ZAT3_ARATH
ID ZAT3_ARATH Reviewed; 284 AA.
AC O65499; A0MFC0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Zinc finger protein ZAT3 {ECO:0000305};
DE AltName: Full=Protein DUO1-ACTIVATED ZINC FINGER 2 {ECO:0000303|PubMed:21285328};
GN Name=ZAT3 {ECO:0000305}; Synonyms=DAZ2 {ECO:0000303|PubMed:21285328};
GN OrderedLocusNames=At4g35280 {ECO:0000312|Araport:AT4G35280};
GN ORFNames=F23E12.160 {ECO:0000312|EMBL:CAB80245.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION.
RX PubMed=21285328; DOI=10.1105/tpc.110.081059;
RA Borg M., Brownfield L., Khatab H., Sidorova A., Lingaya M., Twell D.;
RT "The R2R3 MYB transcription factor DUO1 activates a male germline-specific
RT regulon essential for sperm cell differentiation in Arabidopsis.";
RL Plant Cell 23:534-549(2011).
RN [6]
RP FUNCTION, INTERACTION WITH TPL, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RX PubMed=24876252; DOI=10.1105/tpc.114.124743;
RA Borg M., Rutley N., Kagale S., Hamamura Y., Gherghinoiu M., Kumar S.,
RA Sari U., Esparza-Franco M.A., Sakamoto W., Rozwadowski K., Higashiyama T.,
RA Twell D.;
RT "An EAR-dependent regulatory module promotes male germ cell division and
RT sperm fertility in Arabidopsis.";
RL Plant Cell 26:2098-2113(2014).
CC -!- FUNCTION: Mediates the regulation of male germ cell division by DUO1.
CC {ECO:0000269|PubMed:24876252}.
CC -!- SUBUNIT: Interacts (via the EAR motif) with TPL.
CC {ECO:0000269|PubMed:24876252}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24876252}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in pollen.
CC {ECO:0000269|PubMed:24876252}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the germ cells following microspore
CC division, increases during development and persists into mature pollen.
CC {ECO:0000269|PubMed:24876252}.
CC -!- INDUCTION: Activated by the transcription factor DUO1.
CC {ECO:0000269|PubMed:21285328}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28666.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL022604; CAA18741.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80245.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86489.1; -; Genomic_DNA.
DR EMBL; DQ446896; ABE66112.1; -; mRNA.
DR EMBL; DQ653246; ABK28666.1; ALT_SEQ; mRNA.
DR EMBL; AB493719; BAH30557.1; -; mRNA.
DR PIR; T06129; T06129.
DR RefSeq; NP_195254.1; NM_119694.2.
DR AlphaFoldDB; O65499; -.
DR BioGRID; 14963; 3.
DR IntAct; O65499; 2.
DR STRING; 3702.AT4G35280.1; -.
DR PaxDb; O65499; -.
DR PRIDE; O65499; -.
DR ProteomicsDB; 242962; -.
DR EnsemblPlants; AT4G35280.1; AT4G35280.1; AT4G35280.
DR GeneID; 829681; -.
DR Gramene; AT4G35280.1; AT4G35280.1; AT4G35280.
DR KEGG; ath:AT4G35280; -.
DR Araport; AT4G35280; -.
DR TAIR; locus:2122118; AT4G35280.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_059470_0_0_1; -.
DR InParanoid; O65499; -.
DR OMA; RCHWERG; -.
DR OrthoDB; 1483015at2759; -.
DR PhylomeDB; O65499; -.
DR PRO; PR:O65499; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65499; baseline and differential.
DR Genevisible; O65499; 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:0048235; P:pollen sperm cell differentiation; IEP: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; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..284
FT /note="Zinc finger protein ZAT3"
FT /id="PRO_0000409712"
FT ZN_FING 77..99
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 162..184
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 222..244
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 31362 MW; 9E9DAAA4DC7EE89A CRC64;
MNNNHSYDDR SFHIPLHPSN TSNPNPNLQF ALSSSYDHSP KKKRTKTVAS SSSSSPKSAS
KPKYTKKPDP NAPKITRPCT ECGRKFWSWK ALFGHMRCHP ERQWRGINPP PNYRVPTAAS
SKQLNQILPN WVSFMSEEDH EVASCLLMLS NGTPSSSSIE RFECGGCKKV FGSHQALGGH
RASHKNVKGC FAITNVTDDP MTVSTSSGHD HQGKILTFSG HHKCNICFRV FSSGQALGGH
MRCHWEKEEE PMISGALDLN VPPTIQDLST SDTSGCCLDL RLGL
