GCN5_ORYSJ
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 03-AUG-2022, entry version 110.
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; 4530.OS10T0415900-01; -.
DR PaxDb; Q338B9; -.
DR PRIDE; 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; RWMGYIK; -.
DR OrthoDB; 349249at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q338B9; OS.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblPlants.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IEA:EnsemblPlants.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IEA:EnsemblPlants.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IEA:EnsemblPlants.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1904278; P:positive regulation of wax biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010321; P:regulation of vegetative phase change; IEA:EnsemblPlants.
DR GO; GO:0009416; P:response to light stimulus; IEA:EnsemblPlants.
DR GO; GO:0010015; P:root morphogenesis; IEA:EnsemblPlants.
DR Gene3D; 1.20.920.10; -; 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; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
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
