ENAP2_ARATH
ID ENAP2_ARATH Reviewed; 248 AA.
AC Q9FFG0; Q94AX7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Trihelix transcription factor ENAP2 {ECO:0000305};
DE Short=Trihelix DNA-binding protein ENAP2 {ECO:0000305};
DE AltName: Full=Agrobacterium tumefaciens VirF-interacting protein 5 {ECO:0000303|PubMed:26571494};
DE AltName: Full=EIN2 nuclear associated protein 2 {ECO:0000303|PubMed:27694846};
GN Name=ENAP2 {ECO:0000303|PubMed:27694846};
GN Synonyms=VFP5 {ECO:0000303|PubMed:26571494};
GN OrderedLocusNames=At5g05550 {ECO:0000312|Araport:AT5G05550};
GN ORFNames=MOP10.9 {ECO:0000312|EMBL:ANM71132.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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] (ISOFORM 2).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP INTERACTION WITH AGROBACTERIUM TUMEFACIENS VIRULENCE PROTEIN VIRF, AND
RP 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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH EIN2, AND SUBCELLULAR
RP 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).
CC -!- FUNCTION: Probable transcription regulator (By similarity). Promotes
CC histone acetylation during ethylene signaling in an EIN2-dependent
CC manner, thus regulating positively ethylene-responsive genes (By
CC similarity). {ECO:0000250|UniProtKB:Q8VZI9}.
CC -!- SUBUNIT: Interacts with the Agrobacterium tumefaciens virulence protein
CC F (VirF) in the nucleus (PubMed:26571494). Binds to EIN2 C-terminal
CC region in the presence of ethylene (PubMed:27694846).
CC {ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q8VZI9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FFG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FFG0-2; Sequence=VSP_061349;
CC -!- DISRUPTION PHENOTYPE: Reduced ethylene sensitivity.
CC {ECO:0000269|PubMed:27694846}.
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DR EMBL; AB005241; BAB11544.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90887.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71132.1; -; Genomic_DNA.
DR EMBL; AY045635; AAK73993.1; -; mRNA.
DR EMBL; AY059651; AAL31144.1; -; mRNA.
DR EMBL; AK318629; BAH56744.1; -; mRNA.
DR RefSeq; NP_001332681.1; NM_001342823.1.
DR SMR; Q9FFG0; -.
DR ProteomicsDB; 176804; -.
DR ProteomicsDB; 176869; -.
DR EnsemblPlants; AT5G05550.1; AT5G05550.1; AT5G05550. [Q9FFG0-2]
DR EnsemblPlants; AT5G05550.3; AT5G05550.3; AT5G05550. [Q9FFG0-1]
DR GeneID; 830438; -.
DR Gramene; AT5G05550.1; AT5G05550.1; AT5G05550. [Q9FFG0-2]
DR Gramene; AT5G05550.3; AT5G05550.3; AT5G05550. [Q9FFG0-1]
DR KEGG; ath:AT5G05550; -.
DR Araport; AT5G05550; -.
DR HOGENOM; CLU_042856_0_1_1; -.
DR OMA; LNMFMDA; -.
DR PhylomeDB; Q9FFG0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFG0; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR InterPro; IPR044823; ASIL1/2-like.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR PANTHER; PTHR31307; PTHR31307; 1.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Ethylene signaling pathway;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..248
FT /note="Trihelix transcription factor ENAP2"
FT /id="PRO_0000454498"
FT DNA_BIND 24..113
FT /note="MADF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00372"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..210
FT /evidence="ECO:0000255"
FT MOTIF 69..76
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT VAR_SEQ 245..248
FT /note="KNSH -> QL (in isoform 2)"
FT /id="VSP_061349"
SQ SEQUENCE 248 AA; 28417 MW; C8518B2545360D12 CRC64;
METTTPQSKS SVSHRPPLGR EDWWSEEATA TLVEAWGNRY VKLNHGNLRQ NDWKDVADAV
NSRHGDNSRK KTDLQCKNRV DTLKKKYKTE KAKLSPSTWR FYNRLDVLIG PVVKKSAGGV
VKSAPFKNHL NPTGSNSTGS SLEDDDEDDD EVGDWEFVAR KHPRVEEVDL SEGSTCRELA
TAILKFGEVY ERIEGKKQQM MIELEKQRME VTKEVELKRM NMLMEMQLEI EKSKHRKRAS
ASGKKNSH
