VIP1_ARATH
ID VIP1_ARATH Reviewed; 341 AA.
AC Q9MA75; Q8LDQ9; Q9M5N9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transcription factor VIP1 {ECO:0000305};
DE AltName: Full=Protein SULPHATE UTILIZATION EFFICIENCY 3 {ECO:0000303|PubMed:20547563};
DE AltName: Full=VirE2-interacting protein 1 {ECO:0000303|PubMed:11432846};
DE Short=AtVIP1 {ECO:0000303|PubMed:11432846};
DE AltName: Full=bZIP transcription factor 51 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP51 {ECO:0000303|PubMed:11906833};
DE Short=bZIP protein 51 {ECO:0000305};
GN Name=VIP1 {ECO:0000303|PubMed:11432846};
GN Synonyms=BZIP51 {ECO:0000303|PubMed:11906833},
GN SUE3 {ECO:0000303|PubMed:20547563};
GN OrderedLocusNames=At1g43700 {ECO:0000312|Araport:AT1G43700};
GN ORFNames=F2J6.6 {ECO:0000312|EMBL:AAF63120.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [MRNA] OF 81-341, FUNCTION, INTERACTION WITH
RP AGROBACTERIUM VIRE2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11432846; DOI=10.1093/emboj/20.13.3596;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "VIP1, an Arabidopsis protein that interacts with Agrobacterium VirE2, is
RT involved in VirE2 nuclear import and Agrobacterium infectivity.";
RL EMBO J. 20:3596-3607(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KAP1 AND AGROBACTERIUM
RP VIRE2.
RX PubMed=12124400; DOI=10.1073/pnas.162304099;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "Increasing plant susceptibility to Agrobacterium infection by
RT overexpression of the Arabidopsis nuclear protein VIP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10435-10440(2002).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION DURING
RP PLURIPOTENTIALITY ACQUISITION.
RX PubMed=15108305; DOI=10.1002/dvdy.20006;
RA Avivi Y., Morad V., Ben-Meir H., Zhao J., Kashkush K., Tzfira T.,
RA Citovsky V., Grafi G.;
RT "Reorganization of specific chromosomal domains and activation of silent
RT genes in plant cells acquiring pluripotentiality.";
RL Dev. Dyn. 230:12-22(2004).
RN [9]
RP PROTEASOMAL DEGRADATION MEDIATED BY AGROBACTERIUM VIRF, AND INTERACTION
RP WITH AGROBACTERIUM VIRF.
RX PubMed=15343337; DOI=10.1038/nature02857;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "Involvement of targeted proteolysis in plant genetic transformation by
RT Agrobacterium.";
RL Nature 431:87-92(2004).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, HOMOMULTIMERIZATION,
RP INTERACTION WITH HISTONE H2A RAT5, AND MUTAGENESIS OF 163-ILE--GLY-341.
RC STRAIN=cv. Columbia;
RX PubMed=15824315; DOI=10.1073/pnas.0404118102;
RA Li J., Krichevsky A., Vaidya M., Tzfira T., Citovsky V.;
RT "Uncoupling of the functions of the Arabidopsis VIP1 protein in transient
RT and stable plant genetic transformation by Agrobacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5733-5738(2005).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16581911; DOI=10.1073/pnas.0510607103;
RA Lee J.-Y., Colinas J., Wang J.Y., Mace D., Ohler U., Benfey P.N.;
RT "Transcriptional and posttranscriptional regulation of transcription factor
RT expression in Arabidopsis roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6055-6060(2006).
RN [12]
RP INTERACTION WITH BZIP34 AND BZIP61.
RX PubMed=17719007; DOI=10.1016/j.bbrc.2007.08.026;
RA Shen H., Cao K., Wang X.;
RT "A conserved proline residue in the leucine zipper region of AtbZIP34 and
RT AtbZIP61 in Arabidopsis thaliana interferes with the formation of
RT homodimer.";
RL Biochem. Biophys. Res. Commun. 362:425-430(2007).
RN [13]
RP INTERACTION WITH VIP2.
