GATA3_HUMAN
ID GATA3_HUMAN Reviewed; 443 AA.
AC P23771; Q5VWG7; Q5VWG8; Q96J16;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Trans-acting T-cell-specific transcription factor GATA-3;
DE AltName: Full=GATA-binding factor 3;
GN Name=GATA3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=2050118; DOI=10.1002/j.1460-2075.1991.tb07706.x;
RA Joulin V., Bories D., Eleouet J.-F., Labastie M.-C., Chretien S.,
RA Mattei M.-G., Romeo P.-H.;
RT "A T-cell specific TCR delta DNA binding protein is a member of the human
RT GATA family.";
RL EMBO J. 10:1809-1816(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=1827068; DOI=10.1002/j.1460-2075.1991.tb08059.x;
RA Ho I.-C., Vorhees P., Marin N., Oakley B.K., Tsai S.-F., Orkin S.H.,
RA Leiden J.M.;
RT "Human GATA-3: a lineage-restricted transcription factor that regulates the
RT expression of the T cell receptor alpha gene.";
RL EMBO J. 10:1187-1192(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1871134; DOI=10.1073/pnas.88.16.7284;
RA Marine J., Winoto A.;
RT "The human enhancer-binding protein Gata3 binds to several T-cell receptor
RT regulatory elements.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7284-7288(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-242.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, and Placenta;
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 [9]
RP INVOLVEMENT IN HDR.
RX PubMed=10935639; DOI=10.1038/35019088;
RA Van Esch H., Groenen P., Nesbit M.A., Schuffenhauer S., Lichtner P.,
RA Vanderlinden G., Harding B., Beetz R., Bilous R.W., Holdaway I., Shaw N.J.,
RA Fryns J.-P., Van de Ven W., Thakker R.V., Devriendt K.;
RT "GATA3 haplo-insufficiency causes human HDR syndrome.";
RL Nature 406:419-422(2000).
RN [10]
RP INTERACTION WITH TBX21.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP FUNCTION.
RX PubMed=23824597; DOI=10.1371/journal.pone.0066468;
RA Sasaki T., Onodera A., Hosokawa H., Watanabe Y., Horiuchi S., Yamashita J.,
RA Tanaka H., Ogawa Y., Suzuki Y., Nakayama T.;
RT "Genome-wide gene expression profiling revealed a critical role for GATA3
RT in the maintenance of the Th2 cell identity.";
RL PLoS ONE 8:E66468-E66468(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 260-370 IN COMPLEX WITH DNA, AND
RP GATA-TYPE ZINC FINGERS.
RX PubMed=23142663; DOI=10.1016/j.celrep.2012.10.012;
RA Chen Y., Bates D.L., Dey R., Chen P.H., Machado A.C., Laird-Offringa I.A.,
RA Rohs R., Chen L.;
RT "DNA binding by GATA transcription factor suggests mechanisms of DNA
RT looping and long-range gene regulation.";
RL Cell Rep. 2:1197-1206(2012).
RN [14]
RP VARIANT HDR ARG-274.
RX PubMed=11389161; DOI=10.1136/jmg.38.6.374;
RA Muroya K., Hasegawa T., Ito Y., Nagai T., Isotani H., Iwata Y.,
RA Yamamoto K., Fujimoto S., Seishu S., Fukushima Y., Hasegawa Y., Ogata T.;
RT "GATA3 abnormalities and the phenotypic spectrum of HDR syndrome.";
RL J. Med. Genet. 38:374-380(2001).
RN [15]
RP VARIANT LEU-366.
RX PubMed=17224074; DOI=10.1186/bcr1637;
RA Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S.,
RA Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M.,
RA Boerresen-Dale A.-L.;
RT "Somatic sequence alterations in twenty-one genes selected by expression
RT profile analysis of breast carcinomas.";
RL Breast Cancer Res. 9:R5-R5(2007).
RN [16]
RP VARIANT HDR GLN-298, AND CHARACTERIZATION OF VARIANT HDR GLN-298.
RX PubMed=26514990; DOI=10.1186/s12902-015-0065-7;
RA Okawa T., Yoshida M., Usui T., Kudou T., Iwasaki Y., Fukuoka K.,
RA Takahashi N., Uehara Y., Oiso Y.;
RT "A novel loss-of-function mutation of GATA3 (p.R299Q) in a Japanese family
RT with Hypoparathyroidism, Deafness, and Renal Dysplasia (HDR) syndrome.";
RL BMC Endocr. Disord. 15:66-66(2015).
