ID   GCN5_ORYSJ              Reviewed;         511 AA.
AC   Q338B9; B7F469;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=Histone acetyltransferase GCN5;
DE            EC=2.3.1.48 {ECO:0000269|PubMed:28487409};
GN   Name=GCN5; OrderedLocusNames=Os10g0415900, LOC_Os10g28040;
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=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
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, CATALYTIC ACTIVITY, INTERACTION WITH ADA2, 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: Acetylates histones H3 and H4 in vitro (PubMed:28487409).
CC       Acetylates 'Lys-4' of histone H3 (H3K4ac), 'Lys-9' (H3K9ac), 'Lys-14'
CC       (H3K14ac), 'Lys-27' (H3K27ac), and 'Lys-5' of histone H4 (H4K5ac)
CC       (PubMed:28487409). Acetylation of histones gives a specific tag for
CC       epigenetic transcription activation (By similarity). Operates in
CC       concert with certain DNA-binding transcriptional activators (By
CC       similarity). ADA2 and GCN5 function to acetylate nucleosomes, opening
CC       up the promoter region (PubMed:28487409). The ADA2-GCN5 histone
CC       acetyltransferase (HAT) module is recruited by WOX11 to regulate crown
CC       root cell proliferation and stem cell maintenance of root meristem
CC       (PubMed:28487409). The ADA2-GCN5 HAT module together with WOX11 targets
CC       and regulates a set of root-specific genes involved in carbon
CC       metabolism, cell wall biosynthesis, and auxin transport and response
CC       (PubMed:28487409). {ECO:0000250|UniProtKB:Q03330,
CC       ECO:0000269|PubMed:28487409}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000269|PubMed:28487409};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC         Evidence={ECO:0000269|PubMed:28487409};
CC   -!- SUBUNIT: Interacts with ADA2. {ECO:0000269|PubMed:28487409}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, mature leaves, stems and
CC       panicles. {ECO:0000269|PubMed:28487409}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DP000086; ABB47615.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF26518.1; -; Genomic_DNA.
DR   EMBL; AP014966; BAT10851.1; -; Genomic_DNA.
DR   EMBL; AK111779; BAG99416.1; -; mRNA.
DR   RefSeq; XP_015614202.1; XM_015758716.1.
DR   AlphaFoldDB; Q338B9; -.
DR   SMR; Q338B9; -.
DR   STRING; 39947.Q338B9; -.
DR   PaxDb; 39947-Q338B9; -.
DR   EnsemblPlants; Os10t0415900-01; Os10t0415900-01; Os10g0415900.
DR   GeneID; 4348629; -.
DR   Gramene; Os10t0415900-01; Os10t0415900-01; Os10g0415900.
DR   KEGG; osa:4348629; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   HOGENOM; CLU_015741_5_0_1; -.
DR   InParanoid; Q338B9; -.
DR   OMA; FAQPVNR; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
DR   GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IDA:UniProtKB.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR037800; GCN5.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR45750; GH11602P; 1.
DR   PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   Genevisible; Q338B9; OS.
PE   1: Evidence at protein level;
KW   Activator; Acyltransferase; Bromodomain; Chromatin regulator; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..511
FT                   /note="Histone acetyltransferase GCN5"
FT                   /id="PRO_0000269749"
FT   DOMAIN          168..315
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   DOMAIN          415..486
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        233
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         237..239
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         244..250
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         276..279
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
SQ   SEQUENCE   511 AA;  56685 MW;  A506C27F8D96D673 CRC64;
     MDGLAAPSPS HSGATSGGGA SHRKRKLPPS SLSDATADED DDTTAPSSPS TSPSSPSRPS
     SPSSSHSDDD DDDSLHTFTA ARLDGAPPSS SGRPPKPESS TVSAAAAAAA AAAAPKPDSA
     SAAAGDGKED PKGLFTDNIQ TSGAYSAREE GLKREEEAGR LKFLCYSNDG VDEHMIWLVG
     LKNIFARQLP NMPKEYIVRL VMDRTHKSMM VIRNNIVVGG ITYRPYTSQK FGEIAFCAIT
     ADEQVKGYGT RLMNHLKQHA RDADGLTHFL TYADNNAVGY FVKQGFTKEI TLDKERWQGY
     IKDYDGGILM ECRIDQKLPY VDLATMIRRQ RQAIDEKIRE LSNCHIVYSG IDFQKKEAGI
     PRRTMKPEDI QGLREAGWTP DQWGHSKSRS AFSPDYSTYR QQLTNLMRSL LKNMNEHPDA
     WPFKEPVDSR DVPDYYDIIK DPIDLKTMSK RVESEQYYVT LEMFVADMKR MFSNAKTYNS
     PDTIYYKCAS RLESFFSNKV ASQLAQASTK N
//