ID   HAC12_ARATH             Reviewed;        1706 AA.
AC   Q9FWQ5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Histone acetyltransferase HAC12;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN   Name=HAC12; OrderedLocusNames=At1g16710; ORFNames=F17F16.8, F17F16_21;
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   IDENTIFICATION, AND 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.
CC       {ECO:0000250|UniProtKB:Q9C5X9}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FWQ5-1; Sequence=Displayed;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG09087.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC026237; AAG09087.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29487.1; -; Genomic_DNA.
DR   PIR; E86302; E86302.
DR   RefSeq; NP_173115.1; NM_101532.3. [Q9FWQ5-1]
DR   AlphaFoldDB; Q9FWQ5; -.
DR   SMR; Q9FWQ5; -.
DR   STRING; 3702.Q9FWQ5; -.
DR   iPTMnet; Q9FWQ5; -.
DR   PaxDb; 3702-AT1G16710-1; -.
DR   ProteomicsDB; 247213; -. [Q9FWQ5-1]
DR   EnsemblPlants; AT1G16710.1; AT1G16710.1; AT1G16710. [Q9FWQ5-1]
DR   GeneID; 838242; -.
DR   Gramene; AT1G16710.1; AT1G16710.1; AT1G16710. [Q9FWQ5-1]
DR   KEGG; ath:AT1G16710; -.
DR   Araport; AT1G16710; -.
DR   TAIR; AT1G16710; HAC12.
DR   eggNOG; KOG1778; Eukaryota.
DR   InParanoid; Q9FWQ5; -.
DR   OrthoDB; 5490807at2759; -.
DR   PhylomeDB; Q9FWQ5; -.
DR   PRO; PR:Q9FWQ5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FWQ5; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006473; P:protein acetylation; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15614; PHD_HAC_like; 1.
DR   Gene3D; 3.30.60.90; -; 2.
DR   Gene3D; 1.20.1020.10; TAZ domain; 2.
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; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_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:SF57; HISTONE ACETYLTRANSFERASE HAC12; 1.
DR   Pfam; PF08214; HAT_KAT11; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
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; 2.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 2.
DR   PROSITE; PS50135; ZF_ZZ_2; 2.
DR   Genevisible; Q9FWQ5; AT.
PE   3: Inferred from homology;
KW   Activator; Acyltransferase; Alternative splicing; Chromatin regulator;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1706
FT                   /note="Histone acetyltransferase HAC12"
FT                   /id="PRO_0000269744"
FT   DOMAIN          1090..1526
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT   ZN_FING         637..716
FT                   /note="TAZ-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT   ZN_FING         998..1075
FT                   /note="PHD-type"
FT   ZN_FING         1408..1471
FT                   /note="ZZ-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         1528..1581
FT                   /note="ZZ-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         1588..1671
FT                   /note="TAZ-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..805
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..909
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1213..1215
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1232..1233
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1288
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1453
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1461
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1533
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1536
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1548
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1551
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1557
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1560
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1569
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ   SEQUENCE   1706 AA;  190272 MW;  71CDA5B8B6184518 CRC64;
     MNVQAHMSGQ RSGQVPNQGT VPQNNGNSQM QNLVGSNGAA TAVTGAGAAT GSGTGVRPSR
     NIVGAMDHDI MKLRQYMQTL VFNMLQQRQP SPADAASKAK YMDVARRLEE GLFKMAVTKE
     DYMNRSTLES RITSLIKGRQ INNYNQRHAN SSSVGTMIPT PGLSQTAGNP NLMVTSSVDA
     TIVGNTNITS TALNTGNPLI AGGMHGGNMS NGYQHSSRNF SLGSGGSMTS MGAQRSTAQM
     IPTPGFVNSV TNNNSGGFSA EPTIVPQSQQ QQQRQHTGGQ NSHMLSNHMA AGVRPDMQSK
     PSGAANSSVN GDVGANEKIV DSGSSYTNAS KKLQQGNFSL LSFCPDDLIS GQHIESTFHI
     SGEGYSTTNP DPFDGAITSA GTGTKAHNIN TASFQPVSRV NSSLSHQQQF QQPPNRFQQQ
     PNQIQQQQQQ FLNQRKLKQQ TPQQHRLISN DGLGKTQVDS DMVTKVKCEP GMENKSQAPQ
     SQASERFQLS QLQNQYQNSG EDCQADAQLL PVESQSDICT SLPQNSQQIQ QMMHPQNIGS
     DSSNSFSNLA VGVKSESSPQ GQWPSKSQEN TLMSNAISSG KHIQEDFRQR ITGMDEAQPN
     NLTEGSVIGQ NHTSTISESH NLQNSIGTTC RYGNVSHDPK FKNQQRWLLF LRHARSCKPP
     GGRCQDQNCV TVQKLWSHMD NCADPQCLYP RCRHTKALIG HYKNCKDPRC PVCVPVKTYQ
     QQANVRALAR LKNESSAVGS VNRSVVSNDS LSANAGAVSG TPRCADTLDN LQPSLKRLKV
     EQSFQPVVPK TESCKSSIVS TTEADLSQDA ERKDHRPLKS ETMEVKVEIP DNSVQAGFGI
     KETKSEPFEN VPKPKPVSEP GKHGLSGDSP KQENIKMKKE PGWPKKEPGC PKKEELVESP
     ELTSKSRKPK IKGVSLTELF TPEQVREHIR GLRQWVGQSK AKAEKNQAME NSMSENSCQL
     CAVEKLTFEP PPIYCTPCGA RIKRNAMYYT VGGGETRHYF CIPCYNESRG DTILAEGTSM
     PKAKLEKKKN DEEIEESWVQ CDKCQAWQHQ ICALFNGRRN DGGQAEYTCP YCYVIDVEQN
     ERKPLLQSAV LGAKDLPRTI LSDHIEQRLF KRLKQERTER ARVQGTSYDE IPTVESLVVR
     VVSSVDKKLE VKSRFLEIFR EDNFPTEFPY KSKVVLLFQK IEGVEVCLFG MYVQEFGSEC
     SNPNQRRVYL SYLDSVKYFR PDIKSANGEA LRTFVYHEIL IGYLEYCKLR GFTSCYIWAC
     PPLKGEDYIL YCHPEIQKTP KSDKLREWYL AMLRKAAKEG IVAETTNLYD HFFLQTGECR
     AKVTAARLPY FDGDYWPGAA EDIISQMSQE DDGRKGNKKG ILKKPITKRA LKASGQSDFS
     GNASKDLLLM HKLGETIHPM KEDFIMVHLQ HSCTHCCTLM VTGNRWVCSQ CKDFQLCDGC
     YEAEQKREDR ERHPVNQKDK HNIFPVEIAD IPTDTKDRDE ILESEFFDTR QAFLSLCQGN
     HYQYDTLRRA KHSSMMVLYH LHNPTAPAFV TTCNVCHLDI ESGLGWRCEV CPDYDVCNAC
     YKKEGCINHP HKLTTHPSLA DQNAQNKEAR QLRVLQLRKM LDLLVHASQC RSPVCLYPNC
     RKVKGLFRHG LRCKVRASGG CVLCKKMWYL LQLHARACKE SECDVPRCGD LKEHLRRLQQ
     QSDSRRRAAV MEMMRQRAAE VAGTSG
//