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 (By similarity). {ECO:0000250|UniProtKB:P23772,
CC ECO:0000269|PubMed:23824597}.
CC -!- SUBUNIT: Interacts with TBX21 ('Tyr-530' phosphorylated form).
CC {ECO:0000269|PubMed:15662016}.
CC -!- INTERACTION:
CC P23771; P35609: ACTN2; NbExp=3; IntAct=EBI-6664760, EBI-77797;
CC P23771; P28329-3: CHAT; NbExp=3; IntAct=EBI-6664760, EBI-25837549;
CC P23771; Q96KQ7: EHMT2; NbExp=20; IntAct=EBI-6664760, EBI-744366;
CC P23771; P22607: FGFR3; NbExp=3; IntAct=EBI-6664760, EBI-348399;
CC P23771; Q9NP62: GCM1; NbExp=9; IntAct=EBI-6664760, EBI-21194843;
CC P23771; O15379: HDAC3; NbExp=7; IntAct=EBI-6664760, EBI-607682;
CC P23771; Q9UQL6: HDAC5; NbExp=4; IntAct=EBI-6664760, EBI-715576;
CC P23771; Q16665: HIF1A; NbExp=3; IntAct=EBI-6664760, EBI-447269;
CC P23771; P06239: LCK; NbExp=3; IntAct=EBI-6664760, EBI-1348;
CC P23771; Q9BTC8: MTA3; NbExp=18; IntAct=EBI-6664760, EBI-2461787;
CC P23771; P25788: PSMA3; NbExp=3; IntAct=EBI-6664760, EBI-348380;
CC P23771; Q9UL17: TBX21; NbExp=6; IntAct=EBI-6664760, EBI-3922312;
CC P23771-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-6672518, EBI-3867333;
CC P23771-2; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-6672518, EBI-10210845;
CC P23771-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-6672518, EBI-11953846;
CC P23771-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-6672518, EBI-11962084;
CC P23771-2; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-6672518, EBI-949255;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23771-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23771-2; Sequence=VSP_001598;
CC -!- TISSUE SPECIFICITY: T-cells and endothelial cells.
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.
CC -!- DOMAIN: The YxKxHxxxRP motif is critical for DNA-binding and function.
CC {ECO:0000250}.
CC -!- DISEASE: Hypoparathyroidism, sensorineural deafness, and renal disease
CC (HDR) [MIM:146255]: A disease characterized by steroid-resistant
CC nephrosis with progressive renal failure, hypoparathyroidism,
CC sensorineural deafness, and renal dysplasia.
CC {ECO:0000269|PubMed:10935639, ECO:0000269|PubMed:11389161,
CC ECO:0000269|PubMed:26514990}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/gata3/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GATA3ID107ch10p14.html";
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DR EMBL; X58072; CAA41102.1; -; mRNA.
DR EMBL; X55037; CAA38877.1; -; mRNA.
DR EMBL; X55122; CAA38916.1; -; mRNA.
DR EMBL; M69106; AAA35870.1; -; mRNA.
DR EMBL; AY497006; AAR32096.1; -; Genomic_DNA.
DR EMBL; AL390294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86367.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86368.1; -; Genomic_DNA.
DR EMBL; BC003070; AAH03070.1; -; mRNA.
DR EMBL; BC006793; AAH06793.1; -; mRNA.
DR CCDS; CCDS31143.1; -. [P23771-2]
DR CCDS; CCDS7083.1; -. [P23771-1]
DR PIR; A39794; A39794.
DR RefSeq; NP_001002295.1; NM_001002295.1. [P23771-2]
DR RefSeq; NP_002042.1; NM_002051.2. [P23771-1]
DR RefSeq; XP_005252499.1; XM_005252442.2. [P23771-2]
DR RefSeq; XP_005252500.1; XM_005252443.4. [P23771-2]
DR PDB; 4HC7; X-ray; 2.65 A; A/B=260-370.
DR PDB; 4HC9; X-ray; 1.60 A; A=260-370.
DR PDB; 4HCA; X-ray; 2.80 A; A=260-370.
DR PDBsum; 4HC7; -.
DR PDBsum; 4HC9; -.
DR PDBsum; 4HCA; -.
DR AlphaFoldDB; P23771; -.
DR SMR; P23771; -.
DR BioGRID; 108895; 151.
DR DIP; DIP-61302N; -.
