ID STAT3_RAT Reviewed; 770 AA. AC P52631; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 198. DE RecName: Full=Signal transducer and activator of transcription 3; GN Name=Stat3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=8530402; DOI=10.1074/jbc.270.50.29998; RA Ripperger J.A., Fritz S., Richter K., Hocke G.M., Lottspeich F., Fey G.H.; RT "Transcription factors Stat3 and Stat5b are present in rat liver nuclei RT late in an acute phase response and bind interleukin-6 response elements."; RL J. Biol. Chem. 270:29998-30006(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 CAV2. RX PubMed=19427337; DOI=10.1016/j.bbamcr.2009.04.015; RA Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S., Pak Y.; RT "Caveolin-2 regulation of STAT3 transcriptional activation in response to RT insulin."; RL Biochim. Biophys. Acta 1793:1325-1333(2009). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=19538478; DOI=10.1111/j.1582-4934.2009.00804.x; RA Manukyan I., Galatioto J., Mascareno E., Bhaduri S., Siddiqui M.A.; RT "Cross-talk between calcineurin/NFAT and Jak/STAT signalling induces RT cardioprotective alphaB-crystallin gene expression in response to RT hypertrophic stimuli."; RL J. Cell. Mol. Med. 14:1707-1716(2010). CC -!- FUNCTION: Signal transducer and transcription activator that mediates CC cellular responses to interleukins, KITLG/SCF, LEP and other growth CC factors. Once activated, recruits coactivators, such as NCOA1 or MED1, CC to the promoter region of the target gene. May mediate cellular CC responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation CC of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6- CC responsive elements identified in the promoters of various acute-phase CC protein genes. Activated by IL31 through IL31RA (By similarity). Acts CC as a regulator of inflammatory response by regulating differentiation CC of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells CC (Treg): acetylation promotes its transcription activity and cell CC differentiation while deacetylation and oxidation of lysine residues by CC LOXL3 inhibits differentiation (By similarity). Involved in cell cycle CC regulation by inducing the expression of key genes for the progression CC from G1 to S phase, such as CCND1 (By similarity). Mediates the effects CC of LEP on melanocortin production, body energy homeostasis and CC lactation. May play an apoptotic role by transctivating BIRC5 CC expression under LEP activation (By similarity). Cytoplasmic STAT3 CC represses macroautophagy by inhibiting EIF2AK2/PKR activity (By CC similarity). Plays a crucial role in basal beta cell functions, such as CC regulation of insulin secretion. Following JAK/STAT signaling CC activation and as part of a complex with NFATC3 and NFATC4, binds to CC the alpha-beta E4 promoter region of CRYAB and activates transcription CC in cardiomyocytes (PubMed:19538478). Plays an important role in host CC defense in methicillin-resistant S.aureus lung infection by regulating CC the expression of the antimicrobial lectin REG3G (By similarity). CC {ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P42227, CC ECO:0000269|PubMed:19538478}. CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family CC member (at least STAT1). Component of a promoter-binding complex CC composed of STAT3, NFATC3 and NFATC4; complex formation is enhanced by CC calcineurin (By similarity). Interacts with IL31RA, NCOA1, PELP1, CC SIPAR, SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence of CC IL23. Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the CC interaction is enhanced by LIF and JAK1 expression (By similarity). CC Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of CC nuclear import (By similarity). Interacts with CAV2; the interaction is CC increased on insulin-induced tyrosine phosphorylation of CAV2 and leads CC to STAT3 activation (PubMed:19427337). Interacts with ARL2BP; CC interaction is enhanced with ARL2. Interacts with NEK6 (By similarity). CC Binds to CDK9 when activated and nuclear. Interacts with BMX. Interacts CC with ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on CC stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity CC of STAT3. In prostate cancer cells, interacts with PRKCE and promotes CC DNA binding activity of STAT3 (By similarity). Interacts with STMN3, CC antagonizing its microtubule-destabilizing activity (By similarity). CC Interacts with the 'Lys-129' acetylated form of BIRC5/survivin. CC Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via CC the kinase