RC STRAIN=cv. Columbia;
RX PubMed=17496122; DOI=10.1105/tpc.106.042903;
RA Anand A., Krichevsky A., Schornack S., Lahaye T., Tzfira T., Tang Y.,
RA Citovsky V., Mysore K.S.;
RT "Arabidopsis VIRE2 INTERACTING PROTEIN2 is required for Agrobacterium T-DNA
RT integration in plants.";
RL Plant Cell 19:1695-1708(2007).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-79, INTERACTION WITH
RP MPK3, AND MUTAGENESIS OF SER-79.
RX PubMed=17947581; DOI=10.1126/science.1148110;
RA Djamei A., Pitzschke A., Nakagami H., Rajh I., Hirt H.;
RT "Trojan horse strategy in Agrobacterium transformation: abusing MAPK
RT defense signaling.";
RL Science 318:453-456(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [16]
RP FUNCTION, MUTAGENESIS OF LYS-212, AND HOMODIMERIZATION.
RX PubMed=19820165; DOI=10.1073/pnas.0905599106;
RA Pitzschke A., Djamei A., Teige M., Hirt H.;
RT "VIP1 response elements mediate mitogen-activated protein kinase 3-induced
RT stress gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18414-18419(2009).
RN [17]
RP PROTEASOMAL DEGRADATION MEDIATED BY VBF, AND INTERACTION WITH VBF AND
RP AGROBACTERIUM VIRE2.
RX PubMed=20227663; DOI=10.1016/j.chom.2010.02.009;
RA Zaltsman A., Krichevsky A., Loyter A., Citovsky V.;
RT "Agrobacterium induces expression of a host F-box protein required for
RT tumorigenicity.";
RL Cell Host Microbe 7:197-209(2010).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20547563; DOI=10.1093/jxb/erq161;
RA Wu Y., Zhao Q., Gao L., Yu X.-M., Fang P., Oliver D.J., Xiang C.-B.;
RT "Isolation and characterization of low-sulphur-tolerant mutants of
RT Arabidopsis.";
RL J. Exp. Bot. 61:3407-3422(2010).
RN [19]
RP FUNCTION.
RX PubMed=22452852; DOI=10.1104/pp.112.197020;
RA Tsugama D., Liu S., Takano T.;
RT "A bZIP protein, VIP1, is a regulator of osmosensory signaling in
RT Arabidopsis.";
RL Plant Physiol. 159:144-155(2012).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25093810; DOI=10.1371/journal.pone.0103930;
RA Tsugama D., Liu S., Takano T.;
RT "Analysis of functions of VIP1 and its close homologs in osmosensory
RT responses of Arabidopsis thaliana.";
RL PLoS ONE 9:e103930-e103930(2014).
RN [21]
RP FUNCTION.
RX PubMed=27208231; DOI=10.1104/pp.16.00256;
RA Tsugama D., Liu S., Takano T.;
RT "The bZIP protein VIP1 is involved in touch responses in Arabidopsis
RT roots.";
RL Plant Physiol. 171:1355-1365(2016).
RN [22]
RP FUNCTION.
RX PubMed=30010769; DOI=10.1093/aob/mcy125;
RA Tsugama D., Liu S., Fujino K., Takano T.;
RT "Calcium signalling regulates the functions of the bZIP protein VIP1 in
RT touch responses in Arabidopsis thaliana.";
RL Ann. Bot. 122:1219-1229(2018).
RN [23]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31504762; DOI=10.1093/jxb/erz384;
RA Tsugama D., Yoon H.S., Fujino K., Liu S., Takano T.;
RT "Protein phosphatase 2A regulates the nuclear accumulation of the
RT Arabidopsis bZIP protein VIP1 under hypo-osmotic stress.";
RL J. Exp. Bot. 70:6101-6112(2019).
CC -!- FUNCTION: Transcription activator that binds specifically to the VIP1
CC response elements (VREs) DNA sequence 5'-ACNGCT-3' found in some stress
CC genes (e.g. TRX8 and MYB44), when phosphorylated/activated by MPK3.
CC Required for Agrobacterium VirE2 nuclear import and tumorigenicity.
