VOZ2_ARATH
ID VOZ2_ARATH Reviewed; 450 AA.
AC Q9SLB9; Q9ASU2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription factor VOZ2;
DE AltName: Full=Protein VASCULAR PLANT ONE-ZINC FINGER 2;
DE Short=AtVOZ2;
GN Name=VOZ2; OrderedLocusNames=At2g42400; ORFNames=MHK10.12;
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 [MRNA], DNA-BINDING, DOMAIN, FUNCTION, SUBUNIT, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF CYS-230; CYS-235; CYS-249 AND HIS-253.
RX PubMed=15295067; DOI=10.1093/pcp/pch101;
RA Mitsuda N., Hisabori T., Takeyasu K., Sato M.H.;
RT "VOZ; isolation and characterization of novel vascular plant transcription
RT factors with a one-zinc finger from Arabidopsis thaliana.";
RL Plant Cell Physiol. 45:845-854(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP DOMAIN VOZ.
RX DOI=10.1016/j.plantsci.2005.05.035;
RA Olsena A.N., Ernstb H.A., Leggiob L.L., Skriver K.;
RT "DNA-binding specificity and molecular functions of NAC transcription
RT factors.";
RL Plant Sci. 169:785-797(2005).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH PHYB, DISRUPTION PHENOTYPE,
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=22904146; DOI=10.1105/tpc.112.101915;
RA Yasui Y., Mukougawa K., Uemoto M., Yokofuji A., Suzuri R., Nishitani A.,
RA Kohchi T.;
RT "The phytochrome-interacting VASCULAR PLANT ONE-ZINC FINGER1 and VOZ2
RT redundantly regulate flowering in Arabidopsis.";
RL Plant Cell 24:3248-3263(2012).
CC -!- FUNCTION: Transcriptional activator acting positively in the
CC phytochrome B signaling pathway. Functions redundantly with VOZ1 to
CC promote flowering downstream of phytochrome B (phyB). Down-regulates
CC 'FLOWERING LOCUS C' (FLC) and up-regulates 'FLOWERING LOCUS T' (FT).
CC Binds to the 38-bp cis-acting region of the AVP1 gene. Binds as a dimer
CC to the palindromic sequence 5'-GCGTNNNNNNNACGC-3'. Interacts with phyB
CC in the cytoplasm and is translocated to the nucleus at signal
CC transmission, where it is subjected to degradation in a phytochrome-
CC dependent manner. {ECO:0000269|PubMed:15295067,
CC ECO:0000269|PubMed:22904146}.
CC -!- SUBUNIT: Homodimer. Interacts with phytochrome B (phyB).
CC {ECO:0000269|PubMed:15295067, ECO:0000269|PubMed:22904146}.
CC -!- INTERACTION:
CC Q9SLB9; P14713: PHYB; NbExp=4; IntAct=EBI-6306942, EBI-300727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22904146}. Nucleus
CC {ECO:0000269|PubMed:22904146}. Note=Cytoplasmic in darkness, and
CC translocated to the nucleus depending on the light quality mediated by
CC phytochromes.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the vascular bundles and
CC mesophyll cells of various tissues. Expressed in the root, especially
CC in the root tip. Also detected in stamen filaments, stipules and
CC anthers. {ECO:0000269|PubMed:15295067, ECO:0000269|PubMed:22904146}.
CC -!- INDUCTION: By far-red light. Down-regulated by far-red light (at
CC protein level). {ECO:0000269|PubMed:22904146}.
CC -!- DOMAIN: The VOZ region includes a DNA-binding domain and a dimerization
CC domain. Contains an atypical zinc-finger followed by a basic region
CC structurally related to the NAC domain. {ECO:0000269|PubMed:15295067,
CC ECO:0000269|Ref.5}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:22904146}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Voz1 and voz2 double mutant
CC displays a late flowering phenotype under long-day conditions.
CC {ECO:0000269|PubMed:22904146}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB125257; BAD17858.1; -; mRNA.
DR EMBL; AC005956; AAD23723.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10117.1; -; Genomic_DNA.
DR EMBL; AF361831; AAK32843.1; -; mRNA.
DR EMBL; AY078048; AAL77749.1; -; mRNA.
DR PIR; E84853; E84853.
DR RefSeq; NP_565972.1; NM_129802.6.
DR AlphaFoldDB; Q9SLB9; -.
DR BioGRID; 4178; 5.
DR IntAct; Q9SLB9; 1.
DR STRING; 3702.AT2G42400.1; -.
DR PaxDb; Q9SLB9; -.
DR PRIDE; Q9SLB9; -.
DR ProteomicsDB; 242681; -.
DR EnsemblPlants; AT2G42400.1; AT2G42400.1; AT2G42400.
DR GeneID; 818841; -.
DR Gramene; AT2G42400.1; AT2G42400.1; AT2G42400.
DR KEGG; ath:AT2G42400; -.
DR Araport; AT2G42400; -.
DR TAIR; locus:2053786; AT2G42400.
DR eggNOG; ENOG502SKK8; Eukaryota.
DR HOGENOM; CLU_037371_1_0_1; -.
DR InParanoid; Q9SLB9; -.
DR OMA; EVGIPKC; -.
DR OrthoDB; 524603at2759; -.
DR PhylomeDB; Q9SLB9; -.
DR PRO; PR:Q9SLB9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLB9; baseline and differential.
DR Genevisible; Q9SLB9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0048578; P:positive regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR InterPro; IPR039277; VOZ1/VOZ2.
DR PANTHER; PTHR33873; PTHR33873; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Phytochrome signaling pathway; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..450
FT /note="Transcription factor VOZ2"
FT /id="PRO_0000420173"
FT ZN_FING 230..253
FT /note="C3H1-type; atypical"
FT /evidence="ECO:0000255"
FT REGION 91..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..418
FT /note="VOZ"
FT REGION 339..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT MUTAGEN 230
FT /note="C->A: Reduces DNA-binding ability."
FT /evidence="ECO:0000269|PubMed:15295067"
FT MUTAGEN 235
FT /note="C->A: Reduces DNA-binding ability."
FT /evidence="ECO:0000269|PubMed:15295067"
FT MUTAGEN 249
FT /note="C->A: Reduces DNA-binding ability."
FT /evidence="ECO:0000269|PubMed:15295067"
FT MUTAGEN 253
FT /note="H->A: Reduces DNA-binding ability."
FT /evidence="ECO:0000269|PubMed:15295067"
SQ SEQUENCE 450 AA; 50566 MW; 44DBE7B4AB689B95 CRC64;
MSNHPKITSA HQNVEEKLRE LQERFCHLQA ARKEGRHGDL ALLEAQISQN IREWQAELTA
PSPESSLLGE GISQFLEEFA PLLKLDEEDD ATSTLKEHAG AKPDPEGFSQ SLCPPEWTSE
NFSQSPFNGN FSCGFEDALN STETHGQQLH YGYEGFDPSI NSAPDFHDQK LSSNLDITSQ
YDYIFSEVRQ ELDNSPSTKL DSSEEIDNFA EFSTPSSVRV PPSAFLGPKC ALWDCTRPAQ
GSEWYLDYCS NYHGTLALNE DSPGTAPVLR PGGISLKDNL LIDALRAKTQ GKNVGIPVCE
GAVNTKCPWN AAELFHLELV EGETIREWLF FDKPRRAYDS GNRKQRSLPD YSGRGWHESR
KQLMKEQEGQ KRSYYMDPQP PGPFEWHLFE YQINESDACA LYRLELKVGN GKKSPKGKIS
KDPLADLQKK MGQFKVASDK PSPPTKGRKE
