HAC4_ARATH
ID HAC4_ARATH Reviewed; 1470 AA.
AC Q9LG11; F4I3I0; Q8LRK3; Q8LRK4; Q94EW2; Q9SGS6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Histone acetyltransferase HAC4;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN Name=HAC4; Synonyms=PCAT3; OrderedLocusNames=At1g55970;
GN ORFNames=F14J16.27, T6H22.22;
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 10-760 AND 1086-1470, 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 772-1470.
RA Richards E.J.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
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).
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 -!- 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=AAF02849.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79331.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK73519.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002304; AAF79331.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009894; AAF02849.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AH011643; AAM34789.1; -; mRNA.
DR EMBL; AH011643; AAM34790.1; -; mRNA.
DR EMBL; AF389513; AAK73519.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q9LG11; -.
DR SMR; Q9LG11; -.
DR STRING; 3702.AT1G55970.1; -.
DR PaxDb; Q9LG11; -.
DR PeptideAtlas; Q9LG11; -.
DR PRIDE; Q9LG11; -.
DR Araport; AT1G55970; -.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_002956_2_0_1; -.
DR InParanoid; Q9LG11; -.
DR OrthoDB; 27931at2759; -.
DR PhylomeDB; Q9LG11; -.
DR PRO; PR:Q9LG11; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LG11; baseline and differential.
DR Genevisible; Q9LG11; 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; 2.
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..1470
FT /note="Histone acetyltransferase HAC4"
FT /id="PRO_0000269742"
FT DOMAIN 856..1293
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 416..495
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 764..841
FT /note="PHD-type"
FT ZN_FING 1175..1238
FT /note="ZZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1295..1347
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1358..1436
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 979..981
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 998..999
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1054
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1220
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 1300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 1470 AA; 166802 MW; C1583E17D19C06CD CRC64;
MNNNKEVPQN SVAVSSSSSA PITVISPQQD ANNFIKKRRT ALRNRIYAIV RHKQKQHQIF
LDKKNQQQQQ RVDDATQRAL LEKQDQQCIA ATRMIEEELL KSSRSFEEYF DLRTFDARVR
TILQQLGTML SQRRAAAAAM NNGEAQCITS TRAVHTSISV SNSFQCGRSL VPINCTTATA
GAFSIGPDMQ THHSTGANHQ MVEVNRPNMN QITCGISSPL ITGFNGNCVP VSANIPMTSQ
DLFNATHFST LPQPFLQPPP DQSHMHRYSM SNVASFGQSN PYPCGVVMSS GSMAVAQNSI
PWNNPNPMQG LDPTVTSYHS NLQPMQQTPL PKRQLHHPLW NTNFQSAPNN RDNLPQVSQQ
LSNHGSRQHR GQHSQNLYPG QLQNQDRLLP NLTQQAMALA APVMHVPSKQ VNEDCGQTSS
NTVLRWIPFM FHARHCKAKK DKCASKFCFQ ARKIVKHIDC CKVPNCKYRY CLGTRMWLDH
FKQCKSISCR TCVAVREYME KNKYTIVPLR RAKCSSASSK CQPKKSSKSR QAYKKGGAEA
PSVDADLQRS IKRPKLHRPS QNITPETKSI SVTGCGVVCK PHSLMNMQEK DGLQSLKVEA
MPMDIDVPGA SEIPVTRELV KHVAEDTPKG NNCGGFAMVE KTSCLLAQGK SKCMNEMSAP
KEENVKQSVE VVDASKMEIS SLVELFTPEQ VKEHIRSLRQ WVGQSKTKAE KNKAMGCSMS
VNSCQLCAVE WLVFEPVPIY CSPCGIRIKK NALHYSIAVG ESRHYVCAPC YNEAREKLVF
LDGTSIPKTR LQKKKNDEQV PEGWVQCDKC EAWQHIICAL FNSRRNHGES TKYTCPSCYI
QEVEQRERRP LPLSAVPGAT SLPVTSLSKH LEERLFKKLK EERQERARLQ GKTYEEVPGA
ESLTVRVVAS VDKVLEVKER FLELFREENY PSEFPYKSKA IFLFQKIENV EVCLFGMFVQ
EFGTDSGPPN ERRVYLSYLD SVKYFRPTFR TVSGEALRTF VYHEILIGYL DYCKKRGFTS
CYIWACPPLK GDDYILYCHP EIQKTPKTDK LREWYLAMLR KASKEDVVVE CTNLYNHFFV
QSGECRANVT AARLPYFDGD YWPSAAEDLL RQMNQEDDGE TKLHRKGLTK KVISKRALKA
VGQLDLSLNA SKDRLMMQKL GETICPMKED FIMVHLQHCC KHCTTLMVSG NRWVCNHCKN
FQICDKCYEV EQNRINIERH PINQKEKHAL FPVAIKDVPT KIEDKDNNLE SEFFHNRQAF
LNLCQGNNYQ YETLRRAKHS SMMILYHLHN PTAPAFATVC TICQQEVENS QGWHCEVCPG
YDVCSACYSK DSINHSHKLT SRSSSTDSTV VQQNGQASQS YQVKLEKLKK LLVHAATCRS
TQCQYQGCRK SKMLFRHCID CTTGDCPICK GLWSLLKLHA RNCRDSKCTV PKCSGLRAIS
RRKQQQADKR RRAAVMEMMR ERAAEATRTG
