STAT4_MOUSE
ID STAT4_MOUSE Reviewed; 749 AA.
AC P42228;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Signal transducer and activator of transcription 4;
GN Name=Stat4;
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].
RC TISSUE=Thymus;
RX PubMed=7545930; DOI=10.1073/pnas.91.11.4806;
RA Zhong Z., Wen Z., Darnell J.E. Jr.;
RT "Stat3 and Stat4: members of the family of signal transducers and
RT activators of transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4806-4810(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=8007943; DOI=10.1128/mcb.14.7.4342-4349.1994;
RA Yamamoto K., Quelle F.W., Thierfelder W.E., Kreider B.L., Gilbert D.J.,
RA Jenkins N.A., Copeland N.G., Silvennoinen O., Ihle J.N.;
RT "Stat4, a novel gamma interferon activation site-binding protein expressed
RT in early myeloid differentiation.";
RL Mol. Cell. Biol. 14:4342-4349(1994).
RN [3]
RP INTERACTION WITH ARL2BP.
RX PubMed=18234692; DOI=10.1093/intimm/dxm154;
RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
RA Matsuda T.;
RT "BART is essential for nuclear retention of STAT3.";
RL Int. Immunol. 20:395-403(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-123.
RX PubMed=9461439; DOI=10.1126/science.279.5353.1048;
RA Vinkemeier U., Moarefi I., Darnell J.E. Jr., Kuriyan J.;
RT "Structure of the amino-terminal protein interaction domain of STAT-4.";
RL Science 279:1048-1052(1998).
CC -!- FUNCTION: Carries out a dual function: signal transduction and
CC activation of transcription.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member (By similarity). Interacts with ARL2BP. {ECO:0000250,
CC ECO:0000269|PubMed:18234692}.
CC -!- INTERACTION:
CC P42228; P42225: Stat1; NbExp=2; IntAct=EBI-6253572, EBI-647118;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the
CC nucleus in response to phosphorylation.
CC -!- PTM: Tyrosine phosphorylated. Serine phosphorylation is also required
CC for maximal transcriptional activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; U06923; AAA19453.1; -; mRNA.
DR EMBL; U09351; AAA19692.1; -; mRNA.
DR PIR; A56047; A56047.
DR RefSeq; NP_001295195.1; NM_001308266.1.
DR RefSeq; NP_035617.1; NM_011487.5.
DR PDB; 1BGF; X-ray; 1.45 A; A=2-123.
DR PDBsum; 1BGF; -.
DR AlphaFoldDB; P42228; -.
DR BMRB; P42228; -.
DR SMR; P42228; -.
DR BioGRID; 203524; 1.
DR DIP; DIP-1170N; -.
DR IntAct; P42228; 2.
DR STRING; 10090.ENSMUSP00000027277; -.
DR iPTMnet; P42228; -.
DR PhosphoSitePlus; P42228; -.
DR SwissPalm; P42228; -.
DR EPD; P42228; -.
DR MaxQB; P42228; -.
DR PaxDb; P42228; -.
DR PRIDE; P42228; -.
DR ProteomicsDB; 257369; -.
DR DNASU; 20849; -.
DR GeneID; 20849; -.
DR KEGG; mmu:20849; -.
DR CTD; 6775; -.
DR MGI; MGI:103062; Stat4.
DR eggNOG; KOG3667; Eukaryota.
DR InParanoid; P42228; -.
DR OrthoDB; 327469at2759; -.
DR PhylomeDB; P42228; -.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8984722; Interleukin-35 Signalling.
DR Reactome; R-MMU-9020591; Interleukin-12 signaling.
DR Reactome; R-MMU-9020933; Interleukin-23 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR BioGRID-ORCS; 20849; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Stat4; mouse.
DR EvolutionaryTrace; P42228; -.
DR PRO; PR:P42228; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P42228; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0070661; P:leukocyte proliferation; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR CDD; cd10375; SH2_STAT4; 1.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID50278; -.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001217; STAT.
DR InterPro; IPR029839; STAT4.
DR InterPro; IPR035856; STAT4_SH2.
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; PTHR11801; 1.
DR PANTHER; PTHR11801:SF19; PTHR11801:SF19; 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 SMART; SM00964; STAT_int; 1.
DR SUPFAM; SSF47655; SSF47655; 1.
DR SUPFAM; SSF48092; SSF48092; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT CHAIN 1..749
FT /note="Signal transducer and activator of transcription 4"
FT /id="PRO_0000182421"
FT DOMAIN 570..665
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT MOD_RES 694
FT /note="Phosphotyrosine; by JAK"
FT /evidence="ECO:0000250"
FT CONFLICT 199
FT /note="Missing (in Ref. 2; AAA19692)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="A -> P (in Ref. 2; AAA19692)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 50..74
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:1BGF"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:1BGF"
SQ SEQUENCE 749 AA; 85941 MW; A88B837E49FCFEBC CRC64;
MSQWNQVQQL EIKFLEQVDQ FYDDNFPMEI RHLLAQWIET QDWEVASNNE TMATILLQNL
LIQLDEQLGR VSKEKNLLLI HNLKRIRKVL QGKFHGNPMH VAVVISNCLR EERRILAAAN
MPIQGPLEKS LQSSSVSERQ RNVEHKVSAI KNSVQMTEQD TKYLEDLQDE FDYRYKTIQT
MDQGDKNSIL VNQEVLTLLQ EMLNSLDFKR KEALSKMTQI VNETDLLMNS MLLEELQDWK
KRQQIACIGG PLHNGLDQLQ NCFTLLAESL FQLRQQLEKL QEQSTKMTYE GDPIPAQRAH
LLERATFLIY NLFKNSFVVE RQPCMPTHPQ RPMVLKTLIQ FTVKLRLLIK LPELNYQVKV
KASIDKNVST LSNRRFVLCG THVKAMSSEE SSNGSLSVEF RHLQPKEMKC STGSKGNEGC
HMVTEELHSI TFETQICLYG LTINLETSSL PVVMISNVSQ LPNAWASIIW YNVSTNDSQN
LVFFNNPPSV TLGQLLEVMS WQFSSYVGRG LNSEQLNMLA EKLTVQSNYN DGHLTWAKFC
KEHLPGKTFT FWTWLEAILD LIKKHILPLW IDGYIMGFVS KEKERLLLKD KMPGTFLLRF
SESHLGGITF TWVDQSENGE VRFHSVEPYN KGRLSALAFA DILRDYKVIM AENIPENPLK
YLYPDIPKDK AFGKHYSSQP CEVSRPTERG DKGYVPSVFI PISTIRSDST EPQSPSDLLP
MSPSAYAVLR ENLSPTTIET AMNSPYSAE
