EAF1A_ARATH
ID EAF1A_ARATH Reviewed; 1957 AA.
AC F4J7T3; Q9LRX3;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Chromatin modification-related protein EAF1 A;
DE AltName: Full=ESA1-associated factor 1 A;
GN Name=EAF1A; OrderedLocusNames=At3g24880 {ECO:0000312|Araport:AT3G24880};
GN ORFNames=K7P8.17 {ECO:0000312|EMBL:BAB02898.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, TISSUE SPECIFICITY,
RP INTERACTION WITH TAF14 AND TAF14B, AND SUBCELLULAR LOCATION.
RX DOI=10.1186/s12870-015-0461-1;
RA Bieluszewski T., Galganski L., Sura W., Bieluszewska A., Abram M.,
RA Ludwikow A., Ziolkowski P., Sadowski J.;
RT "AtEAF1 is a potential platform protein for Arabidopsis NuA4
RT acetyltransferase complex.";
RL BMC Plant Biol. 15:0-0(2015).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. {ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC Interacts with ARP4 and SWC4, and (via HSA domain) with TAF14 and
CC TAF14B. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|Ref.3}.
CC -!- MISCELLANEOUS: Decreased expression of EAF1A leads to decreased levels
CC of H4K5 acetylation in the promoter region of major flowering regulator
CC genes, decreased FLC expression and early flowering.
CC {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the EAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02898.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB028609; BAB02898.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76957.1; -; Genomic_DNA.
DR RefSeq; NP_189132.2; NM_113400.4.
DR AlphaFoldDB; F4J7T3; -.
DR SMR; F4J7T3; -.
DR STRING; 3702.AT3G24880.1; -.
DR iPTMnet; F4J7T3; -.
DR MetOSite; F4J7T3; -.
DR PaxDb; F4J7T3; -.
DR PRIDE; F4J7T3; -.
DR ProteomicsDB; 221959; -.
DR EnsemblPlants; AT3G24880.1; AT3G24880.1; AT3G24880.
DR GeneID; 822086; -.
DR Gramene; AT3G24880.1; AT3G24880.1; AT3G24880.
DR KEGG; ath:AT3G24880; -.
DR Araport; AT3G24880; -.
DR TAIR; locus:2087308; AT3G24880.
DR eggNOG; ENOG502S9E7; Eukaryota.
DR HOGENOM; CLU_002111_0_0_1; -.
DR InParanoid; F4J7T3; -.
DR OrthoDB; 37139at2759; -.
DR PRO; PR:F4J7T3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J7T3; baseline and differential.
DR Genevisible; F4J7T3; AT.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR044798; EAF1A/B.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR46774; PTHR46774; 2.
DR Pfam; PF07529; HSA; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..1957
FT /note="Chromatin modification-related protein EAF1 A"
FT /id="PRO_0000432986"