DR IntAct; P23771; 156.
DR MINT; P23771; -.
DR STRING; 9606.ENSP00000368632; -.
DR iPTMnet; P23771; -.
DR PhosphoSitePlus; P23771; -.
DR BioMuta; GATA3; -.
DR DMDM; 120962; -.
DR EPD; P23771; -.
DR jPOST; P23771; -.
DR MassIVE; P23771; -.
DR MaxQB; P23771; -.
DR PaxDb; P23771; -.
DR PeptideAtlas; P23771; -.
DR PRIDE; P23771; -.
DR ProteomicsDB; 54162; -. [P23771-1]
DR ProteomicsDB; 54163; -. [P23771-2]
DR Antibodypedia; 11113; 1043 antibodies from 49 providers.
DR DNASU; 2625; -.
DR Ensembl; ENST00000346208.4; ENSP00000341619.3; ENSG00000107485.18. [P23771-1]
DR Ensembl; ENST00000379328.9; ENSP00000368632.3; ENSG00000107485.18. [P23771-2]
DR GeneID; 2625; -.
DR KEGG; hsa:2625; -.
DR MANE-Select; ENST00000379328.9; ENSP00000368632.3; NM_001002295.2; NP_001002295.1. [P23771-2]
DR UCSC; uc001ijz.4; human. [P23771-1]
DR CTD; 2625; -.
DR DisGeNET; 2625; -.
DR GeneCards; GATA3; -.
DR HGNC; HGNC:4172; GATA3.
DR HPA; ENSG00000107485; Tissue enhanced (parathyroid gland, skin).
DR MalaCards; GATA3; -.
DR MIM; 131320; gene.
DR MIM; 146255; phenotype.
DR neXtProt; NX_P23771; -.
DR OpenTargets; ENSG00000107485; -.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR Orphanet; 2237; Hypoparathyroidism-sensorineural deafness-renal disease syndrome.
DR PharmGKB; PA28586; -.
DR VEuPathDB; HostDB:ENSG00000107485; -.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000159247; -.
DR HOGENOM; CLU_027524_1_0_1; -.
DR InParanoid; P23771; -.
DR OMA; HSYMDPT; -.
DR OrthoDB; 1240204at2759; -.
DR PhylomeDB; P23771; -.
DR TreeFam; TF315391; -.
DR PathwayCommons; P23771; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P23771; -.
DR SIGNOR; P23771; -.
DR BioGRID-ORCS; 2625; 73 hits in 1095 CRISPR screens.
DR ChiTaRS; GATA3; human.
DR GeneWiki; GATA3; -.
DR GenomeRNAi; 2625; -.
DR Pharos; P23771; Tbio.
DR PRO; PR:P23771; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P23771; protein.
DR Bgee; ENSG00000107485; Expressed in upper leg skin and 152 other tissues.
DR ExpressionAtlas; P23771; baseline and differential.
DR Genevisible; P23771; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005134; F:interleukin-2 receptor binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0061290; P:canonical Wnt signaling pathway involved in metanephric kidney development; ISS:UniProtKB.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; ISS:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0001709; P:cell fate determination; ISS:UniProtKB.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IEP:UniProtKB.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEP:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0043583; P:ear development; IMP:UniProtKB.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
DR GO; GO:0002520; P:immune system development; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0072676; P:lymphocyte migration; IDA:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0060374; P:mast cell differentiation; IEA:Ensembl.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IDA:UniProtKB.
DR GO; GO:0001823; P:mesonephros development; ISS:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000607; P:negative regulation of cell proliferation involved in mesonephros development; ISS:UniProtKB.
DR GO; GO:1901536; P:negative regulation of DNA demethylation; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:2000703; P:negative regulation of fibroblast growth factor receptor signaling pathway involved in ureteric bud formation; ISS:UniProtKB.
DR GO; GO:2000734; P:negative regulation of glial cell-derived neurotrophic factor receptor signaling pathway involved in ureteric bud formation; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0072179; P:nephric duct formation; ISS:UniProtKB.
DR GO; GO:0072178; P:nephric duct morphogenesis; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0071599; P:otic vesicle development; IEA:Ensembl.
DR GO; GO:0060017; P:parathyroid gland development; IEA:Ensembl.
DR GO; GO:0035898; P:parathyroid hormone secretion; IEA:Ensembl.
