ZAT5_ARATH
ID ZAT5_ARATH Reviewed; 286 AA.
AC Q681X4; Q42375; Q9SL35;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc finger protein ZAT5;
GN Name=ZAT5; OrderedLocusNames=At2g28200; ORFNames=T3B23.13;
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 / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9132053; DOI=10.1023/a:1005746803089;
RA Meissner R., Michael A.J.;
RT "Isolation and characterisation of a diverse family of Arabidopsis two and
RT three-fingered protein genes and cDNA's.";
RL Plant Mol. Biol. 33:615-624(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 INDUCTION BY GIBBERELLIN.
RX PubMed=12837949; DOI=10.1105/tpc.011650;
RA Ogawa M., Hanada A., Yamauchi Y., Kuwahara A., Kamiya Y., Yamaguchi S.;
RT "Gibberellin biosynthesis and response during Arabidopsis seed
RT germination.";
RL Plant Cell 15:1591-1604(2003).
RN [7]
RP INDUCTION.
RX PubMed=16244149; DOI=10.1104/pp.105.067686;
RA Pavet V., Olmos E., Kiddle G., Mowla S., Kumar S., Antoniw J.,
RA Alvarez M.E., Foyer C.H.;
RT "Ascorbic acid deficiency activates cell death and disease resistance
RT responses in Arabidopsis.";
RL Plant Physiol. 139:1291-1303(2005).
CC -!- FUNCTION: Probable transcription factor that may be involved in stress
CC responses. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC {ECO:0000269|PubMed:9132053}.
CC -!- INDUCTION: By gibberellin and H(2)O(2). Down-regulated by ascorbate.
CC {ECO:0000269|PubMed:12837949, ECO:0000269|PubMed:16244149}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29833.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA67233.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA67236.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X98675; CAA67233.1; ALT_INIT; Genomic_DNA.
DR EMBL; X98678; CAA67236.1; ALT_INIT; mRNA.
DR EMBL; AC006202; AAD29833.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08090.1; -; Genomic_DNA.
DR EMBL; AK175493; BAD43256.1; -; mRNA.
DR EMBL; AK229812; BAF01643.1; -; mRNA.
DR PIR; A84682; A84682.
DR RefSeq; NP_180387.2; NM_128380.5.
DR AlphaFoldDB; Q681X4; -.
DR BioGRID; 2716; 3.
DR IntAct; Q681X4; 3.
DR STRING; 3702.AT2G28200.1; -.
DR iPTMnet; Q681X4; -.
DR PaxDb; Q681X4; -.
DR PRIDE; Q681X4; -.
DR ProteomicsDB; 242979; -.
DR EnsemblPlants; AT2G28200.1; AT2G28200.1; AT2G28200.
DR GeneID; 817366; -.
DR Gramene; AT2G28200.1; AT2G28200.1; AT2G28200.
DR KEGG; ath:AT2G28200; -.
DR Araport; AT2G28200; -.
DR TAIR; locus:2046153; AT2G28200.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_059471_0_0_1; -.
DR InParanoid; Q681X4; -.
DR OMA; HFKVSGP; -.
DR OrthoDB; 1366946at2759; -.
DR PhylomeDB; Q681X4; -.
DR PRO; PR:Q681X4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q681X4; baseline and differential.
DR Genevisible; Q681X4; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..286
FT /note="Zinc finger protein ZAT5"
FT /id="PRO_0000409714"
FT ZN_FING 115..137
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 190..212
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 262
FT /note="E -> G (in Ref. 1; CAA67233/CAA67236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31047 MW; ACD5506F5232F119 CRC64;
MMMGQDEVGS DQTQIIKGKR TKRQRSSSTF VVTAATTVTS TSSSAGGSGG ERAVSDEYNS
AVSSPVTTDC TQEEEDMAIC LIMLARGTVL PSPDLKNSRK IHQKISSENS SFYVYECKTC
NRTFSSFQAL GGHRASHKKP RTSTEEKTRL PLTQPKSSAS EEGQNSHFKV SGSALASQAS
NIINKANKVH ECSICGSEFT SGQALGGHMR RHRTAVTTIS PVAATAEVSR NSTEEEIEIN
IGRSMEQQRK YLPLDLNLPA PEDDLRESKF QGIVFSATPA LIDCHY
