ID   STAT6_MOUSE             Reviewed;         837 AA.
AC   P52633; Q8R2F1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Signal transducer and transcription activator 6;
GN   Name=Stat6;
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=7760829; DOI=10.1128/mcb.15.6.3336;
RA   Quelle F.W., Shimoda K., Thierfelder W., Fischer C.L., Kim A., Ruben S.M.,
RA   Cleveland J.L., Pierce J.H., Keegan A.D., Nelms K., Paul W.E., Ihle J.N.;
RT   "Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine
RT   phosphorylated in responses to IL-4 and IL-3 but are not required for
RT   mitogenesis.";
RL   Mol. Cell. Biol. 15:3336-3343(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Leyva F.J., Evans C.M., Tuvim M.J., Dickey B.F.;
RT   "Murine signal transducer and activator of transcription 6 (mSTAT6).";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   FUNCTION IN IL4/INTERLEUKIN-4 SIGNALING, PHOSPHORYLATION, AND
RP   DEPHOSPHORYLATION BY PTPN2.
RX   PubMed=17210636; DOI=10.1128/mcb.01234-06;
RA   Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T.,
RA   Lossos I.S.;
RT   "T-cell protein tyrosine phosphatase, distinctively expressed in activated-
RT   B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of
RT   STAT6.";
RL   Mol. Cell. Biol. 27:2166-2179(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
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).
CC   -!- FUNCTION: Carries out a dual function: signal transduction and
CC       activation of transcription. Involved in IL4/interleukin-4- and
CC       IL3/interleukin-3-mediated signaling. {ECO:0000269|PubMed:17210636}.
CC   -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC       member. Interacts with NCOA1 via its C-terminal LXXLL motif (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P52633; Q2EMV9: Parp14; NbExp=3; IntAct=EBI-647085, EBI-1534943;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the
CC       nucleus in response to phosphorylation.
CC   -!- PTM: Tyrosine phosphorylated on Tyr-641 following stimulation by
CC       IL4/interleukin-4. Tyrosine phosphorylated following stimulation by
CC       IL3/interleukin-3. Dephosphorylation on tyrosine residues by PTPN2
CC       negatively regulates the IL4/interleukin-4 mediated signaling.
CC       {ECO:0000269|PubMed:17210636}.
CC   -!- PTM: Mono-ADP-ribosylated by PARP14. {ECO:0000250|UniProtKB:P42226}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
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DR   EMBL; L47650; AAA79006.1; -; mRNA.
DR   EMBL; AF481809; AAL82638.1; -; mRNA.
DR   EMBL; AK163053; BAE37172.1; -; mRNA.
DR   EMBL; CH466578; EDL24514.1; -; Genomic_DNA.
DR   EMBL; BC127054; AAI27055.1; -; mRNA.
DR   CCDS; CCDS36082.1; -.
DR   PIR; I57557; I57557.
DR   RefSeq; NP_033310.2; NM_009284.2.
DR   AlphaFoldDB; P52633; -.
DR   SMR; P52633; -.
DR   BioGRID; 203527; 7.
DR   DIP; DIP-49680N; -.
DR   IntAct; P52633; 9.
DR   STRING; 10090.ENSMUSP00000089708; -.
DR   BindingDB; P52633; -.
DR   ChEMBL; CHEMBL2189147; -.
DR   GlyGen; P52633; 8 sites, 1 O-linked glycan (8 sites).
DR   iPTMnet; P52633; -.
DR   PhosphoSitePlus; P52633; -.
DR   EPD; P52633; -.
DR   MaxQB; P52633; -.
DR   PaxDb; 10090-ENSMUSP00000089708; -.
DR   PeptideAtlas; P52633; -.
DR   ProteomicsDB; 254580; -.
DR   Pumba; P52633; -.
DR   Antibodypedia; 662; 1683 antibodies from 50 providers.
DR   DNASU; 20852; -.
DR   Ensembl; ENSMUST00000092074.12; ENSMUSP00000089708.6; ENSMUSG00000002147.19.
DR   GeneID; 20852; -.
DR   KEGG; mmu:20852; -.
DR   UCSC; uc007hka.1; mouse.
DR   AGR; MGI:103034; -.
DR   CTD; 6778; -.
DR   MGI; MGI:103034; Stat6.
DR   VEuPathDB; HostDB:ENSMUSG00000002147; -.
DR   eggNOG; KOG3667; Eukaryota.
DR   GeneTree; ENSGT01080000257420; -.
DR   HOGENOM; CLU_014189_2_1_1; -.
DR   InParanoid; P52633; -.
DR   OMA; EPQMPAM; -.
DR   OrthoDB; 7823at2759; -.
DR   PhylomeDB; P52633; -.
