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Transcription factor VIP1 (Protein SULPHATE UTILIZATION EFFICIENCY 3) (VirE2-interacting protein 1) (AtVIP1) (bZIP transcription factor 51) (AtbZIP51) (bZIP protein 51)

 VIP1_ARATH              Reviewed;         341 AA.
Q9MA75; Q8LDQ9; Q9M5N9;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 123.
RecName: Full=Transcription factor VIP1;
AltName: Full=Protein SULPHATE UTILIZATION EFFICIENCY 3;
AltName: Full=VirE2-interacting protein 1;
Short=AtVIP1;
AltName: Full=bZIP transcription factor 51 {ECO:0000303|PubMed:11906833};
Short=AtbZIP51 {ECO:0000303|PubMed:11906833};
Short=bZIP protein 51;
Name=VIP1; Synonyms=BZIP51 {ECO:0000303|PubMed:11906833}, SUE3;
OrderedLocusNames=At1g43700; ORFNames=F2J6.6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 81-341, FUNCTION, INTERACTION WITH
AGROBACTERIUM VIRE2, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=11432846; DOI=10.1093/emboj/20.13.3596;
Tzfira T., Vaidya M., Citovsky V.;
"VIP1, an Arabidopsis protein that interacts with Agrobacterium VirE2,
is involved in VirE2 nuclear import and Agrobacterium infectivity.";
EMBO J. 20:3596-3607(2001).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KAP1 AND
AGROBACTERIUM VIRE2.
PubMed=12124400; DOI=10.1073/pnas.162304099;
Tzfira T., Vaidya M., Citovsky V.;
"Increasing plant susceptibility to Agrobacterium infection by
overexpression of the Arabidopsis nuclear protein VIP1.";
Proc. Natl. Acad. Sci. U.S.A. 99:10435-10440(2002).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11906833; DOI=10.1016/S1360-1385(01)02223-3;
Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
Tiedemann J., Kroj T., Parcy F.;
"bZIP transcription factors in Arabidopsis.";
Trends Plant Sci. 7:106-111(2002).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION
DURING PLURIPOTENTIALITY ACQUISITION.
PubMed=15108305; DOI=10.1002/dvdy.20006;
Avivi Y., Morad V., Ben-Meir H., Zhao J., Kashkush K., Tzfira T.,
Citovsky V., Grafi G.;
"Reorganization of specific chromosomal domains and activation of
silent genes in plant cells acquiring pluripotentiality.";
Dev. Dyn. 230:12-22(2004).
[9]
PROTEASOMAL DEGRADATION MEDIATED BY AGROBACTERIUM VIRF, AND
INTERACTION WITH AGROBACTERIUM VIRF.
PubMed=15343337; DOI=10.1038/nature02857;
Tzfira T., Vaidya M., Citovsky V.;
"Involvement of targeted proteolysis in plant genetic transformation
by Agrobacterium.";
Nature 431:87-92(2004).
[10]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
HOMOMULTIMERIZATION, INTERACTION WITH HISTONE H2A RAT5, AND
MUTAGENESIS OF 163-ILE--GLY-341.
STRAIN=cv. Columbia;
PubMed=15824315; DOI=10.1073/pnas.0404118102;
Li J., Krichevsky A., Vaidya M., Tzfira T., Citovsky V.;
"Uncoupling of the functions of the Arabidopsis VIP1 protein in
transient and stable plant genetic transformation by Agrobacterium.";
Proc. Natl. Acad. Sci. U.S.A. 102:5733-5738(2005).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16581911; DOI=10.1073/pnas.0510607103;
Lee J.-Y., Colinas J., Wang J.Y., Mace D., Ohler U., Benfey P.N.;
"Transcriptional and posttranscriptional regulation of transcription
factor expression in Arabidopsis roots.";
Proc. Natl. Acad. Sci. U.S.A. 103:6055-6060(2006).
[12]
INTERACTION WITH BZIP34 AND BZIP61.
PubMed=17719007; DOI=10.1016/j.bbrc.2007.08.026;
Shen H., Cao K., Wang X.;
"A conserved proline residue in the leucine zipper region of AtbZIP34
and AtbZIP61 in Arabidopsis thaliana interferes with the formation of
homodimer.";
Biochem. Biophys. Res. Commun. 362:425-430(2007).
[13]
INTERACTION WITH VIP2.
