EAF1B_ARATH
ID EAF1B_ARATH Reviewed; 1907 AA.
AC F4J7T2; Q9LRX4;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Chromatin modification-related protein EAF1 B;
DE AltName: Full=ESA1-associated factor 1 B;
GN Name=EAF1B; OrderedLocusNames=At3g24870 {ECO:0000312|Araport:AT3G24870};
GN ORFNames=K7P8.16 {ECO:0000312|EMBL:BAB02897.1};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. {ECO:0000305};
CC Name=1;
CC IsoId=F4J7T2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the EAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02897.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB028609; BAB02897.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76955.1; -; Genomic_DNA.
DR RefSeq; NP_189131.5; NM_113399.7. [F4J7T2-1]
DR AlphaFoldDB; F4J7T2; -.
DR SMR; F4J7T2; -.
DR STRING; 3702.AT3G24870.1; -.
DR iPTMnet; F4J7T2; -.
DR PaxDb; F4J7T2; -.
DR PRIDE; F4J7T2; -.
DR EnsemblPlants; AT3G24870.1; AT3G24870.1; AT3G24870. [F4J7T2-1]
DR GeneID; 822085; -.
DR Gramene; AT3G24870.1; AT3G24870.1; AT3G24870. [F4J7T2-1]
DR KEGG; ath:AT3G24870; -.
DR Araport; AT3G24870; -.
DR TAIR; locus:2087298; AT3G24870.
DR eggNOG; ENOG502S9E7; Eukaryota.
DR HOGENOM; CLU_002111_0_0_1; -.
DR InParanoid; F4J7T2; -.
DR OrthoDB; 37139at2759; -.
DR PRO; PR:F4J7T2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J7T2; baseline and differential.
DR Genevisible; F4J7T2; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
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:2000028; P:regulation of photoperiodism, flowering; IMP:TAIR.
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 Alternative splicing; Chromatin regulator; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1907
FT /note="Chromatin modification-related protein EAF1 B"
FT /id="PRO_0000432987"
FT DOMAIN 563..641
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 1049..1105
FT /note="SANT"
FT /evidence="ECO:0000305"
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 836..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..952
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 1235..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1767..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..1907
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 836..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..909
FT /note="Polar 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 1296..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1907 AA; 206412 MW; 32235FB746FC11BE 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
ATQICHRVAL TCQLRFEERN QHRKLKKIAS VLSYAILQFW SSVEAEVPGE LEETSLGIVK
ETCQESNCLN GIRCLAAGVK EYASRFLKYN NSSISYHSAA LSTPDNMCDP EILDISMVDQ
LTEASLFYSV PSGAMEVYLK SIESHLTRCE KSGSSMQEEV DTSAYDTAGD IGYNVTAFDE
DEGETSTYYL PGAFESSRSF NISHKKRKNL MKSHSARSYD LGDDLPYVNN TGGSNSSSLI
VKRPDSNINA GSVPTRRVRT ASRHRVVSPF GCATTGNLPV PSKTDASSGD TSSFQDEYSS
LHGGSAVQKG TEVESSVNFE KLLPYDMAET SGKPKKKKKT HQGSAYDQTW HLNPSVHVEQ
KDHWKKRPEN NFDMNGLYGP HSAKKQKTTK QLVENNFDMA IPHTGSIPSP AASQMSNMSN
PNKSIKFIGG RDRGRKIKGL KISPGQHGSG NPWSLFEDQA LVVLVHDMGP NWELISDAMN
STLKIKYIYR NPTECKDRHK ILMDKTAGDG ADSAEDSGNS QSYPSTLPGI PKGSARQLFQ
RLQGPMEEDT LKSHFEKICL IGKKLHYRKT QNDGRDPKQI VPVHNSQVMA LSQVFPNNLN
GGVLTPLDVC DASTSGQDVF SLENPGLPML NQGTPVLPTS GAHPSTPGSS GVVLSNNLPT
TSGLQSASVR DGRFNVPRGS LPLDEQHRLQ QFNQTLSGRN LQQPSLSTPA AVSGSDRGHR
MVPGGNAMGV SGMNRNTPMS RPGFQGMASA AMPNTGNMHT SGMVGIPNTG NIHSGGGASQ
GNSMIRPREA VQHMMRMQAA QGNSPGIPAF SNLSSGFTNQ TTPVQAYPGH LSQQHQMSPQ
SHVLGNSHHP HLQSPSQATG AQQEAFAIRQ RQIHQRYLQQ QQQQFPASGS MMPHVQQPQG
SSVSSSSQNS PQTQPPVSPQ PLSMPPVSPS PNINAMAQQK PQKSQLALHG LGRSPQSGTS
GVNNQAGKQR QRQLQQSARQ HPHQRQPTQG QQLNKQLKGM GRGNMIHQNI TVDQSHLNGL
TMPQGNQATE KGEIAVSVRP DQQSSVGTTT STDLQSKPFV SPLSSNHSQQ LPKSFPGALS
PSPQQQMQLH SDNSIQGQSS PATPCNILST SSLSIAPAVA PSNHQHLLIH QKQRNQVQST
AQRVVQHNHL GNSELSKKSQ AECMPRVPQS VTNTTQTASM GTTKGMPQAS NDLKNIKAVG
STAVPALEPP SCVASVQSTA SKVVNNSNTD SAGNDPVSTP NQGLAQKHGI KGVTQRQQQS
LPSEEKRPKL PEKPTVQNQK HLASEEQPHL EEAQELSSSK PPDTKVE