DR   TreeFam; TF318648; -.
DR   Reactome; R-MMU-186763; Downstream signal transduction.
DR   Reactome; R-MMU-3249367; STAT6-mediated induction of chemokines.
DR   Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   BioGRID-ORCS; 20852; 3 hits in 119 CRISPR screens.
DR   ChiTaRS; Stat6; mouse.
DR   PRO; PR:P52633; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P52633; Protein.
DR   Bgee; ENSMUSG00000002147; Expressed in granulocyte and 239 other cell types or tissues.
DR   ExpressionAtlas; P52633; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR   GO; GO:1902170; P:cellular response to reactive nitrogen species; ISO:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0048289; P:isotype switching to IgE isotypes; IGI:MGI.
DR   GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0060443; P:mammary gland morphogenesis; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0002829; P:negative regulation of type 2 immune response; IGI:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0048295; P:positive regulation of isotype switching to IgE isotypes; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0070666; P:regulation of mast cell proliferation; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR   GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IMP:MGI.
DR   GO; GO:0002296; P:T-helper 1 cell lineage commitment; IGI:MGI.
DR   CDD; cd10377; SH2_STAT6; 1.
DR   CDD; cd16856; STAT6_CCD; 1.
DR   CDD; cd16850; STAT6_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   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR028187; STAT6_C.
DR   InterPro; IPR035857; STAT6_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:SF48; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 6; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF14596; STAT6_C; 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; SM00252; SH2; 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; P52633; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ADP-ribosylation; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P42226"
FT   CHAIN           2..837
FT                   /note="Signal transducer and transcription activator 6"
FT                   /id="PRO_0000182434"
FT   DOMAIN          517..632
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          802..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           793..797
FT                   /note="LXXLL motif"
FT   COMPBIAS        804..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42226"
FT   MOD_RES         641
FT                   /note="Phosphotyrosine; by JAK"
FT                   /evidence="ECO:0000250|UniProtKB:P42226"
FT   CONFLICT        133
FT                   /note="A -> P (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="Q -> H (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152..155
FT                   /note="QQGA -> HLGP (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="V -> L (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180..182
FT                   /note="ATM -> PTI (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="A -> T (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="A -> P (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="K -> L (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="Q -> H (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="A -> T (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="A -> S (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="P -> S (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="A -> G (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="A -> V (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        753
FT                   /note="C -> W (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        786
FT                   /note="M -> L (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        804
FT                   /note="A -> G (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        815
FT                   /note="Q -> K (in Ref. 1; AAA79006)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   837 AA;  93497 MW;  082E0A15C7457307 CRC64;
     MSLWGLISKM SPEKLQRLYV DFPQRLRHLL ADWLESQPWE FLVGSDAFCY NMASALLSAT
     VQRLQATAGE QGKGNSILPH ISTLESIYQR DPLKLVATIR QILQGEKKAV IEEFRHLPGP
     FHRKQEELKF TTALGRLQHR VRETRLLRES LQQGAKTGQV SLQNLIDPPV NGPGPSEDLA
     TMLQGTVGDL EATQALVLKR IQIWKRQQQL AGNGTPFEES LAGLQERCES LVEIYSQLQQ
     EIGAASGELE PKTRASLISR LDEVLRTLVT SSFLVEKQPP QVLKTQTKFQ AGVRFLLGLQ
     FLGTSAKPPM VRADMVTEKQ ARELSLAQGP GTGVESTGEI MNNTVPLENS IPSNCCSALF
     KNLLLKKIKR CERKGTESVT EEKCAVLFST SFTLGPNKLL IQLQALSLPL VVIVHGNQDN
     NAKATILWDN AFSEMDRVPF VVAERVPWEK MCETLNLKFM AEVGTSRGLL PEHFLFLAQK
     IFNDNSLSVE AFQHRCVSWS QFNKEILLGR GFTFWQWFDG VLDLTKRCLR SYWSDRLIIG
     FISKQYVTSL LLNEPDGTFL LRFSDSEIGG ITIAHVIRGQ DGSSQIENIQ PFSAKDLSIR
     SLGDRIRDLA QLKNLYPKKP KDEAFRSHYK PEQMGKDGRG YVSTTIKMTV ERDQPLPTPE
     PQMPAMVPPY DLGMAPDASM QLSSDMGYPP QSIHSFQSLE ESMSVLPSFQ EPHLQMPPNM
     SQITMPFDQP HPQGLLQCQS QEHAVSSPEP MLCSDVTMVE DSCLTQPVGG FPQGTWVSED
     MYPPLMPPTE QDLTKLLLEN QGEAGGSLGS QPLLQPSPYG QSGISLSHLD LRTNPSW
//