DR GO; GO:0060037; P:pharyngeal system development; ISS:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0071442; P:positive regulation of histone H3-K14 acetylation; IEA:Ensembl.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IEA:Ensembl.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IDA:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IDA:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0009967; P:positive regulation of signal transduction; IMP:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; ISS:UniProtKB.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IEA:Ensembl.
DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0072107; P:positive regulation of ureteric bud formation; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0002572; P:pro-T cell differentiation; IEA:Ensembl.
DR GO; GO:2000683; P:regulation of cellular response to X-ray; IMP:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0061085; P:regulation of histone H3-K27 methylation; IEA:Ensembl.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0045622; P:regulation of T-helper cell differentiation; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEP:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; IDA:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IEA:Ensembl.
DR GO; GO:0045061; P:thymic T cell selection; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001806; P:type IV hypersensitivity; IEA:Ensembl.
DR GO; GO:0035799; P:ureter maturation; IEA:Ensembl.
DR GO; GO:0072197; P:ureter morphogenesis; IEA:Ensembl.
DR GO; GO:0060676; P:ureteric bud formation; ISS:UniProtKB.
DR GO; GO:0060065; P:uterus development; ISS:UniProtKB.
DR GO; GO:0003281; P:ventricular septum development; ISS:UniProtKB.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR029521; GATA-3.
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; PTHR10071; 1.
DR PANTHER; PTHR10071:SF106; PTHR10071:SF106; 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 PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Deafness; Disease variant;
KW DNA-binding; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..443
FT /note="Trans-acting T-cell-specific transcription factor
FT GATA-3"
FT /id="PRO_0000083408"
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..258
FT /note="Interaction with TBX21"
FT /evidence="ECO:0000250|UniProtKB:P23772"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..316
FT /note="Flexible linker"
FT REGION 361..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..353
FT /note="YxKxHxxxRP"
FT /evidence="ECO:0000250"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 259
FT /note="T -> TE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1871134, ECO:0000303|PubMed:2017177"
FT /id="VSP_001598"
FT VARIANT 242
FT /note="G -> S (in dbSNP:rs11567901)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019202"
FT VARIANT 274
FT /note="W -> R (in HDR; dbSNP:rs104894163)"
FT /evidence="ECO:0000269|PubMed:11389161"
FT /id="VAR_017818"
FT VARIANT 298
FT /note="R -> Q (in HDR; loss of enhancer activity on PTH
FT gene promoter and on GATA responsive element)"
FT /evidence="ECO:0000269|PubMed:26514990"
FT /id="VAR_075427"
FT VARIANT 366
FT /note="R -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17224074"
FT /id="VAR_033025"
FT CONFLICT 11
FT /note="V -> L (in Ref. 4; AAA35870)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="A -> V (in Ref. 2; CAA38877)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="A -> G (in Ref. 2; CAA38877)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="I -> Y (in Ref. 4; AAA35870)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..226
FT /note="YV -> TC (in Ref. 4; AAA35870)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..286
FT /note="NA -> RR (in Ref. 4; AAA35870)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="P -> A (in Ref. 4; AAA35870)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="A -> G (in Ref. 4; AAA35870)"
FT /evidence="ECO:0000305"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:4HC9"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:4HC9"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:4HC7"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:4HC9"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:4HC9"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4HC9"
SQ SEQUENCE 443 AA; 47916 MW; F24C58681E1D02A5 CRC64;
MEVTADQPRW VSHHHPAVLN GQHPDTHHPG LSHSYMDAAQ YPLPEEVDVL FNIDGQGNHV
PPYYGNSVRA TVQRYPPTHH GSQVCRPPLL HGSLPWLDGG KALGSHHTAS PWNLSPFSKT
SIHHGSPGPL SVYPPASSSS LSGGHASPHL FTFPPTPPKD VSPDPSLSTP GSAGSARQDE
KECLKYQVPL PDSMKLESSH SRGSMTALGG ASSSTHHPIT TYPPYVPEYS SGLFPPSSLL
GGSPTGFGCK SRPKARSSTG RECVNCGATS TPLWRRDGTG HYLCNACGLY HKMNGQNRPL
IKPKRRLSAA RRAGTSCANC QTTTTTLWRR NANGDPVCNA CGLYYKLHNI NRPLTMKKEG
IQTRNRKMSS KSKKCKKVHD SLEDFPKNSS FNPAALSRHM SSLSHISPFS HSSHMLTTPT
PMHPPSSLSF GPHHPSSMVT AMG
