional activator
RT involved in cold-regulated gene expression.";
RL Nucleic Acids Res. 29:1524-1533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-306 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX DOI=10.1002/cfg.146;
RA Paz-Ares J., Valencia A., Costantino P., Vittorioso P., Davies B.,
RA Gilmartin P., Giraudat J., Parcy F., Reindl A., Sablowski R., Coupland G.,
RA Martin C., Angenent G.C., Baeumlein H., Mock H.-P., Carbonero P.,
RA Colombo L., Tonelli C., Engstroem P., Droege-Laser W., Gatz C.,
RA Kavanagh T., Kushnir S., Zabeau M., Laux T., Hordsworth M., Ruberti I.,
RA Ratcliff F., Smeekens S., Somssich I., Weisshaar B., Traas J.;
RT "REGIA, an EU project on functional genomics of transcription factors from
RT Arabidopsis thaliana.";
RL Comp. Funct. Genomics 3:102-108(2002).
RN [7]
RP INTERACTION WITH GCN5 AND DREB1B/CBF1, ACETYLATION AT LYS-257, AND
RP MUTAGENESIS OF LYS-257.
RX PubMed=16603259; DOI=10.1016/j.bbaexp.2006.02.006;
RA Mao Y., Pavangadkar K.A., Thomashow M.F., Triezenberg S.J.;
RT "Physical and functional interactions of Arabidopsis ADA2 transcriptional
RT coactivator proteins with the acetyltransferase GCN5 and with the cold-
RT induced transcription factor CBF1.";
RL Biochim. Biophys. Acta 1759:69-79(2006).
CC -!- FUNCTION: Required for the function of some acidic activation domains,
CC which activate transcription from a distant site. The exact mechanism
CC of action is not yet known (By similarity). ADA2 stimulates the
CC acetyltransferase activity of GCN5 on free histones or nucleosomes,
CC probably by opening up the promoter region. {ECO:0000250}.
CC -!- SUBUNIT: Interacts in vitro with the HAT domain of GCN5 and with the
CC DNA-binding domain of the transcriptional activator DREB1B/CBF1.
CC {ECO:0000269|PubMed:11266554, ECO:0000269|PubMed:16603259}.
CC -!- INTERACTION:
CC Q9SFD5; Q9SDW0: GT-3A; NbExp=4; IntAct=EBI-979206, EBI-9348720;
CC Q9SFD5; Q9AR19: HAG1; NbExp=5; IntAct=EBI-979206, EBI-979271;
CC Q9SFD5; Q9LV52: HSFC1; NbExp=5; IntAct=EBI-979206, EBI-4457746;
CC Q9SFD5; O22179: MYB70; NbExp=3; IntAct=EBI-979206, EBI-1238013;
CC Q9SFD5; Q8S8E3: PYL6; NbExp=3; IntAct=EBI-979206, EBI-2363192;
CC Q9SFD5; Q84MC7: PYL9; NbExp=3; IntAct=EBI-979206, EBI-2349513;
CC Q9SFD5; Q9S7W5: TCP13; NbExp=4; IntAct=EBI-979206, EBI-4424877;
CC Q9SFD5; Q93Z00: TCP14; NbExp=3; IntAct=EBI-979206, EBI-4424563;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SFD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SFD5-2; Sequence=VSP_022094;
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:11266554}.
CC -!- DOMAIN: The middle domain of ADA2a is sufficient for interaction with
CC the HAT catalytic domain of GCN5.
CC -!- PTM: Acetylated in vitro by GCN5, but acetylation is not essential for
CC biological activity. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF338769; AAK31319.1; -; mRNA.
DR EMBL; AC009176; AAF13092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013483; AAF21184.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74594.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74595.1; -; Genomic_DNA.
DR EMBL; AY040045; AAK64103.1; -; mRNA.
DR EMBL; AF360246; AAK25956.1; -; mRNA.
DR EMBL; BX824819; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DR751137; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DR751119; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001078122.2; NM_001084653.2.
DR RefSeq; NP_566317.1; NM_111653.2. [Q9SFD5-1]
DR RefSeq; NP_974251.1; NM_202522.1. [Q9SFD5-2]
DR AlphaFoldDB; Q9SFD5; -.
DR SMR; Q9SFD5; -.
DR BioGRID; 5300; 35.
DR IntAct; Q9SFD5; 31.
DR STRING; 3702.AT3G07740.4; -.
DR iPTMnet; Q9SFD5; -.
DR PaxDb; Q9SFD5; -.
DR PRIDE; Q9SFD5; -.
DR ProteomicsDB; 245280; -. [Q9SFD5-1]
DR EnsemblPlants; AT3G07740.1; AT3G07740.1; AT3G07740. [Q9SFD5-1]
DR EnsemblPlants; AT3G07740.2; AT3G07740.2; AT3G07740. [Q9SFD5-2]
DR GeneID; 819965; -.
DR Gramene; AT3G07740.1; AT3G07740.1; AT3G07740. [Q9SFD5-1]
DR Gramene; AT3G07740.2; AT3G07740.2; AT3G07740. [Q9SFD5-2]
DR KEGG; ath:AT3G07740; -.
DR Araport; AT3G07740; -.
DR eggNOG; KOG0457; Eukaryota.
DR InParanoid; Q9SFD5; -.
DR PhylomeDB; Q9SFD5; -.
DR PRO; PR:Q9SFD5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFD5; baseline and differential.
DR Genevisible; Q9SFD5; AT.
DR GO; GO:0005634; C:nucleus; 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:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IBA:GO_Central.
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; IPR034318; ADA2_plants.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12374:SF60; PTHR12374:SF60; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..548
FT /note="Transcriptional adapter ADA2a"
FT /id="PRO_0000269750"
FT DOMAIN 106..158
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 461..548
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 48..104
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..386
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 257
FT /note="N6-acetyllysine; by GCN5"
FT /evidence="ECO:0000269|PubMed:16603259"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207, ECO:0000303|Ref.6"
FT /id="VSP_022094"
FT MUTAGEN 257
FT /note="K->A,R: No phenotypic effect."
FT /evidence="ECO:0000269|PubMed:16603259"
SQ SEQUENCE 548 AA; 62042 MW; 5B2BDA01D4C9F67F CRC64;
MGRSKLASRP AEEDLNPGKS KRKKISLGPE NAAASISTGI EAGNERKPGL YCCNYCDKDL
SGLVRFKCAV CMDFDLCVEC FSVGVELNRH KNSHPYRVMD NLSFSLVTSD WNADEEILLL
EAIATYGFGN WKEVADHVGS KTTTECIKHF NSAYMQSPCF PLPDLSHTIG KSKDELLAMS
KDSAVKTEIP AFVRLSPKEE LPVSAEIKHE ASGKVNEIDP PLSALAGVKK KGNVPQAKDI
IKLEAAKQQS DRSVGEKKLR LPGEKVPLVT ELYGYNLKRE EFEIEHDNDA EQLLADMEFK
DSDTDAEREQ KLQVLRIYSK RLDERKRRKE FVLERNLLYP DQYEMSLSAE ERKIYKSCKV
FARFQSKEEH KELIKKVIEE HQILRRIEDL QEARTAGCRT TSDANRFIEE KRKKEAEESM
LLRLNHGAPG SIAGKTLKSP RGLPRNLHPF GSDSLPKVTP PRIYSGLDTW DVDGLLGADL
LSETEKKMCN ETRILPVHYL KMLDILTREI KKGQIKKKSD AYSFFKVEPS KVDRVYDMLV
HKGIGDST
