位置:首页 > 蛋白库 > VOZ1_ARATH
VOZ1_ARATH
ID   VOZ1_ARATH              Reviewed;         486 AA.
AC   Q9SGQ0; B9DG33; Q9SHP3;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Transcription factor VOZ1;
DE   AltName: Full=Protein VASCULAR PLANT ONE-ZINC FINGER 1;
DE            Short=AtVOZ1;
GN   Name=VOZ1; OrderedLocusNames=At1g28520; ORFNames=F1K23.24, F3M18.4;
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, AND TISSUE
RP   SPECIFICITY.
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=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   [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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478.
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   [7]
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   [8]
RP   DNA-BINDING.
RX   PubMed=19995345; DOI=10.1042/bj20091234;
RA   Jensen M.K., Kjaersgaard T., Nielsen M.M., Galberg P., Petersen K.,
RA   O'Shea C., Skriver K.;
RT   "The Arabidopsis thaliana NAC transcription factor family: structure-
RT   function relationships and determinants of ANAC019 stress signalling.";
RL   Biochem. J. 426:183-196(2010).
RN   [9]
RP   INTERACTION WITH PHYB, DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY,
RP   AND INDUCTION.
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 VOZ2 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. Interacts with
CC       phyB 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 (By similarity). Interacts with phytochrome B
CC       (phyB). {ECO:0000250, ECO:0000269|PubMed:22904146}.
CC   -!- INTERACTION:
CC       Q9SGQ0; P14713: PHYB; NbExp=4; IntAct=EBI-6306928, EBI-300727;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Cytoplasmic in darkness, and translocated to the nucleus depending
CC       on the light quality mediated by phytochromes. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the vascular bundles of
CC       various tissues, specifically in the phloem.
CC       {ECO:0000269|PubMed:15295067, ECO:0000269|PubMed:22904146}.
CC   -!- INDUCTION: By far-red light. {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.7}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24553.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AB125256; BAD17857.1; -; mRNA.
DR   EMBL; AC007508; AAF24553.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC010155; AAF16771.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30986.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30987.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58935.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58936.1; -; Genomic_DNA.
DR   EMBL; BT020261; AAV84482.1; -; mRNA.
DR   EMBL; AK227014; BAE99078.1; -; mRNA.
DR   EMBL; AK317006; BAH19700.1; -; mRNA.
DR   PIR; B86411; B86411.
DR   RefSeq; NP_001077618.1; NM_001084149.1.
DR   RefSeq; NP_001319100.1; NM_001332816.1.
DR   RefSeq; NP_001321335.1; NM_001332818.1.
DR   RefSeq; NP_174174.1; NM_102620.5.
DR   AlphaFoldDB; Q9SGQ0; -.
DR   SMR; Q9SGQ0; -.
DR   BioGRID; 24987; 13.
DR   IntAct; Q9SGQ0; 5.
DR   STRING; 3702.AT1G28520.1; -.
DR   PaxDb; Q9SGQ0; -.
DR   PRIDE; Q9SGQ0; -.
DR   ProteomicsDB; 242701; -.
DR   EnsemblPlants; AT1G28520.1; AT1G28520.1; AT1G28520.
DR   EnsemblPlants; AT1G28520.2; AT1G28520.2; AT1G28520.
DR   EnsemblPlants; AT1G28520.4; AT1G28520.4; AT1G28520.
DR   EnsemblPlants; AT1G28520.5; AT1G28520.5; AT1G28520.
DR   GeneID; 839752; -.
DR   Gramene; AT1G28520.1; AT1G28520.1; AT1G28520.
DR   Gramene; AT1G28520.2; AT1G28520.2; AT1G28520.
DR   Gramene; AT1G28520.4; AT1G28520.4; AT1G28520.
DR   Gramene; AT1G28520.5; AT1G28520.5; AT1G28520.
DR   KEGG; ath:AT1G28520; -.
DR   Araport; AT1G28520; -.
DR   TAIR; locus:2018738; AT1G28520.
DR   eggNOG; ENOG502QPN5; Eukaryota.
DR   HOGENOM; CLU_037371_1_0_1; -.
DR   InParanoid; Q9SGQ0; -.
DR   OMA; ECKNTPL; -.
DR   OrthoDB; 524603at2759; -.
DR   PhylomeDB; Q9SGQ0; -.
DR   PRO; PR:Q9SGQ0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SGQ0; baseline and differential.
DR   Genevisible; Q9SGQ0; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0009631; P:cold acclimation; IGI:CACAO.
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:0009408; P:response to heat; IGI:CACAO.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IGI:CACAO.
DR   InterPro; IPR039277; VOZ1/VOZ2.
DR   PANTHER; PTHR33873; PTHR33873; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Phytochrome signaling pathway; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..486
FT                   /note="Transcription factor VOZ1"
FT                   /id="PRO_0000420172"
FT   ZN_FING         217..240
FT                   /note="C3H1-type; atypical"
FT                   /evidence="ECO:0000255"
FT   REGION          208..405
FT                   /note="VOZ"
FT   REGION          424..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        474
FT                   /note="N -> K (in Ref. 6; BAH19700)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  54080 MW;  9BA92951E2128858 CRC64;
     MTGKRSKTNC RSASHKLFKD KAKNRVDDLQ GMLLDLQFAR KESRPTDVTL LEEQVNQMLR
     EWKSELNEPS PASSLQQGGT LGSFSSDICR LLQLCDEEDD ATSKLAAPKP EPADQNLEAG
     KAAVFQRGYN LVQGKSEHGL PLVDNCKDLS LAAGNNFDGT APLEYHQQYD LQQEFEPNFN
     GGFNNCPSYG VVEGPIHISN FIPTICPPPS AFLGPKCALW DCPRPAQGFD WFQDYCSSFH
     AALAFNEGPP GMNPVVRPGG IGLKDGLLFA ALSAKAGGKD VGIPECEGAA TAKSPWNAPE
     LFDLTVLESE TLREWLFFDK PRRAFESGNR KQRSLPDYNG RGWHESRKQI MVEFGGLKRS
     YYMDPQPLHH FEWHLYEYEI NKCDACALYR LELKLVDGKK TSKGKVSNDS VADLQKQMGR
     LTAEFPPENN TTNTTNNNKR CIKGRPKVST KVATGNVQNT VEQANDYGVG EEFNYLVGNL
     SDYYIP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024