CC Promotes transient expression of T-DNA in early stages by interacting
CC with VirE2 in complex with the T-DNA and facilitating its translocation
CC to the nucleus, and mediates stable genetic transformation by
CC Agrobacterium by binding H2A histone. Prevents cell differentiation and
CC shoot formation. Limits sulfate utilization efficiency (SUE) and
CC sulfate uptake, especially in low-sulfur conditions (PubMed:11432846,
CC PubMed:12124400, PubMed:15108305, PubMed:15824315, PubMed:17947581,
CC PubMed:19820165, PubMed:20547563). Plays a role in osmosensory response
CC by binding to the 5'-AGCTGT/G-3' DNA sequence found in the promoters of
CC the hypoosmolarity-responsive genes CYP707A1 and CYP707A3
CC (PubMed:25093810, PubMed:22452852). Involved in the negative regulation
CC of touch-induced root bending and salt-dependent root bending
CC (PubMed:27208231, PubMed:30010769, PubMed:31504762).
CC {ECO:0000269|PubMed:11432846, ECO:0000269|PubMed:12124400,
CC ECO:0000269|PubMed:15108305, ECO:0000269|PubMed:15824315,
CC ECO:0000269|PubMed:17947581, ECO:0000269|PubMed:19820165,
CC ECO:0000269|PubMed:20547563, ECO:0000269|PubMed:22452852,
CC ECO:0000269|PubMed:25093810, ECO:0000269|PubMed:27208231,
CC ECO:0000269|PubMed:30010769, ECO:0000269|PubMed:31504762}.
CC -!- SUBUNIT: Forms homomultimers. Interacts with Agrobacterium tumefaciens
CC VirE2 and mediates its translocation to the host nucleus. Binds to
CC VIP2. Forms a complex made of Agrobacterium VirE2, VIP1, VIP2 and
CC single-stranded DNA (ssDNA). The interaction with KAP1 mediates its
CC nuclear import. Binds to the H2A histone RAT5. Interacts with MPK3 and
CC Agrobacterium virF. Forms a complex made of VIP1, VBF and Agrobacterium
CC virE2. Interacts with SCF(VBF) E3 ubiquitin ligase complex. Binds
CC directly to VBF. Forms heterodimers with BZIP34 AND BZIP61.
CC {ECO:0000269|PubMed:11432846, ECO:0000269|PubMed:12124400,
CC ECO:0000269|PubMed:15343337, ECO:0000269|PubMed:15824315,
CC ECO:0000269|PubMed:17496122, ECO:0000269|PubMed:17719007,
CC ECO:0000269|PubMed:17947581, ECO:0000269|PubMed:20227663}.
CC -!- INTERACTION:
CC Q9MA75; P15597: virF; Xeno; NbExp=3; IntAct=EBI-606057, EBI-605118;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17947581,
CC ECO:0000269|PubMed:25093810, ECO:0000269|PubMed:31504762}. Nucleus
CC {ECO:0000269|PubMed:17947581, ECO:0000269|PubMed:25093810,
CC ECO:0000269|PubMed:31504762}. Note=Confined to nucleus when
CC phosphorylated (PubMed:17947581). Transiently accumulates in the
CC nucleus when cells are exposed to hypoosmotic conditions
CC (PubMed:25093810, PubMed:31504762). {ECO:0000269|PubMed:17947581,
CC ECO:0000269|PubMed:25093810, ECO:0000269|PubMed:31504762}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in dividing cells, present in
CC leaves, roots and seedlings. {ECO:0000269|PubMed:15108305,
CC ECO:0000269|PubMed:15824315}.
CC -!- INDUCTION: Transcriptionally activated during the acquisition of
CC pluripotentiality (in protoplasts) by pericentromeric chromatin
CC decondensation and DNA demethylation. Targeted to degradation by the
CC proteasome by VBF and Agrobacterium virF in SCF(VBF) and SCF(virF) E3
CC ubiquitin ligase complexes after mediating T-DNA translocation to the
CC nucleus. {ECO:0000269|PubMed:15108305}.
CC -!- PTM: Phosphorylated by MPK3. This phosphorylation promotes nuclear
CC localization. {ECO:0000269|PubMed:17947581}.
CC -!- DISRUPTION PHENOTYPE: Enhanced low sulfur tolerance with higher rate of
CC sulfate uptake at low sulfate levels. Improved tolerance to heavy metal
CC (e.g. CdCl(2)) and oxidative stress (e.g. paraquat).
CC {ECO:0000269|PubMed:20547563}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AC009526; AAF63120.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31988.1; -; Genomic_DNA.