catalytic domain) (By similarity). Interacts with FGFR4 (By CC similarity). Interacts with INPP5F; the interaction is independent of CC STAT3 Tyr-705 phosphorylation status (By similarity). Interacts with CC OCAD1 (By similarity). Interacts (unphosphorylated or phosphorylated at CC Ser-727) with PHB1 (By similarity). Interacts and may form heterodimers CC with NHLH1 (By similarity). Found in a complex with SLC39A6, SLC39A10 CC and with the 'Ser-727' phosphorylated form of STAT3 throughout mitosis CC (By similarity). Interacts (when acetylated) with EP300 (via bromo CC domain); interaction takes place following STAT3 acetylation by EP300 CC and promotes enhanceosome assembly (By similarity). Interacts (when CC acetylated) with BRD2 (via bromo domain); interaction promotes STAT3 CC recruitment to chromatin and T-helper Th17 cell differentiation (By CC similarity). {ECO:0000250|UniProtKB:P40763, CC ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:19427337}. CC -!- INTERACTION: CC P52631; O13097: efnb1; Xeno; NbExp=4; IntAct=EBI-10764775, EBI-15667006; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19538478}. Nucleus CC {ECO:0000269|PubMed:19538478}. Note=Shuttles between the nucleus and CC the cytoplasm. Translocated into the nucleus upon tyrosine CC phosphorylation and dimerization, in response to signaling by activated CC FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is CC independent of tyrosine phosphorylation. Predominantly present in the CC cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) CC stimulation, accumulates in the nucleus. The complex composed of BART CC and ARL2 plays an important role in the nuclear translocation and CC retention of STAT3 (By similarity). Translocates to the nucleus in the CC presence of EDN1 (PubMed:19538478). {ECO:0000250, CC ECO:0000269|PubMed:19538478}. CC -!- TISSUE SPECIFICITY: Detected in lung, heart, oviduct, ovary, uterus and CC kidney (at protein level). Expressed in cardiomyocytes (at protein CC level) (PubMed:19538478). Detected in ovary, oviduct, and at lower CC levels in uterus and lung. {ECO:0000269|PubMed:19538478}. CC -!- PTM: Activated through tyrosine phosphorylation by BMX. Tyrosine CC phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1, CC EGF, PDGF, IFN-alpha and OSM. Activated KIT promotes phosphorylation on CC tyrosine residues and subsequent translocation to the nucleus. Tyrosine CC phosphorylated in response to constitutively activated FGFR1, FGFR2, CC FGFR3 and FGFR4. Phosphorylated on serine upon DNA damage, probably by CC ATM or ATR. Serine phosphorylation is important for the formation of CC stable DNA-binding STAT3 homodimers and maximal transcriptional CC activity. ARL2BP may participate in keeping the phosphorylated state of CC STAT3 within the nucleus. Tyrosine phosphorylated upon stimulation with CC EGF. Upon LPS challenge, phosphorylated within the nucleus by IRAK1. CC Phosphorylated on Ser-727 by RPS6KA5 (By similarity). Dephosphorylation CC on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 CC signaling (By similarity). Phosphorylation at Tyr-705 by FER, isoform CC M2 of PKM (PKM2) or PTK6 leads to an increase of its transcriptional CC activity. Phosphorylation at Tyr-705 is increased in the presence of CC calcineurin (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P42227}. CC -!- PTM: Acetylated on lysine residues by EP300/p300, promoting its CC activation (By similarity). Acetylation at Lys-49 and Lys-87 by CC EP300/p300 promotes its activation (By similarity). Acetylation at Lys- CC 87 by EP300/p300 promotes its association with BRD2 and recruitment to CC chromatin (By similarity). Deacetylated at Lys-49 and Lys-87 by HDAC1 CC (By similarity). Acetylation at Lys-685 by EP300/p300 promotes its CC homodimerization and activation (By similarity). Deacetylated at Lys- CC 685 by HDAC3 (By similarity). Acetylated on lysine residues by CREBBP CC (By similarity). Deacetylation by LOXL3 leads to disrupt STAT3 CC dimerization and inhibit STAT3 transcription activity (By similarity). CC Oxidation of lysine residues to allysine on STAT3 preferentially takes CC place on lysine residues that are acetylated (By similarity). CC {ECO:0000250|UniProtKB:P40763}. CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to CC disrupt STAT3 dimerization and inhibit STAT3 transcription activity. CC Oxidation of lysine residues to allysine on STAT3 preferentially takes CC place on lysine residues that are acetylated. CC {ECO:0000250|UniProtKB:P40763}. CC -!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway. CC -!