ID   GATA3_MOUSE             Reviewed;         443 AA.
AC   P23772;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Trans-acting T-cell-specific transcription factor GATA-3;
DE   AltName: Full=GATA-binding factor 3;
GN   Name=Gata3; Synonyms=Gata-3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2017177; DOI=10.1128/mcb.11.5.2778-2784.1991;
RA   Ko L.J., Yamamoto M., Leonard M.W., George K.M., Ting P., Engel J.D.;
RT   "Murine and human T-lymphocyte GATA-3 factors mediate transcription through
RT   a cis-regulatory element within the human T-cell receptor delta gene
RT   enhancer.";
RL   Mol. Cell. Biol. 11:2778-2784(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH TBX21, AND SUBCELLULAR LOCATION.
RX   PubMed=15662016; DOI=10.1126/science.1103336;
RA   Hwang E.S., Szabo S.J., Schwartzberg P.L., Glimcher L.H.;
RT   "T helper cell fate specified by kinase-mediated interaction of T-bet with
RT   GATA-3.";
RL   Science 307:430-433(2005).
RN   [4]
RP   FUNCTION, YXKXHXXXRP MOTIF, AND MUTAGENESIS OF TYR-344; LYS-346; HIS-348;
RP   ARG-352 AND PRO-353.
RX   PubMed=17056504; DOI=10.4049/jimmunol.177.9.5801;
RA   Shinnakasu R., Yamashita M., Shinoda K., Endo Y., Hosokawa H., Hasegawa A.,
RA   Ikemizu S., Nakayama T.;
RT   "Critical YxKxHxxxRP motif in the C-terminal region of GATA3 for its DNA
RT   binding and function.";
RL   J. Immunol. 177:5801-5810(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   INTERACTION WITH TBX21.
RX   PubMed=21690296; DOI=10.1128/mcb.05383-11;
RA   Chen A., Lee S.M., Gao B., Shannon S., Zhu Z., Fang D.;
RT   "c-Abl-mediated tyrosine phosphorylation of the T-bet DNA-binding domain
RT   regulates CD4+ T-cell differentiation and allergic lung inflammation.";
RL   Mol. Cell. Biol. 31:3445-3456(2011).
RN   [7]
RP   INTERACTION WITH TBX21.
RX   PubMed=23616576; DOI=10.4049/jimmunol.1203403;
RA   Jang E.J., Park H.R., Hong J.H., Hwang E.S.;
RT   "Lysine 313 of T-box is crucial for modulation of protein stability, DNA
RT   binding, and threonine phosphorylation of T-bet.";
RL   J. Immunol. 190:5764-5770(2013).
RN   [8]
RP   FUNCTION.
RX   PubMed=31175139; DOI=10.1158/2326-6066.cir-18-0562;
RA   Spinner C.A., Lamsoul I., Metais A., Febrissy C., Moog-Lutz C., Lutz P.G.;
RT   "The E3 Ubiquitin Ligase Asb2alpha in T Helper 2 Cells Negatively Regulates
RT   Antitumor Immunity in Colorectal Cancer.";
RL   Cancer Immunol. Res. 7:1332-1344(2019).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY IL33.
RX   PubMed=34644537; DOI=10.1016/j.immuni.2021.09.010;
RA   Faas M., Ipseiz N., Ackermann J., Culemann S., Grueneboom A., Schroeder F.,
RA   Rothe T., Scholtysek C., Eberhardt M., Boettcher M., Kirchner P., Stoll C.,
RA   Ekici A., Fuchs M., Kunz M., Weigmann B., Wirtz S., Lang R., Hofmann J.,
RA   Vera J., Voehringer D., Michelucci A., Mougiakakos D., Uderhardt S.,
RA   Schett G., Kroenke G.;
RT   "IL-33-induced metabolic reprogramming controls the differentiation of
RT   alternatively activated macrophages and the resolution of inflammation.";
RL   Immunity 54:2531-2546.e5(2021).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 308-370 IN COMPLEX WITH DNA, AND
RP   DOMAIN.