FT DOMAIN 563..641
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 1049..1105
FT /note="SANT"
FT REGION 108..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1804..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1934..1957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1957 AA; 211667 MW; CB1B90D98678DE5A CRC64;
MHGSVSGYLL VNAEVDSMGG VIDSGGGIGV KTSPRRTAIE KAQAELRQEY DVREERRREL
EFLEKGGNPL DFKFGIATSH SVQSTSLTDQ QAEHFVNSEV KDSFALTASP HGDSVESSGR
PGVPTISEPN TADNLLLFDS ENKSVEGERN LRHPNRQNRT SESERSSKAH TNQNTKETED
SAIFRPYARR NRSKISRDPA RSSSTDLVQN RGGLATSISI RRGSVEGKGC IPEAANQKDM
HTTSVSCPVF ANSNGNIVPK NRVSSNSLNT KVDGEPVVRE STAGSKTSLL KDEADISYSK
SSAYLPVGES GLAGEKAQLV STGGSPKAAT IAGQKNSSTQ LNGLRDSTVE EESLTNRGAT
GTNGLESESS HANNVEVNVD NERDLYKVDK LDSDEISMQK TLRVEGLLDQ TVGEMTKTKI
EDETGQSTTI ISECIPECEM QMKSVKIENQ SHRSTAEMQT KEKSSETEKR LQDGLVVLEN
DSKVGSILSE NPSSTLCSGI PQASVDTSSC TVGNSLLSGT DIEALKHQPS SDAVMLDTVK
EDAILEEARI IQAKKKRIAE LSCGTAPVEV REKSQWDFVL EEMAWLANDF AQERLWKMTA
AAQICHRVAL TCQLRFEERN QHRKLKKIAS VLSNAILQFW SSVEAEVPGE LEETSLGIVK
ETCQESNCLN GRRCLAAGVK EYASRFLKYN NSSISYHSAA PSTPDNMCDP EILDISMVDQ
LTEASLFYSV PSGAMEVYLK SIESHLTRCE KSGSSMQEEV DTSAYDTAGD IGYNVTAFDE
DEGETSTYYL PGAFESSRSF NISHKKRKNL MKSHSARSYD LGDDLPYVNN TGGSNSSSLM
AKRPDSNINA GSVPTRRVRT ASRQRVVSPF GCATTGNLPV PSKTDASSGD TSSFQDEYSS
LHGGSAVQKG TEVESSVNFE KLLPYDMAET SGRPKKKKKT HQGSAYDQTW HLDPSVHVEQ
KDHWKKRPEN NFDMNGLYGP HSAKKQKTTK QLVENNFDMA IPHTGSIPSP AASQMSNMSN
PNKSIKFIGG RDRGRKIKGL KISPGQHGSG NPWSLFEDQA LVVLVHDMGP NWELISDAMN
STLKIKCIYR NPTECKDRHK ILMDKTAGDG ADSAEDSGNS QSYPSTLPGI PKGSARQLFQ
RLQGPMEEDT LKSHFEKICL IGKKLHYRKT QSVIGVSVVS FVHGIQFSSC TGAGISQSLD
IPGLHVSKYS CKSWLGFPEN DGRDSKQIVP VHNSQVMALS QVFPNNLNGG VLTPLDVCDA
STSGQDVFSL ENPGLPMLNQ GTPVLPTSGA HPSTPGSSGV VLSNNLPTTS GLQSASVRDG
RFNVPRGSLP LDEQHRLQQF NQTLSGRNLQ QPSLSTPAAV SGSDRGHRMV PGGNAMGVSG
MNRNTPMSRP GFQGMASSAM PNTGSMLSSG MVEIPNTGNI HSGGGASQGN SMIRPREAVQ
HMMRMQAAQG NSPGIPAFSN LSSGFTNQTT PVQAYPGHLS QQHQMSPQSH VLGNSHHPHL
QSPSQATGAQ QEAFAIRQRQ IHQRYLQQQQ QQQQFPASGS MMPHVQQPQG SSVSSSPQNS
PQTQPPVSPQ PLSMPPVSPS PNINAMAQQK PQKSQLALHG LGRSPQSGTS GVNNQAGKQR
QRQLQQSARQ HPHQRQPTQG QQLNKQLKGM GRGNMIHQNI TVDQSHLNGL TMPQGNQATE
KGEIAVPVRP DQQSSVGTTT STNLQSKPFV SPLSSNHSQQ LPKSFPGALP PSPQQQMQLH
SDNSIQGQSS PATPCNILST SSPSIAPAVA PSNHQHLLIH QKQRNQVQST AQRVVQHNHL
GNSELSKKSQ AERMPRVPQS VTNTTQTVSM GTTKGMPQAS NDLKNIKAVG STAVPALEPP
SCVASVQITA SKVVNSSNTD SAGNDPVSTP NQGLAQKHGI KGVTQRQQQS LPSEEKRPKL
PEKPTVQNQK HLASEEQPHL EEAQELSSSK PPDTKVE