- SIMILARITY: Belongs to the transcription factor STAT family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X91810; CAA62920.1; -; mRNA. DR EMBL; BC087025; AAH87025.1; -; mRNA. DR RefSeq; NP_036879.1; NM_012747.2. DR AlphaFoldDB; P52631; -. DR SMR; P52631; -. DR BioGRID; 247196; 3. DR CORUM; P52631; -. DR DIP; DIP-44909N; -. DR IntAct; P52631; 18. DR MINT; P52631; -. DR STRING; 10116.ENSRNOP00000026760; -. DR ChEMBL; CHEMBL1764933; -. DR iPTMnet; P52631; -. DR PhosphoSitePlus; P52631; -. DR jPOST; P52631; -. DR PaxDb; 10116-ENSRNOP00000026760; -. DR Ensembl; ENSRNOT00000026760.5; ENSRNOP00000026760.3; ENSRNOG00000019742.6. DR Ensembl; ENSRNOT00055055737; ENSRNOP00055045927; ENSRNOG00055032275. DR Ensembl; ENSRNOT00060021941; ENSRNOP00060017357; ENSRNOG00060012887. DR Ensembl; ENSRNOT00065050949; ENSRNOP00065041898; ENSRNOG00065029490. DR GeneID; 25125; -. DR KEGG; rno:25125; -. DR AGR; RGD:3772; -. DR CTD; 6774; -. DR RGD; 3772; Stat3. DR eggNOG; KOG3667; Eukaryota. DR GeneTree; ENSGT01050000244905; -. DR HOGENOM; CLU_014189_3_0_1; -. DR InParanoid; P52631; -. DR OrthoDB; 7823at2759; -. DR PhylomeDB; P52631; -. DR TreeFam; TF318648; -. DR Reactome; R-RNO-1059683; Interleukin-6 signaling. DR Reactome; R-RNO-1266695; Interleukin-7 signaling. DR Reactome; R-RNO-1433557; Signaling by SCF-KIT. DR Reactome; R-RNO-186763; Downstream signal transduction. DR Reactome; R-RNO-201556; Signaling by ALK. DR Reactome; R-RNO-6783783; Interleukin-10 signaling. DR Reactome; R-RNO-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-RNO-8849474; PTK6 Activates STAT3. DR Reactome; R-RNO-8854691; Interleukin-20 family signaling. DR Reactome; R-RNO-8875791; MET activates STAT3. DR Reactome; R-RNO-8983432; Interleukin-15 signaling. DR Reactome; R-RNO-8984722; Interleukin-35 Signalling. DR Reactome; R-RNO-8985947; Interleukin-9 signaling. DR Reactome; R-RNO-9008059; Interleukin-37 signaling. DR Reactome; R-RNO-9020933; Interleukin-23 signaling. DR Reactome; R-RNO-9020956; Interleukin-27 signaling. DR Reactome; R-RNO-9020958; Interleukin-21 signaling. DR Reactome; R-RNO-9701898; STAT3 nuclear events downstream of ALK signaling. DR Reactome; R-RNO-9833482; PKR-mediated signaling. DR PRO; PR:P52631; -. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000019742; Expressed in heart and 20 other cell types or tissues. DR GO; GO:0000785; C:chromatin; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:RGD. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD. DR GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:RGD. DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:RGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:RGD. DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD. DR GO; GO:0070878; F:primary miRNA binding; ISO:RGD. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD. DR GO; GO:0140610; F:RNA sequestering activity; ISO:RGD. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD. DR GO; GO:0035591; F:signaling adaptor activity; ISO:RGD. DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEP:RGD. DR GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; ISO:RGD. DR GO; GO:0008283; P:cell population proliferation; ISO:RGD. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI. DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD. DR GO; GO:0097398; P:cellular response to interleukin-17; ISO:RGD. DR GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI. DR GO; GO:0006952; P:defense response; IBA:GO_Central. DR GO; GO:0042755; P:eating behavior; ISS:UniProtKB. DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB. DR GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:RGD. DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0038154; P:interleukin-11-mediated signaling pathway; ISO:RGD. DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:RGD. DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; ISO:RGD. DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0038113; P:interleukin-9-mediated signaling pathway; ISO:RGD. DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:RGD. DR GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD. DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:RGD. DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IMP:RGD. DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD. DR GO; GO:0106015; P:negative regulation of inflammatory response to wounding; ISO:RGD. DR GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD. DR GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:RGD. DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:RGD. