ID HAC2_ARATH Reviewed; 1367 AA.
AC Q9FYH1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=Histone acetyltransferase HAC2;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN Name=HAC2; Synonyms=PCAT1; OrderedLocusNames=At1g67220; ORFNames=F1N21.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1357, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=11160878; DOI=10.1093/nar/29.3.589;
RA Bordoli L., Netsch M., Luethi U., Lutz W., Eckner R.;
RT "Plant orthologs of p300/CBP: conservation of a core domain in metazoan
RT p300/CBP acetyltransferase-related proteins.";
RL Nucleic Acids Res. 29:589-597(2001).
RN [4]
RP NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation (By similarity). No
CC acetyltransferase activity found in vitro.
CC {ECO:0000250|UniProtKB:Q9C5X9, ECO:0000269|PubMed:11160878}.
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:0000250|UniProtKB:Q9C5X9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Rosette leaves, stems and flowers.
CC {ECO:0000269|PubMed:11160878}.
CC -!- DEVELOPMENTAL STAGE: Expressed in young seedlings.
CC {ECO:0000269|PubMed:11160878}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00238.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002130; AAG00238.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34614.1; -; Genomic_DNA.
DR PIR; B96696; B96696.
DR RefSeq; NP_564891.4; NM_105391.4.
DR AlphaFoldDB; Q9FYH1; -.
DR SMR; Q9FYH1; -.
DR STRING; 3702.Q9FYH1; -.
DR iPTMnet; Q9FYH1; -.
DR PaxDb; 3702-AT1G67220-1; -.
DR EnsemblPlants; AT1G67220.1; AT1G67220.1; AT1G67220.
DR GeneID; 843042; -.
DR Gramene; AT1G67220.1; AT1G67220.1; AT1G67220.
DR KEGG; ath:AT1G67220; -.
DR Araport; AT1G67220; -.
DR TAIR; AT1G67220; HAC2.
DR eggNOG; KOG1778; Eukaryota.
DR eggNOG; KOG2673; Eukaryota.
DR HOGENOM; CLU_002956_1_0_1; -.
DR InParanoid; Q9FYH1; -.
DR OrthoDB; 5490807at2759; -.
DR PRO; PR:Q9FYH1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FYH1; baseline and differential.
DR Genevisible; Q9FYH1; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15614; PHD_HAC_like; 1.
DR CDD; cd02345; ZZ_dah; 1.
DR Gene3D; 3.30.60.90; -; 2.
DR Gene3D; 1.20.1020.10; TAZ domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF53; HISTONE ACETYLTRANSFERASE HAC2; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02135; zf-TAZ; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 2: Evidence at transcript level;
KW Activator; Acyltransferase; Chromatin regulator; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1367
FT /note="Histone acetyltransferase HAC2"
FT /id="PRO_0000269741"
FT REPEAT 188..200
FT /note="1"
FT REPEAT 223..235
FT /note="2"
FT REPEAT 251..263
FT /note="3"
FT REPEAT 286..298
FT /note="4"
FT REPEAT 314..326
FT /note="5"
FT REPEAT 349..361
FT /note="6"
FT REPEAT 377..389
FT /note="7"
FT REPEAT 418..430
FT /note="8"
FT REPEAT 432..444
FT /note="9"
FT REPEAT 459..471
FT /note="10"
FT REPEAT 473..485
FT /note="11"
FT REPEAT 500..512
FT /note="12"
FT DOMAIN 780..1213
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 688..765
FT /note="PHD-type"
FT ZN_FING 1094..1157
FT /note="ZZ-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1220..1273
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1274..1359
FT /note="TAZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 110..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..512
FT /note="12 X 13 AA approximate repeats"
FT COMPBIAS 110..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 903..905
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 922..923
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 978
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1099
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 1367 AA; 155772 MW; 140EF2D47193F0FB CRC64;
MAPPRKRTRD LMPKFLNTES FDEFNQRLNN LPAESNVTSD EDAQFLESRK CQSKRWRKEE
PLKLNLRSPW NVLCSPESIS SAKFIVEKTC LIPVPSFEEA ATNARRCLNT SSIPGSSGSA
SETNSGSDIT KQDFKNDSPS DSKKVQGSST SKSAKPKVIK VYSFVDLVTT TKKGNIQTEE
SSLNHEKKLG TVVDIVEPMK CDERSKEVQG SSTSKSAKPK VIKVYSFADV VTTTKKGNIQ
TEESSLNHEK KLGTVVDIIE PMKCDERSKE VQGSSTSKSA KLKVIKVYSF ADVVTTTKKG
NIQTEESSLN HEKKLGTVVD IVEPMKCDER SKEVQGSSTS KSEKPKVIKV YSFADVVTTT
KKGNIQTEES SLNHEKKLGT VVDIVEPMKC DEGTKCEVTT TNKGKIHTEE RSLNHEKKLG
TVVDIVEPMK CDEGSKCEVT TTNKGNTQTE ERSLNHEKKL GIGVDIVEPM KCDEGTKCEV
TTTNKGKIQT EERSLNYEKK LGIGVDIVEP MKCDEENKCE VNADTFDVVI VEPMKCNKVT
KCEVNVDTTG VNIVEPMKCN EVTKCEVNVD TIGVDIVEPM KCNEESKCEV NADTMSLQKR
SKRAVSLVER FTEEEIKLHI MSLKKPSTQS AVEGMCDLKE EEESCQLCDD GTLLFPPQPL
YCLLCSRRID DRSFYYTPGE EELSNAQHQI CSPCHSRCKT KFPLCGVFID KHKMLKRSNF
DNADTEEWVQ CESCEKWQHQ ICGLYNKLKD EDKTAEYICP TCLLEECQSI NNMALVDYTD
SGAKDLPETV LSYFLEQRLF KRLKEERYQT AKATGKSIND VPEPEGLTLR VVFSADRTLT
VNKQFASLLH KENFPSEFPY RSKVILLFQK VHGVDICIFA LFVQEFGSEC SQPNQRSTYI
FYLDSVKYFK PERVTFAGEA LRTFVYHEVL IGYLEYCKLR GFTTSYIWAC PPKIGQDYIM
YSHPKTQQTP DTKKLRKWYV SMLQKAAEQR VVMNVTNLYD RFFDSTEEYM TAARLPYFEG
SFWSNRAEIM IQDIEREGNN ELQKKVKLLS RRKVKTMSYK TTGDVDVDDV KNILLMEKLE
KEVFPNKKDL MVVELNYSCT RCSKAVLSGL RWFCEKCKNL HLCESCYDAG QELPGEHIYK
RMDKEKHQLS KVQVNGVLFS TTEDNDIIQE NDMFESRQAF LAFSQKHNYN FHTLRHAKHS
SMMILHHLHT SNKHHCSQNS SSLTCTACKK DVSTTIYFPC LLCPDYRACT GCYTKNRTLR
HLHIFPTLPS ANRAPSRTVM VLEILNAISH ALLCQHKTTK SCSYPKCHEV KALFTHNVQC
KIRKKGTRCN TCYKLWQTIR IHVYHCQDLN CPVPQCRDRK EVLIRKV
//
