AZF2_ARATH
ID AZF2_ARATH Reviewed; 273 AA.
AC Q9SSW2;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Zinc finger protein AZF2;
DE AltName: Full=Zinc-finger protein 2;
GN Name=AZF2; Synonyms=ZF2; OrderedLocusNames=At3g19580;
GN ORFNames=MMB12.27, MMB12.4;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10806347; DOI=10.1016/s0378-1119(00)00133-5;
RA Sakamoto H., Araki T., Meshi T., Iwabuchi M.;
RT "Expression of a subset of the Arabidopsis Cys(2)/His(2)-type zinc-finger
RT protein gene family under water stress.";
RL Gene 248:23-32(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL Plant J. 23:115-122(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15333755; DOI=10.1104/pp.104.046599;
RA Sakamoto H., Maruyama K., Sakuma Y., Meshi T., Iwabuchi M., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Arabidopsis Cys2/His2-type zinc-finger proteins function as transcription
RT repressors under drought, cold, and high-salinity stress conditions.";
RL Plant Physiol. 136:2734-2746(2004).
RN [7]
RP FUNCTION.
RX PubMed=18216250; DOI=10.1073/pnas.0711203105;
RA Pauwels L., Morreel K., De Witte E., Lammertyn F., Van Montagu M.,
RA Boerjan W., Inze D., Goossens A.;
RT "Mapping methyl jasmonate-mediated transcriptional reprogramming of
RT metabolism and cell cycle progression in cultured Arabidopsis cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1380-1385(2008).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20619483; DOI=10.1016/j.jplph.2010.05.010;
RA Drechsel G., Raab S., Hoth S.;
RT "Arabidopsis zinc-finger protein 2 is a negative regulator of ABA signaling
RT during seed germination.";
RL J. Plant Physiol. 167:1418-1421(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21852415; DOI=10.1104/pp.111.182683;
RA Kodaira K.S., Qin F., Tran L.S., Maruyama K., Kidokoro S., Fujita Y.,
RA Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Arabidopsis Cys2/His2 zinc-finger proteins AZF1 and AZF2 negatively
RT regulate abscisic acid-repressive and auxin-inducible genes under abiotic
RT stress conditions.";
RL Plant Physiol. 157:742-756(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22709441; DOI=10.1111/j.1744-7909.2012.01136.x;
RA Li Z., Peng J., Wen X., Guo H.;
RT "Gene network analysis and functional studies of senescence-associated
RT genes reveal novel regulators of Arabidopsis leaf senescence.";
RL J. Integr. Plant Biol. 54:526-539(2012).
CC -!- FUNCTION: Transcriptional repressor involved in the inhibition of plant
CC growth under abiotic stress conditions. Can repress the expression of
CC various genes, including osmotic stress and abscisic acid-repressive
CC genes and auxin-inducible genes, by binding to their promoter regions
CC in a DNA sequence-specific manner. Acts as a negative regulator of
CC abscisic acid (ABA) signaling during seed germination. Probably
CC involved in jasmonate (JA) early signaling response. May regulate the
CC expression of the JA biosynthesis gene LOX3 and control the expression
CC of TIFY10A/JAZ1, a key repressor in the JA signaling cascade. May act
CC as a positive regulator of leaf senescence. Has been identified as a
CC suppressor of the deficiency of yeast snf4 mutant to grow on non-
CC fermentable carbon source. {ECO:0000269|PubMed:10929106,
CC ECO:0000269|PubMed:15333755, ECO:0000269|PubMed:18216250,
CC ECO:0000269|PubMed:20619483, ECO:0000269|PubMed:21852415,
CC ECO:0000269|PubMed:22709441}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15333755,
CC ECO:0000269|PubMed:21852415}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, radicles, cotyledons,
CC hypocotyls, leaf veins, stems, sepals, petals, stamens, placenta,
CC funiculi and maturated seeds. {ECO:0000269|PubMed:10806347,
CC ECO:0000269|PubMed:15333755, ECO:0000269|PubMed:20619483}.
CC -!- INDUCTION: By abscisic acid (ABA), ethylene, salt, cold, dehydration
CC and the monovalent and divalent cations Li(+), Na(+), K(+), Cs(+),
CC Ca(2+) and Mg(2+). {ECO:0000269|PubMed:10806347,
CC ECO:0000269|PubMed:15333755, ECO:0000269|PubMed:20619483,
CC ECO:0000269|PubMed:21852415}.
CC -!- DISRUPTION PHENOTYPE: Delayed senescence and hypersensitivity to ABA
CC during seed germination. {ECO:0000269|PubMed:20619483,
CC ECO:0000269|PubMed:22709441}.
CC -!- MISCELLANEOUS: Plants overexpressing AZF2 have increased sensitivity to
CC salt stress and barely survive under high salt conditons.
CC {ECO:0000305|PubMed:21852415}.
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DR EMBL; AB030730; BAA85107.1; -; Genomic_DNA.
DR EMBL; AF250337; AAG10143.1; -; mRNA.
DR EMBL; AP000417; BAB02542.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76261.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76262.1; -; Genomic_DNA.
DR EMBL; BT003816; AAO41869.1; -; mRNA.
DR PIR; T52385; T52385.
DR RefSeq; NP_001118663.1; NM_001125191.1.
DR RefSeq; NP_188592.1; NM_112848.2.
DR AlphaFoldDB; Q9SSW2; -.
DR BioGRID; 6828; 1.
DR STRING; 3702.AT3G19580.1; -.
DR PaxDb; Q9SSW2; -.
DR PRIDE; Q9SSW2; -.
DR ProteomicsDB; 241166; -.
DR EnsemblPlants; AT3G19580.1; AT3G19580.1; AT3G19580.
DR EnsemblPlants; AT3G19580.2; AT3G19580.2; AT3G19580.
DR GeneID; 821495; -.
DR Gramene; AT3G19580.1; AT3G19580.1; AT3G19580.
DR Gramene; AT3G19580.2; AT3G19580.2; AT3G19580.
DR KEGG; ath:AT3G19580; -.
DR Araport; AT3G19580; -.
DR TAIR; locus:2091201; AT3G19580.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_059471_1_2_1; -.
DR OMA; HRGFIDL; -.
DR OrthoDB; 1395906at2759; -.
DR PhylomeDB; Q9SSW2; -.
DR PRO; PR:Q9SSW2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SSW2; baseline and differential.
DR Genevisible; Q9SSW2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEP:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR InterPro; IPR044653; AZF1/2/3-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45988; PTHR45988; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; DNA-binding;
KW Jasmonic acid signaling pathway; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..273
FT /note="Zinc finger protein AZF2"
FT /id="PRO_0000421827"
FT ZN_FING 106..128
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 165..187
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 33..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 29796 MW; 010930062AAE70C9 CRC64;
MALEAMNTPT SSFTRIETKE DLMNDAVFIE PWLKRKRSKR QRSHSPSSSS SSPPRSRPKS
QNQDLTEEEY LALCLLMLAK DQPSQTRFHQ QSQSLTPPPE SKNLPYKCNV CEKAFPSYQA
LGGHKASHRI KPPTVISTTA DDSTAPTISI VAGEKHPIAA SGKIHECSIC HKVFPTGQAL
GGHKRCHYEG NLGGGGGGGS KSISHSGSVS STVSEERSHR GFIDLNLPAL PELSLHHNPI
VDEEILSPLT GKKPLLLTDH DQVIKKEDLS LKI