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD. DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD. DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD. DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; IMP:RGD. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:ARUK-UCL. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD. DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD. DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO. DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB. DR GO; GO:0060019; P:radial glial cell differentiation; ISS:UniProtKB. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:RGD. DR GO; GO:0097696; P:receptor signaling pathway via STAT; ISO:RGD. DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IMP:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB. DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:RGD. DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0034097; P:response to cytokine; IDA:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0002931; P:response to ischemia; IMP:RGD. DR GO; GO:0044321; P:response to leptin; ISS:UniProtKB. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0010033; P:response to organic substance; IEP:RGD. DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0060221; P:retinal rod cell differentiation; ISO:RGD. DR GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB. DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD. DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB. DR GO; GO:0072538; P:T-helper 17 type immune response; ISO:RGD. DR GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD. DR CDD; cd10374; SH2_STAT3; 1. DR CDD; cd16853; STAT3_CCD; 1. DR CDD; cd16847; STAT3_DBD; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 1.20.1050.20; STAT transcription factor, all-alpha domain; 1. DR Gene3D; 2.60.40.630; STAT transcription factor, DNA-binding domain; 1. DR Gene3D; 1.10.532.10; STAT transcription factor, N-terminal domain; 1. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR001217; STAT. DR InterPro; IPR035855; STAT3_SH2. DR InterPro; IPR048988; STAT_linker. DR InterPro; IPR036535; STAT_N_sf. DR InterPro; IPR013800; STAT_TF_alpha. DR InterPro; IPR015988; STAT_TF_coiled-coil. DR InterPro; IPR013801; STAT_TF_DNA-bd. DR InterPro; IPR012345; STAT_TF_DNA-bd_N. DR InterPro; IPR013799; STAT_TF_prot_interaction. DR PANTHER; PTHR11801; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION; 1. DR PANTHER; PTHR11801:SF2; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 3; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF01017; STAT_alpha; 1. DR Pfam; PF02864; STAT_bind; 1. DR Pfam; PF02865; STAT_int; 1. DR Pfam; PF21354; STAT_linker; 1. DR SMART; SM00964; STAT_int; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF47655; STAT; 1. DR SUPFAM; SSF48092; Transcription factor STAT-4 N-domain; 1. DR PROSITE; PS50001; SH2; 1. DR Genevisible; P52631; RN. PE 1: Evidence at protein level; KW Acetylation; Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; KW Reference proteome; SH2 domain; Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P40763" FT CHAIN 2..770 FT /note="Signal transducer and activator of transcription 3" FT /id="PRO_0000182419" FT DOMAIN 580..670 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT MOTIF 150..162 FT /note="Essential for nuclear import" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 87 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 601 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 601 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 615 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 615 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 631 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 631 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 685 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 685 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 705 FT /note="Phosphotyrosine; by FER and PTK6" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 707 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 714 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P40763" FT MOD_RES 727 FT /note="Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, FT ZIPK/DAPK3 and PKC/PRKCE" FT /evidence="ECO:0000250|UniProtKB:P40763" SQ SEQUENCE 770 AA; 88040 MW; D74A0C76954754ED CRC64; MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ HRPMLEERIV DLFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDMD LTSECATSPM //