TADA2_ORYSJ
ID TADA2_ORYSJ Reviewed; 567 AA.
AC Q75LL6; B7EL06; Q10CS4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transcriptional adapter ADA2;
GN Name=ADA2; OrderedLocusNames=Os03g0750800, LOC_Os03g53960;
GN ORFNames=OSJNBa0047E24.21;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, INTERACTION WITH GCN5 AND WOX11, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=28487409; DOI=10.1105/tpc.16.00908;
RA Zhou S., Jiang W., Long F., Cheng S., Yang W., Zhao Y., Zhou D.X.;
RT "Rice homeodomain protein WOX11 recruits a histone acetyltransferase
RT complex to establish programs of cell proliferation of crown root
RT meristem.";
RL Plant Cell 29:1088-1104(2017).
CC -!- FUNCTION: Required for the function of some acidic activation domains,
CC which activate transcription from a distant site (By similarity). The
CC exact mechanism of action is not yet known (By similarity). ADA2 and
CC GCN5 function to acetylate nucleosomes, opening up the promoter region
CC (PubMed:28487409). The ADA2-GCN5 histone acetyltransferase (HAT) module
CC is recruited by WOX11 to regulate crown root cell proliferation and
CC stem cell maintenance of root meristem (PubMed:28487409). The ADA2-GCN5
CC HAT module together with WOX11 targets and regulates a set of root-
CC specific genes involved in carbon metabolism, cell wall biosynthesis,
CC and auxin transport and response (PubMed:28487409).
CC {ECO:0000250|UniProtKB:Q03330, ECO:0000269|PubMed:28487409}.
CC -!- SUBUNIT: Interacts with GCN5 and WOX11 (via N-terminus).
CC {ECO:0000269|PubMed:28487409}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28487409}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, mature leaves, stems and
CC panicles. {ECO:0000269|PubMed:28487409}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR87248.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF98901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC092556; AAR87248.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98900.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF13201.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86407.1; -; Genomic_DNA.
DR EMBL; AK072597; BAG93053.1; -; mRNA.
DR RefSeq; XP_015631988.1; XM_015776502.1.
DR AlphaFoldDB; Q75LL6; -.
DR SMR; Q75LL6; -.
DR STRING; 4530.OS03T0750800-01; -.
DR PaxDb; Q75LL6; -.
DR PRIDE; Q75LL6; -.
DR EnsemblPlants; Os03t0750800-01; Os03t0750800-01; Os03g0750800.
DR GeneID; 4334126; -.
DR Gramene; Os03t0750800-01; Os03t0750800-01; Os03g0750800.
DR KEGG; osa:4334126; -.
DR eggNOG; KOG0457; Eukaryota.
DR HOGENOM; CLU_018273_3_1_1; -.
DR InParanoid; Q75LL6; -.
DR OMA; EFETEYF; -.
DR OrthoDB; 812864at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q75LL6; baseline and differential.
DR Genevisible; Q75LL6; OS.
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; 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; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..567
FT /note="Transcriptional adapter ADA2"
FT /id="PRO_0000269752"
FT DOMAIN 106..158
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 476..567
FT /note="SWIRM"
FT ZN_FING 48..104
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 288..308
FT /evidence="ECO:0000255"
FT COILED 405..429
FT /evidence="ECO:0000255"
FT COMPBIAS 10..27
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"
SQ SEQUENCE 567 AA; 63552 MW; 2765A8205B0EDA21 CRC64;
MGRSRGVPNS GDDETNHRSK RRRVASSGDA PDSLSAACGG AGEGGGKKAL YHCNYCNKDI
SGKIRIKCSK CPDFDLCVEC FSVGAEVTPH RSNHPYRVMD NLSFPLICPD WNADEEILLL
EGIEMYGLGN WAEVAEHVGT KTKAQCIDHY TTAYMNSPCY PLPDMSHVNG KNRKELLAMA
KVQGESKKVL PGDLTPKDES PFSPPRVKVE DALGEGLAGR SPSHIAGGAN KKASNVGQFK
DGANVAKVED GHVDRSIGVK KPRYSADEGP SLTELSGYNS KRHEFDPEYD NDAEQALAEM
EFKETDSETD RELKLRVLRI YLSRLDERKR RKEFILERNL LFPNPLEKDL TNEDKEVYHR
YKVFMRFLSK EEHEALVRSV LEERKIRRRI QELQECRSAG CRTLAEAKIH IEQKRKKEHE
VNAQKAKESG QLLSNTKVVH KTNRPMKIES DGNLDQKKGG ASLDSTGRDS PKTTGHAGTK
HWDDWDIVGF PGAELLSTSE KNLCCQNRLL PNHYLKMQEV LMQEIFKGSV AKKEDAHVLF
KVDPAKVDNV YDMVTKKLGT NEEAPTV