RX   PubMed=18621058; DOI=10.1016/j.jmb.2008.06.072;
RA   Bates D.L., Chen Y., Kim G., Guo L., Chen L.;
RT   "Crystal structures of multiple GATA zinc fingers bound to DNA reveal new
RT   insights into DNA recognition and self-association by GATA.";
RL   J. Mol. Biol. 381:1292-1306(2008).
CC   -!- FUNCTION: Transcriptional activator which binds to the enhancer of the
CC       T-cell receptor alpha and delta genes. Binds to the consensus sequence
CC       5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process
CC       following immune and inflammatory responses. Positively regulates ASB2
CC       expression (PubMed:31175139). Coordinates macrophage transcriptional
CC       activation and UCP2-dependent metabolic reprogramming in response to
CC       IL33. Upon tissue injury, acts downstream of IL33 signaling to drive
CC       differentiation of inflammation-resolving alternatively activated
CC       macrophages. {ECO:0000269|PubMed:17056504, ECO:0000269|PubMed:31175139,
CC       ECO:0000269|PubMed:34644537}.
CC   -!- SUBUNIT: Interacts with TBX21 ('Tyr-525' phosphorylated form).
CC       {ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296,
CC       ECO:0000269|PubMed:23616576}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15662016,
CC       ECO:0000269|PubMed:34644537}.
CC   -!- TISSUE SPECIFICITY: T-cell specific.
CC   -!- INDUCTION: Up-regulated during macrophage differentiation in response
CC       to IL33. {ECO:0000269|PubMed:34644537}.
CC   -!- DOMAIN: Binds DNA via the 2 GATA-type zinc fingers. Each zinc finger
CC       may bind either adjacent sites in a palindromic motif, or a different
CC       DNA molecule allowing looping and long-range gene regulation (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The YxKxHxxxRP motif is critical for DNA-binding and function.
CC       {ECO:0000269|PubMed:18621058}.
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DR   EMBL; X55123; CAA38917.1; -; mRNA.
DR   EMBL; BC062915; AAH62915.1; -; mRNA.
DR   CCDS; CCDS15674.1; -.
DR   PIR; B39794; B39794.
DR   RefSeq; NP_032117.1; NM_008091.3.
DR   RefSeq; XP_006497417.1; XM_006497354.1.
DR   PDB; 3DFV; X-ray; 3.10 A; C/D=308-370.
DR   PDB; 3DFX; X-ray; 2.70 A; A/B=308-370.
DR   PDBsum; 3DFV; -.
DR   PDBsum; 3DFX; -.
DR   AlphaFoldDB; P23772; -.
DR   SMR; P23772; -.
DR   BioGRID; 199840; 9.
DR   DIP; DIP-29712N; -.
DR   IntAct; P23772; 4.
DR   STRING; 10090.ENSMUSP00000100041; -.
DR   iPTMnet; P23772; -.
DR   PhosphoSitePlus; P23772; -.
DR   jPOST; P23772; -.
DR   PaxDb; 10090-ENSMUSP00000100041; -.
DR   ProteomicsDB; 271635; -.
DR   Antibodypedia; 11113; 1339 antibodies from 49 providers.
DR   DNASU; 14462; -.
DR   Ensembl; ENSMUST00000102976.4; ENSMUSP00000100041.4; ENSMUSG00000015619.11.
DR   GeneID; 14462; -.
DR   KEGG; mmu:14462; -.
DR   UCSC; uc008ihf.1; mouse.
DR   AGR; MGI:95663; -.
DR   CTD; 2625; -.
DR   MGI; MGI:95663; Gata3.
DR   VEuPathDB; HostDB:ENSMUSG00000015619; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   GeneTree; ENSGT00940000159247; -.
DR   HOGENOM; CLU_027524_1_0_1; -.
DR   InParanoid; P23772; -.
DR   OMA; ECVKYQV; -.
DR   OrthoDB; 685518at2759; -.
