HAC5_ARATH
ID HAC5_ARATH Reviewed; 1670 AA.
AC Q9LE42; Q8LRK5; Q8LRK6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Histone acetyltransferase HAC5;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN Name=HAC5; Synonyms=PCAT4; OrderedLocusNames=At3g12980;
GN ORFNames=MGH6.20, MGH6_9;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 32-484 AND 529-1540, 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 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}.
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DR EMBL; AB026645; BAB02507.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75270.1; -; Genomic_DNA.
DR EMBL; AH011642; AAM34787.1; -; mRNA.
DR EMBL; AH011642; AAM34788.1; -; mRNA.
DR RefSeq; NP_187904.1; NM_112135.4.
DR AlphaFoldDB; Q9LE42; -.
DR SMR; Q9LE42; -.
DR BioGRID; 5818; 1.
DR STRING; 3702.AT3G12980.1; -.
DR iPTMnet; Q9LE42; -.
DR PaxDb; Q9LE42; -.
DR PRIDE; Q9LE42; -.
DR ProteomicsDB; 247158; -.
DR EnsemblPlants; AT3G12980.1; AT3G12980.1; AT3G12980.
DR GeneID; 820484; -.
DR Gramene; AT3G12980.1; AT3G12980.1; AT3G12980.
DR KEGG; ath:AT3G12980; -.
DR Araport; AT3G12980; -.
DR TAIR; locus:2089285; AT3G12980.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_002956_2_0_1; -.
DR InParanoid; Q9LE42; -.
DR OMA; PIKHETT; -.
DR OrthoDB; 27931at2759; -.
DR PhylomeDB; Q9LE42; -.
DR PRO; PR:Q9LE42; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LE42; baseline and differential.
DR Genevisible; Q9LE42; AT.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; IPI:TAIR.
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; IDA:TAIR.
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 GO; GO:0006473; P:protein acetylation; IMP:TAIR.
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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
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..1670
FT /note="Histone acetyltransferase HAC5"
FT /id="PRO_0000269743"
FT DOMAIN 1061..1497
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 611..690
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 970..1046
FT /note="PHD-type"
FT ZN_FING 1379..1442
FT /note="ZZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1499..1550
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1554..1634
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 490..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1184..1186
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1203..1204
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1259
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 1670 AA; 188188 MW; 2120E9184B4B98BD CRC64;
MAQGQNRTVL QSGQMHNSVV ASASSVSSQP NMVNGISQDT LLLRQEMLNR TYAWLQQRQP
SKTDDASKAK LSEVAKRLES AMWRTATSKE DYLDFRSFDV RVESTLKQLL SQRRANPSSS
VSTMVQTPGV SHGWGQSYTA TPMVDTSKFN SSNNLSDATT ETGRLLPTNR MYRGTINNGR
QELSAVGQMI PTPGFDNSAN ADVYQSHRNE EYSGDGGKLL ATGSDFGNPS QLQKQRPTGS
NDLMGYNLDH QLGGGFRSNI HQNTSGMTSI PLNAGVGMSG NNVHLANVPR SSEGVLSSTH
FSTFSQPSQQ PVEQLQVSHV NRYSMSNSGT FVSGNLYGVQ TSSGSIETAV DMNSMSLNSM
RRVDTSFGSQ SGLQNNPLLK PHLRHQFENG NFQSSSNSKE NLAQVSHRPL ERQFNQQAHY
GQYHQQELLM NNDAYRQSQP ASNLVSQVKN EPRVEYYNEA FQMQAINKVE PSKPQNQYKQ
NTVKDEYVGA QSAPVSSSQL KMSPSFPPQT HQTQQVSQWK DSSSLSAGVQ PVSGLGQWHS
SSQNLTPISK NSNEEREHFG VRFHKQHEGT NNSSSVREST NCLTVAPSGT LDVPHLPVGI
NVLSKQLNGD CGLSYKNQRR WLLFLLHVRK CNAAEDNCES KYCFTAKTLL KHINCCKAPA
CAYQYCHQTR QLIHHYKHCG DEACPVCVFV KNFKEKQKEK FTFLQRAEPS SASLNHGPKE
SFESMRTSSE RDSEAPFVVD DLQPSPKRQK VEKPSQFAYP DTQGNPATIS AGVSQAHFSM
GLQEKDRLPS DVCKPVRSNV PMNADSSDSS RRLVPVSREL EKPVCKDTHM GRHGVKSALD
GESLRLSKQE KPKRMNEISA PKEENAEQSL GVVSASNCGK SKIKGVSLIE LFTPEQVEEH
IRGLRQWVGQ SKTKAEKNKA MGLSMSENSC QLCAVERLAF EPTPIYCTPC GARVKRNAMH
YTVVAGESRH YVCIPCYNEA RANTVSVDGT PVPKSRFEKK KNDEEVEESW VQCDKCQAWQ
HQICALFNGR RNHGQAEYTC PNCYIQEVEQ GERKPVSQNV ILGAKSLPAS TLSNHLEQRL
FKKLKQERQE RARLQGKSYE EVPGADSLVI RVVASVDKIL EVKPRFLDIF REDNYSSEFP
YKSKAILLFQ KIEGVEVCLF GMYVQEFGTD SASPNQRRVY LSYLDSVKYF RPDVRTVSGE
ALRTFVYHEI LIGYLDYCKK RGFSSCYIWA CPPLKGEDYI LYCHPEIQKT PKTDKLREWY
LAMLKKASKE KVVVECTNFY DHFFVQSGEC RAKVTAARLP YFDGDYWPGA AEDLIDQMSQ
EEDGKKSNRK LMPKKVISKR ALKAVGQLDL SVNASKDLLL MHKLGEIILP MKEDFIMVHL
QHCCKHCCTL MVSGNRWVCN QCKNFQICDK CHEVEENRVE KEKHPVNQKE KHVLYPVAID
NIPTEIKDND DILESEFFDT RQAFLSLCQG NHYQYDTLRR AKHSSMMILY HLHNPTVPAF
AMACAICQQE LETAQGWRCE VCPDYDVCNA CYSKGINHPH SIISRPSATD SVVQNTQTNQ
IQNAQLREVL LHVMTCCTAQ CQYPRCRVIK GLIRHGLVCK TRGCIACKKM WSLFRLHSRN
CRDPQCKVPK CRELRAHFSR KQQQADSRRR AAVMEMVRQR AADTTASTPE