DR EMBL; AY065453; AAL38894.1; -; mRNA.
DR EMBL; AY117284; AAM51359.1; -; mRNA.
DR EMBL; AY085857; AAM63070.1; -; mRNA.
DR EMBL; AF225983; AAF37279.4; -; mRNA.
DR PIR; D96500; D96500.
DR RefSeq; NP_564486.1; NM_103495.4.
DR AlphaFoldDB; Q9MA75; -.
DR SMR; Q9MA75; -.
DR BioGRID; 26182; 17.
DR IntAct; Q9MA75; 13.
DR STRING; 3702.AT1G43700.1; -.
DR iPTMnet; Q9MA75; -.
DR PaxDb; Q9MA75; -.
DR PRIDE; Q9MA75; -.
DR ProteomicsDB; 242481; -.
DR EnsemblPlants; AT1G43700.1; AT1G43700.1; AT1G43700.
DR GeneID; 840957; -.
DR Gramene; AT1G43700.1; AT1G43700.1; AT1G43700.
DR KEGG; ath:AT1G43700; -.
DR Araport; AT1G43700; -.
DR TAIR; locus:2031123; AT1G43700.
DR eggNOG; ENOG502QRMU; Eukaryota.
DR HOGENOM; CLU_026205_2_1_1; -.
DR InParanoid; Q9MA75; -.
DR OMA; MAYIGGH; -.
DR OrthoDB; 967464at2759; -.
DR PhylomeDB; Q9MA75; -.
DR PRO; PR:Q9MA75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA75; baseline and differential.
DR Genevisible; Q9MA75; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009294; P:DNA-mediated transformation; IDA:TAIR.
DR GO; GO:0051170; P:import into nucleus; IDA:TAIR.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IDA:UniProtKB.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0008272; P:sulfate transport; IMP:TAIR.
DR GO; GO:0009652; P:thigmotropism; IMP:TAIR.
DR CDD; cd14703; bZIP_plant_RF2; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR044759; bZIP_RF2.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; Crown gall tumor; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Plant defense; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..341
FT /note="Transcription factor VIP1"
FT /id="PRO_0000405593"
FT DOMAIN 194..257
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..162
FT /note="Necessary and sufficient for transient T-DNA
FT transformation end expression"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..341
FT /note="Involved in homomultimerization and histone H2A
FT binding"
FT REGION 196..217
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 222..257
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 307..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..205
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17947581"
FT MUTAGEN 79
FT /note="S->A: Cytoplasmic and nuclear."
FT /evidence="ECO:0000269|PubMed:17947581"
FT MUTAGEN 79
FT /note="S->D: Only nuclear."
FT /evidence="ECO:0000269|PubMed:17947581"
FT MUTAGEN 163..341
FT /note="Missing: Transient T-DNA transformation end
FT expression, but impaired stable genetic transformation by
FT Agrobacterium, loss of multimerization, and abolished
FT interaction with histone H2A."
FT /evidence="ECO:0000269|PubMed:15824315"
FT MUTAGEN 212
FT /note="K->R,T: Impaired VIP1 response elements (VREs) DNA-
FT binding and altered subsequent transcription activation."
FT /evidence="ECO:0000269|PubMed:19820165"
FT CONFLICT 132
FT /note="I -> L (in Ref. 4; AAM63070)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="T -> K (in Ref. 4; AAM63070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37791 MW; 10BE8D8230C53531 CRC64;
MEGGGRGPNQ TILSEIEHMP EAPRQRISHH RRARSETFFS GESIDDLLLF DPSDIDFSSL
DFLNAPPPPQ QSQQQPQASP MSVDSEETSS NGVVPPNSLP PKPEARFGRH VRSFSVDSDF
FDDLGVTEEK FIATSSGEKK KGNHHHSRSN SMDGEMSSAS FNIESILASV SGKDSGKKNM
GMGGDRLAEL ALLDPKRAKR ILANRQSAAR SKERKIRYTG ELERKVQTLQ NEATTLSAQV
TMLQRGTSEL NTENKHLKMR LQALEQQAEL RDALNEALRD ELNRLKVVAG EIPQGNGNSY
NRAQFSSQQS AMNQFGNKTN QQMSTNGQPS LPSYMDFTKR G
