ENAP1_ARATH
ID ENAP1_ARATH Reviewed; 249 AA.
AC Q8VZI9; Q8LF33; Q9C781; Q9SRL9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Trihelix transcription factor ENAP1 {ECO:0000305};
DE Short=Trihelix DNA-binding protein ENAP1 {ECO:0000305};
DE AltName: Full=Agrobacterium tumefaciens VirF-interacting protein 3 {ECO:0000303|PubMed:26571494};
DE AltName: Full=EIN2 nuclear associated protein 1 {ECO:0000303|PubMed:27694846, ECO:0000303|PubMed:28874528, ECO:0000303|PubMed:29298835};
GN Name=ENAP1 {ECO:0000303|PubMed:27694846, ECO:0000303|PubMed:28874528,
GN ECO:0000303|PubMed:29298835}; Synonyms=VFP3 {ECO:0000303|PubMed:26571494};
GN OrderedLocusNames=At3g11100 {ECO:0000312|Araport:AT3G11100};
GN ORFNames=F11B9.6 {ECO:0000312|EMBL:AAG50987.1},
GN F9F8.9 {ECO:0000312|EMBL:AAF01512.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH AGROBACTERIUM TUMEFACIENS
RP VIRULENCE PROTEIN VIRF, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26571494; DOI=10.1371/journal.pone.0142128;
RA Garcia-Cano E., Magori S., Sun Q., Ding Z., Lazarowitz S.G., Citovsky V.;
RT "Interaction of Arabidopsis trihelix-domain transcription factors VFP3 and
RT VFP5 with Agrobacterium virulence protein VirF.";
RL PLoS ONE 10:e0142128-e0142128(2015).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH EIN2 AND EIN3, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27694846; DOI=10.1038/ncomms13018;
RA Zhang F., Qi B., Wang L., Zhao B., Rode S., Riggan N.D., Ecker J.R.,
RA Qiao H.;
RT "EIN2-dependent regulation of acetylation of histone H3K14 and non-
RT canonical histone H3K23 in ethylene signalling.";
RL Nat. Commun. 7:13018-13018(2016).
RN [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH EIN2 AND EIN3.
RC STRAIN=cv. Columbia;
RX PubMed=28874528; DOI=10.1073/pnas.1707937114;
RA Zhang F., Wang L., Qi B., Zhao B., Ko E.E., Riggan N.D., Chin K., Qiao H.;
RT "EIN2 mediates direct regulation of histone acetylation in the ethylene
RT response.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:10274-10279(2017).
RN [9]
RP INTERACTION WITH RBL, AND SUBCELLULAR LOCATION.
RX PubMed=30338215; DOI=10.1002/2211-5463.12504;
RA de Bossoreille S., Morel P., Trehin C., Negrutiu I.;
RT "REBELOTE, a regulator of floral determinacy in Arabidopsis thaliana,
RT interacts with both nucleolar and nucleoplasmic proteins.";
RL FEBS Open Bio 8:1636-1648(2018).
RN [10]
RP INTERACTION WITH SRT1 AND SRT2, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=29298835; DOI=10.1105/tpc.17.00671;
RA Zhang F., Wang L., Ko E.E., Shao K., Qiao H.;
RT "Histone deacetylases SRT1 and SRT2 interact with ENAP1 to mediate
RT ethylene-induced transcriptional repression.";
RL Plant Cell 30:153-166(2018).
CC -!- FUNCTION: Transcription regulator (PubMed:26571494). Associates with
CC chromatin regions that are associated with ethylene-responses in
CC absence and in presence of ethylene (PubMed:28874528). In the presence
CC of ethylene, promotes histone acetylation in an EIN2- and EIN3-
CC dependent manner, mainly on H3K14 and H3K23, thus regulating positively
CC ethylene-responsive genes (PubMed:27694846, PubMed:28874528).
CC {ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846,
CC ECO:0000269|PubMed:28874528}.
CC -!- SUBUNIT: Interacts with RBL (PubMed:30338215). Interacts with the
CC Agrobacterium tumefaciens virulence protein F (VirF) in the nucleus
CC (PubMed:26571494). Binds to EIN2 and EIN3 C-terminal regions in the
CC presence of ethylene to facilitate their association with histone
CC (PubMed:27694846, PubMed:28874528). Binds to histones in chromatin
CC specific regions associated with ethylene regulated loci
CC (PubMed:28874528). Binds to the promoter region of genes influenced by
CC ethylene (PubMed:29298835). Interacts with SRT1 and SRT2; this
CC interaction is enhanced in the presence of ethylene (PubMed:29298835).
CC {ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846,
CC ECO:0000269|PubMed:28874528, ECO:0000269|PubMed:29298835,
CC ECO:0000269|PubMed:30338215}.