STRAIN=cv. Columbia;
PubMed=17496122; DOI=10.1105/tpc.106.042903;
Anand A., Krichevsky A., Schornack S., Lahaye T., Tzfira T., Tang Y.,
Citovsky V., Mysore K.S.;
"Arabidopsis VIRE2 INTERACTING PROTEIN2 is required for Agrobacterium
T-DNA integration in plants.";
Plant Cell 19:1695-1708(2007).
[14]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-79, INTERACTION
WITH MPK3, AND MUTAGENESIS OF SER-79.
PubMed=17947581; DOI=10.1126/science.1148110;
Djamei A., Pitzschke A., Nakagami H., Rajh I., Hirt H.;
"Trojan horse strategy in Agrobacterium transformation: abusing MAPK
defense signaling.";
Science 318:453-456(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[16]
FUNCTION, MUTAGENESIS OF LYS-212, AND HOMODIMERIZATION.
PubMed=19820165; DOI=10.1073/pnas.0905599106;
Pitzschke A., Djamei A., Teige M., Hirt H.;
"VIP1 response elements mediate mitogen-activated protein kinase 3-
induced stress gene expression.";
Proc. Natl. Acad. Sci. U.S.A. 106:18414-18419(2009).
[17]
PROTEASOMAL DEGRADATION MEDIATED BY VBF, AND INTERACTION WITH VBF AND
AGROBACTERIUM VIRE2.
PubMed=20227663; DOI=10.1016/j.chom.2010.02.009;
Zaltsman A., Krichevsky A., Loyter A., Citovsky V.;
"Agrobacterium induces expression of a host F-box protein required for
tumorigenicity.";
Cell Host Microbe 7:197-209(2010).
[18]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=20547563; DOI=10.1093/jxb/erq161;
Wu Y., Zhao Q., Gao L., Yu X.-M., Fang P., Oliver D.J., Xiang C.-B.;
"Isolation and characterization of low-sulphur-tolerant mutants of
Arabidopsis.";
J. Exp. Bot. 61:3407-3422(2010).
-!- FUNCTION: Transcription activator that binds specifically to the
VIP1 response elements (VREs) DNA sequence 5'-ACNGCT-3' found in
some stress genes (e.g. TRX8 and MYB44), when
phosphorylated/activated by MPK3. Required for Agrobacterium VirE2
nuclear import and tumorigenicity. Promotes transient expression
of T-DNA in early stages by interacting with VirE2 in complex with
the T-DNA and facilitating its translocation to the nucleus, and
mediates stable genetic transformation by Agrobacterium by binding
H2A histone. Prevents cell differentiation and shoot formation.
Limits sulfate utilization efficiency (SUE) and sulfate uptake,
especially in low-sulfur conditions. {ECO:0000269|PubMed:11432846,
ECO:0000269|PubMed:12124400, ECO:0000269|PubMed:15108305,
ECO:0000269|PubMed:15824315, ECO:0000269|PubMed:17947581,
ECO:0000269|PubMed:19820165, ECO:0000269|PubMed:20547563}.
-!- SUBUNIT: Forms homomultimers. Interacts with Agrobacterium
tumefaciens VirE2 and mediates its translocation to the host
nucleus. Binds to VIP2. Forms a complex made of Agrobacterium
VirE2, VIP1, VIP2 and single-stranded DNA (ssDNA). The interaction
with KAP1 mediates its nuclear import. Binds to the H2A histone
RAT5. Interacts with MPK3 and Agrobacterium virF. Forms a complex
made of VIP1, VBF and Agrobacterium virE2. Interacts with SCF(VBF)
E3 ubiquitin ligase complex. Binds directly to VBF. Forms
heterodimers with BZIP34 AND BZIP61. {ECO:0000269|PubMed:11432846,
ECO:0000269|PubMed:12124400, ECO:0000269|PubMed:15343337,
ECO:0000269|PubMed:15824315, ECO:0000269|PubMed:17496122,
ECO:0000269|PubMed:17719007, ECO:0000269|PubMed:17947581,
ECO:0000269|PubMed:20227663}.
-!- INTERACTION:
P15597:virF (xeno); NbExp=3; IntAct=EBI-606057, EBI-605118;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Confined to nucleus
when phosphorylated.
-!- TISSUE SPECIFICITY: Mostly expressed in dividing cells, present in
leaves, roots and seedlings. {ECO:0000269|PubMed:15108305,
ECO:0000269|PubMed:15824315}.
