HAC1_ARATH
ID HAC1_ARATH Reviewed; 1697 AA.
AC Q9C5X9; O64548;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone acetyltransferase HAC1;
DE EC=2.3.1.48 {ECO:0000269|PubMed:11160878};
GN Name=HAC1; Synonyms=PCAT2; OrderedLocusNames=At1g79000;
GN ORFNames=YUP8H12R.38, YUP8H12R_22;
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 7-1660 (ISOFORM 2), MUTAGENESIS OF
RP 1159-PHE--TYR-1161; 1279-TRP-TYR-1280 AND 1283-MET-LEU-1284, DEVELOPMENTAL
RP STAGE, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
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.
CC {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:0000269|PubMed:11160878};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5X9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5X9-2; Sequence=VSP_041112;
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 -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002986; AAC17068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36191.1; -; Genomic_DNA.
DR EMBL; AF323954; AAG60059.1; -; mRNA.
DR PIR; T01055; T01055.
DR RefSeq; NP_565197.3; NM_106550.4. [Q9C5X9-1]
DR AlphaFoldDB; Q9C5X9; -.
DR SMR; Q9C5X9; -.
DR BioGRID; 29460; 14.
DR IntAct; Q9C5X9; 11.
DR STRING; 3702.AT1G79000.2; -.
DR iPTMnet; Q9C5X9; -.
DR PaxDb; Q9C5X9; -.
DR PRIDE; Q9C5X9; -.
DR ProteomicsDB; 230125; -. [Q9C5X9-1]
DR EnsemblPlants; AT1G79000.1; AT1G79000.1; AT1G79000. [Q9C5X9-1]
DR GeneID; 844241; -.
DR Gramene; AT1G79000.1; AT1G79000.1; AT1G79000. [Q9C5X9-1]
DR KEGG; ath:AT1G79000; -.
DR Araport; AT1G79000; -.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_002956_2_0_1; -.
DR InParanoid; Q9C5X9; -.
DR PRO; PR:Q9C5X9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5X9; baseline and differential.
DR Genevisible; Q9C5X9; AT.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.1020.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 2.
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; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; PTHR13808; 1.
DR Pfam; PF08214; HAT_KAT11; 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; SSF57903; 1.
DR SUPFAM; SSF57933; SSF57933; 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; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 1: Evidence at protein level;
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..1697
FT /note="Histone acetyltransferase HAC1"
FT /id="PRO_0000269740"
FT DOMAIN 1081..1517
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 629..709
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 989..1066
FT /note="PHD-type"
FT ZN_FING 1399..1462
FT /note="ZZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1519..1572
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1579..1662
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1204..1206
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1223..1224
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1279
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1551
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="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT VAR_SEQ 1661..1697
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11160878"
FT /id="VSP_041112"
FT MUTAGEN 1159..1161
FT /note="FAY->AAA: Abolishes acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11160878"
FT MUTAGEN 1279..1280
FT /note="WY->AA: Abolishes acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11160878"
FT MUTAGEN 1283..1284
FT /note="ML->AA: 3-fold decrease in acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:11160878"
SQ SEQUENCE 1697 AA; 190045 MW; 3B735C2DF863CDB0 CRC64;
MNVQAHMSGQ VSNQGTMSQQ NGNSQMQNLV GGGSAPATGA GLGPSRVSPV DNDILKLRQA
MRIRIFNILQ QKQPSPADEA SKAKYMDVAR RLEEGLFKIA NTKEDYVNPS TLEPRLASLI
KGRQLNNYNQ RHANSSSVGT MIPTPGLQHS GGNPNLMITS SGDATMAGSN NITTSAMNTG
NLLNSGGMLG GNLSNGYQHS SSNFGLGSGG NMSSMSSQRN TGQMMPTPGF VNSSTNNNSN
NGQSYLSVEA SNNSGGFSTA PMMVPQTQQQ QLRQDIGGQN SRMLQNHGSQ MGVGLRPGMQ
QKLSNVSNSS INGGVGMNAK SVDSGTSYTN PIRNSQQAYD NLQRSGMQGD GYGTNNSDPF
GSGNLYGAVT SVGMMTNTQN ANTASFQAVS RTSSSLSHQQ QQFQQQPNRF QQQPNQFHQQ
QQQFLHQQQL KQQSQQQQRF ISHDAFGQNN VASDMVTHVK HEPGMENPSE SIHSQTPEQF
QLSQFQNQYQ NNAEDRHAGS QILPVTSQSD MCTSVPQNSQ QIQQMLHPHS MASDSVNGFS
NLSVGVKTES GMRGHWQSQS QEHTQMSNSM SNERHIQEDF RQRMSGTDEA QPNNMSGGSI
IGQNRVSTTS ESLNPQNPTA TTCRNGNGNR DPRFKNQQKW LLFLRHARHC KAPEGKCPDR
NCVTVQKLWK HMDSCAAPQC SYPRCLPTKT LINHHRSCKE PNCPVCIPVK AYLQQQANAR
SLARLKNETD AARSVNGGGI SSDAVQTSAG AKSCTSPGAD ISGHLQPSLK RLKVEQSSQP
VDVETESCKS SVVSVTEAQS SQYAERKDHK HSDVRAPSKY FEVKAEVSDF SVQTRPGFKD
TKIGIAENIP KQRPVSQPDK QDLSDVSPMQ ETTKVEKEPE SLKKENLAES TEHTSKSGKP
EIKGVSLTEL FTPEQVREHI RGLRQWVGQS KAKAEKNQAM EHSMSENSCQ LCAVEKLTFE
PPPIYCTPCG ARIKRNAMYY TVGAGDTRHY FCIPCYNESR GDTILAEGTP MPKARLEKKK
NDEETEEWWV QCDKCEAWQH QICALFNGRR NDGGQAEYTC PYCFIAEVEQ SKRKPLPQSA
VLGAKDLPRT ILSDHIEQRL FKRLKQERTE RARAQGKSYD EIPTAESLVI RVVSSVDKKL
EVKPRFLEIF REDSYPTEFA YKSKVVLLFQ KIEGVEVCLF GMYVQEFGSE CAFPNQRRVY
LSYLDSVKYF RPEVRSYNGE ALRTFVYHEI LIGYLEYCKL RGFTSCYIWA CPPLKGEDYI
LYCHPEIQKT PKSDKLREWY LAMLRKASKE GIVAETINLY DHFFMQTGEC RAKVTAARLP
YFDGDYWPGA AEDLIYQMSQ EEDGRKGNKK GMLKKTITKR ALKASGQTDL SGNASKDLLL
MHRLGETIHP MKEDFIMVHL QPSCTHCCIL MVSGNRWVCS QCKHFQICDK CYEAEQRRED
RERHPVNFKD KHALYPVEIM DIPADTRDKD EILESEFFDT RQAFLSLCQG NHYQYDTLRR
AKHSSMMVLY HLHNPTAPAF VTTCNACHLD IETGQGWRCE VCPDYDVCNA CFSRDGGVNH
PHKLTNHPSL ADQNAQNKEA RQLRVLQLRK MLDLLVHASQ CRSAHCQYPN CRKVKGLFRH
GINCKVRASG GCVLCKKMWY LLQLHARACK ESECHVPRCR DLKEHLRRLQ QQSDSRRRAA
VMEMMRQRAA EVAGGSG