CC -!- INTERACTION:
CC Q8VZI9; Q9FZF2: AGL102; NbExp=3; IntAct=EBI-1998580, EBI-622416;
CC Q8VZI9; Q9SYG2: ASIL1; NbExp=4; IntAct=EBI-1998580, EBI-4424669;
CC Q8VZI9; Q9LJG8: ASIL2; NbExp=3; IntAct=EBI-1998580, EBI-4427947;
CC Q8VZI9; Q9LV59: At3g24490; NbExp=3; IntAct=EBI-1998580, EBI-15191981;
CC Q8VZI9; Q8GXR6: At3g58630/F14P22_220; NbExp=3; IntAct=EBI-1998580, EBI-4457957;
CC Q8VZI9; F4JRH5: At4g12850; NbExp=3; IntAct=EBI-1998580, EBI-15192669;
CC Q8VZI9; F4K162: At5g19490; NbExp=4; IntAct=EBI-1998580, EBI-15191807;
CC Q8VZI9; Q9SZC2: ATMYB69; NbExp=3; IntAct=EBI-1998580, EBI-15201770;
CC Q8VZI9; Q9FG01: ATO; NbExp=4; IntAct=EBI-1998580, EBI-4475455;
CC Q8VZI9; Q9SN74: BHLH47; NbExp=3; IntAct=EBI-1998580, EBI-4437532;
CC Q8VZI9; Q9FMM7: BZIP15; NbExp=3; IntAct=EBI-1998580, EBI-15201762;
CC Q8VZI9; Q9LQ65: BZIP4; NbExp=3; IntAct=EBI-1998580, EBI-942986;
CC Q8VZI9; P68350: DOF1.5; NbExp=3; IntAct=EBI-1998580, EBI-15205840;
CC Q8VZI9; Q8LSZ4: E2FE; NbExp=3; IntAct=EBI-1998580, EBI-2651542;
CC Q8VZI9; Q9S763: WRKY45; NbExp=4; IntAct=EBI-1998580, EBI-15195723;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00372,
CC ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:30338215}. Note=Observed in
CC nucleoplasmic bodies. {ECO:0000269|PubMed:30338215}.
CC -!- DISRUPTION PHENOTYPE: Abnormal general transcriptome profiling
CC (PubMed:26571494). Reduced ethylene sensitivity (PubMed:27694846).
CC {ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50987.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009991; AAF01512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC073395; AAG50987.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75002.1; -; Genomic_DNA.
DR EMBL; AY064137; AAL36044.1; -; mRNA.
DR EMBL; AY085073; AAM61629.1; -; mRNA.
DR RefSeq; NP_566386.1; NM_111947.4.
DR AlphaFoldDB; Q8VZI9; -.
DR SMR; Q8VZI9; -.
DR IntAct; Q8VZI9; 68.
DR STRING; 3702.AT3G11100.1; -.
DR PaxDb; Q8VZI9; -.
DR PRIDE; Q8VZI9; -.
DR ProteomicsDB; 181807; -.
DR EnsemblPlants; AT3G11100.1; AT3G11100.1; AT3G11100.
DR GeneID; 820281; -.
DR Gramene; AT3G11100.1; AT3G11100.1; AT3G11100.
DR KEGG; ath:AT3G11100; -.
DR Araport; AT3G11100; -.
DR TAIR; locus:2074658; AT3G11100.
DR eggNOG; KOG4282; Eukaryota.
DR HOGENOM; CLU_042856_0_1_1; -.
DR InParanoid; Q8VZI9; -.
DR OMA; PLSNWCF; -.
DR OrthoDB; 1221690at2759; -.
DR PhylomeDB; Q8VZI9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZI9; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IMP:UniProtKB.
DR GO; GO:0043972; P:histone H3-K23 acetylation; IMP:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR044823; ASIL1/2-like.
DR InterPro; IPR006578; MADF-dom.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR PANTHER; PTHR31307; PTHR31307; 1.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
DR SMART; SM00595; MADF; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA-binding; Ethylene signaling pathway;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..249
FT /note="Trihelix transcription factor ENAP1"
FT /id="PRO_0000454497"
FT DNA_BIND 22..109
FT /note="MADF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00372"
FT REGION 121..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 193..224
FT /evidence="ECO:0000255"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 131
FT /note="S -> Y (in Ref. 4; AAM61629)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="M -> I (in Ref. 4; AAM61629)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> K (in Ref. 4; AAM61629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 28386 MW; 834E232070C05CFB CRC64;
METTPETQSK THRLPAGRED WWSEDATATL IEAWGDRYVN LNRGNLRQND WKEVADAVNS
SHGNGRPKTD VQCKNRIDTL KKKYKTEKAK PLSNWCFFDR LDFLIGPVMK KSSGAVVKSA
LMNPNLNPTG SKSTGSSLDD DDDDDDDDEE DDDDAGDWGF VVRKHRKVED VDSSEGSAFR
ELARSILKLG EAFERIEGKK QQMMIELEKQ RMEVAKELEL QRMNMLMEMQ LELEKSKLGK
RRAASGKKL