-!- INDUCTION: Transcriptionally activated during the acquisition of
pluripotentiality (in protoplasts) by pericentromeric chromatin
decondensation and DNA demethylation. Targeted to degradation by
the proteasome by VBF and Agrobacterium virF in SCF(VBF) and
SCF(virF) E3 ubiquitin ligase complexes after mediating T-DNA
translocation to the nucleus. {ECO:0000269|PubMed:15108305}.
-!- PTM: Phosphorylated by MPK3. This phosphorylation promotes nuclear
localization. {ECO:0000269|PubMed:17947581}.
-!- DISRUPTION PHENOTYPE: Enhanced low sulfur tolerance with higher
rate of sulfate uptake at low sulfate levels. Improved tolerance
to heavy metal (e.g. CdCl(2)) and oxidative stress (e.g.
paraquat). {ECO:0000269|PubMed:20547563}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC009526; AAF63120.1; -; Genomic_DNA.
EMBL; CP002684; AEE31988.1; -; Genomic_DNA.
EMBL; AY065453; AAL38894.1; -; mRNA.
EMBL; AY117284; AAM51359.1; -; mRNA.
EMBL; AY085857; AAM63070.1; -; mRNA.
EMBL; AF225983; AAF37279.4; -; mRNA.
PIR; D96500; D96500.
RefSeq; NP_564486.1; NM_103495.4.
UniGene; At.22614; -.
UniGene; At.24245; -.
ProteinModelPortal; Q9MA75; -.
BioGrid; 26182; 12.
IntAct; Q9MA75; 13.
STRING; 3702.AT1G43700.1; -.
iPTMnet; Q9MA75; -.
PaxDb; Q9MA75; -.
EnsemblPlants; AT1G43700.1; AT1G43700.1; AT1G43700.
GeneID; 840957; -.
Gramene; AT1G43700.1; AT1G43700.1; AT1G43700.
KEGG; ath:AT1G43700; -.
Araport; AT1G43700; -.
TAIR; locus:2031123; AT1G43700.
eggNOG; ENOG410IH5N; Eukaryota.
eggNOG; ENOG410YA2S; LUCA.
HOGENOM; HOG000239687; -.
InParanoid; Q9MA75; -.
KO; K20557; -.
OMA; MLQRGTS; -.
OrthoDB; EOG09360KNN; -.
PhylomeDB; Q9MA75; -.
PRO; PR:Q9MA75; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q9MA75; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003682; F:chromatin binding; IDA:TAIR.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; IDA:TAIR.
GO; GO:0043621; F:protein self-association; IPI:TAIR.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:TAIR.
GO; GO:0009970; P:cellular response to sulfate starvation; IMP:TAIR.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0009294; P:DNA mediated transformation; IDA:TAIR.
GO; GO:0045596; P:negative regulation of cell differentiation; IDA:UniProtKB.
GO; GO:0051170; P:nuclear import; IDA:TAIR.
GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
GO; GO:0008272; P:sulfate transport; IMP:TAIR.
GO; GO:0009652; P:thigmotropism; IMP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Activator; Complete proteome; Crown gall tumor; Cytoplasm;
DNA-binding; Nucleus; Phosphoprotein; Plant defense;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation pathway.
CHAIN 1 341 Transcription factor VIP1.
/FTId=PRO_0000405593.
DOMAIN 194 257 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 162 Necessary and sufficient for transient T-
DNA transformation end expression.
REGION 163 341 Involved in homomultimerization and
histone H2A binding.
REGION 196 217 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 222 257 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 198 205 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000269|PubMed:17947581}.
MUTAGEN 79 79 S->A: Cytoplasmic and nuclear.
{ECO:0000269|PubMed:17947581}.
MUTAGEN 79 79 S->D: Only nuclear.
{ECO:0000269|PubMed:17947581}.
MUTAGEN 163 341 Missing: Transient T-DNA transformation
end expression, but impaired stable
genetic transformation by Agrobacterium,
loss of multimerization, and abolished
interaction with histone H2A.
{ECO:0000269|PubMed:15824315}.
MUTAGEN 212 212 K->R,T: Impaired VIP1 response elements
(VREs) DNA-binding and altered subsequent
transcription activation.
{ECO:0000269|PubMed:19820165}.
CONFLICT 132 132 I -> L (in Ref. 4; AAM63070).
{ECO:0000305}.
CONFLICT 319 319 T -> K (in Ref. 4; AAM63070).
{ECO:0000305}.
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


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