DR   PhylomeDB; P23772; -.
DR   TreeFam; TF315391; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 14462; 2 hits in 82 CRISPR screens.
DR   ChiTaRS; Gata3; mouse.
DR   EvolutionaryTrace; P23772; -.
DR   PRO; PR:P23772; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P23772; Protein.
DR   Bgee; ENSMUSG00000015619; Expressed in urinary bladder urothelium and 217 other cell types or tissues.
DR   ExpressionAtlas; P23772; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI.
DR   GO; GO:0071837; F:HMG box domain binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0005134; F:interleukin-2 receptor binding; IPI:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IMP:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0061290; P:canonical Wnt signaling pathway involved in metanephric kidney development; IMP:UniProtKB.
DR   GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:UniProtKB.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0001775; P:cell activation; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0001709; P:cell fate determination; IDA:MGI.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IDA:MGI.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; IEA:Ensembl.
DR   GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0043583; P:ear development; ISS:UniProtKB.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR   GO; GO:0030218; P:erythrocyte differentiation; IDA:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR   GO; GO:0006959; P:humoral immune response; IMP:MGI.
DR   GO; GO:0002520; P:immune system development; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; ISO:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   GO; GO:0072676; P:lymphocyte migration; ISS:UniProtKB.
DR   GO; GO:0030225; P:macrophage differentiation; IMP:UniProtKB.
DR   GO; GO:0008584; P:male gonad development; IMP:UniProtKB.
DR   GO; GO:0060374; P:mast cell differentiation; IDA:MGI.
DR   GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
DR   GO; GO:0001823; P:mesonephros development; IMP:MGI.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI.
DR   GO; GO:2000146; P:negative regulation of cell motility; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:2000607; P:negative regulation of cell proliferation involved in mesonephros development; IMP:UniProtKB.
DR   GO; GO:1901536; P:negative regulation of DNA demethylation; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR   GO; GO:2000703; P:negative regulation of fibroblast growth factor receptor signaling pathway involved in ureteric bud formation; IMP:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:2000734; P:negative regulation of glial cell-derived neurotrophic factor receptor signaling pathway involved in ureteric bud formation; IMP:UniProtKB.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:MGI.
DR   GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0032689; P:negative regulation of type II interferon production; IDA:MGI.
DR   GO; GO:0072179; P:nephric duct formation; IMP:UniProtKB.
DR   GO; GO:0072178; P:nephric duct morphogenesis; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:MGI.
DR   GO; GO:0071599; P:otic vesicle development; IMP:MGI.
DR   GO; GO:0060017; P:parathyroid gland development; IMP:MGI.
DR   GO; GO:0035898; P:parathyroid hormone secretion; IMP:MGI.
DR   GO; GO:0060037; P:pharyngeal system development; IMP:UniProtKB.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:UniProtKB.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR   GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:MGI.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:MGI.
DR   GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:MGI.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0009967; P:positive regulation of signal transduction; ISS:UniProtKB.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:UniProtKB.
DR   GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:MGI.
DR   GO; GO:2000611; P:positive regulation of thyroid hormone generation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:UniProtKB.
DR   GO; GO:0072107; P:positive regulation of ureteric bud formation; IMP:UniProtKB.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0002572; P:pro-T cell differentiation; IMP:MGI.
DR   GO; GO:2000683; P:regulation of cellular response to X-ray; ISS:UniProtKB.
DR   GO; GO:0001817; P:regulation of cytokine production; IDA:MGI.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; IBA:GO_Central.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; IDA:MGI.
DR   GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; IMP:UniProtKB.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
DR   GO; GO:0045622; P:regulation of T-helper cell differentiation; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR   GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI.
DR   GO; GO:0030217; P:T cell differentiation; IDA:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045064; P:T-helper 2 cell differentiation; IDA:MGI.
DR   GO; GO:0045061; P:thymic T cell selection; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0035799; P:ureter maturation; IMP:MGI.
DR   GO; GO:0072197; P:ureter morphogenesis; IGI:MGI.
DR   GO; GO:0060676; P:ureteric bud formation; IMP:UniProtKB.
DR   GO; GO:0060065; P:uterus development; IMP:UniProtKB.
DR   GO; GO:0003281; P:ventricular septum development; IMP:UniProtKB.
DR   CDD; cd00202; ZnF_GATA; 2.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 2.
DR   InterPro; IPR016374; TF_GATA-2/3.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071:SF106; TRANS-ACTING T-CELL-SPECIFIC TRANSCRIPTION FACTOR GATA-3; 1.
DR   PANTHER; PTHR10071; TRANSCRIPTION FACTOR GATA FAMILY MEMBER; 1.
DR   Pfam; PF00320; GATA; 2.
DR   PIRSF; PIRSF003027; TF_GATA-1/2/3; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
DR   Genevisible; P23772; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Immunity; Innate immunity;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..443
FT                   /note="Trans-acting T-cell-specific transcription factor
FT                   GATA-3"
FT                   /id="PRO_0000083409"
FT   ZN_FING         263..287
FT                   /note="GATA-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   ZN_FING         317..341
FT                   /note="GATA-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          1..257
FT                   /note="Interaction with TBX21"
FT                   /evidence="ECO:0000269|PubMed:15662016"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..316
FT                   /note="Flexible linker"
FT                   /evidence="ECO:0000250"
FT   REGION          412..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           344..353
FT                   /note="YxKxHxxxRP"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23771"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         344
FT                   /note="Y->A: Dramatically decreased Th2 cell
FT                   differentiation."
FT                   /evidence="ECO:0000269|PubMed:17056504"
FT   MUTAGEN         346
FT                   /note="K->A: Moderately decreased Th2 cell
FT                   differentiation."
FT                   /evidence="ECO:0000269|PubMed:17056504"
FT   MUTAGEN         348
FT                   /note="H->A: Dramatically decreased Th2 cell
FT                   differentiation."
FT                   /evidence="ECO:0000269|PubMed:17056504"
FT   MUTAGEN         352
FT                   /note="R->A: Fails to induce Th2 cytokine production."
FT                   /evidence="ECO:0000269|PubMed:17056504"
FT   MUTAGEN         353
FT                   /note="P->A,K: Fails to induce Th2 cytokine production."
FT                   /evidence="ECO:0000269|PubMed:17056504"
FT   TURN            318..320
FT                   /evidence="ECO:0007829|PDB:3DFX"
FT   STRAND          326..330
FT                   /evidence="ECO:0007829|PDB:3DFV"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:3DFV"
FT   HELIX           339..348
FT                   /evidence="ECO:0007829|PDB:3DFX"
FT   HELIX           354..356
FT                   /evidence="ECO:0007829|PDB:3DFX"
SQ   SEQUENCE   443 AA;  47968 MW;  980E58FB9872E560 CRC64;
     MEVTADQPRW VSHHHPAVLN GQHPDTHHPG LGHSYMEAQY PLTEEVDVLF NIDGQGNHVP
     SYYGNSVRAT VQRYPPTHHG SQVCRPPLLH GSLPWLDGGK ALSSHHTASP WNLSPFSKTS
     IHHGSPGPLS VYPPASSSSL AAGHSSPHLF TFPPTPPKDV SPDPSLSTPG SAGSARQDEK
     ECLKYQVQLP DSMKLETSHS RGSMTTLGGA SSSAHHPITT YPPYVPEYSS GLFPPSSLLG
     GSPTGFGCKS RPKARSSTEG RECVNCGATS TPLWRRDGTG HYLCNACGLY HKMNGQNRPL
     IKPKRRLSAA RRAGTSCANC QTTTTTLWRR NANGDPVCNA CGLYYKLHNI NRPLTMKKEG
     IQTRNRKMSS KSKKCKKVHD ALEDFPKSSS FNPAALSRHM SSLSHISPFS HSSHMLTTPT
     PMHPPSGLSF GPHHPSSMVT AMG
//