ID   STAT2_PIG               Reviewed;         864 AA.
AC   O02799;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Signal transducer and activator of transcription 2;
GN   Name=STAT2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RA   Ito Y., Mikawa S., Kobayashi E., Wada Y., Minezawa M.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH AFRICAN SWINE FEVER VIRUS PROTEIN MGF360-9L (MICROBIAL
RP   INFECTION).
RX   PubMed=35076286; DOI=10.1128/mbio.02330-21;
RA   Zhang K., Yang B., Shen C., Zhang T., Hao Y., Zhang D., Liu H., Shi X.,
RA   Li G., Yang J., Li D., Zhu Z., Tian H., Yang F., Ru Y., Cao W.J., Guo J.,
RA   He J., Zheng H., Liu X.;
RT   "MGF360-9L Is a Major Virulence Factor Associated with the African Swine
RT   Fever Virus by Antagonizing the JAK/STAT Signaling Pathway.";
RL   MBio 0:0-0(2022).
CC   -!- FUNCTION: Signal transducer and activator of transcription that
CC       mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following
CC       type I IFN binding to cell surface receptors, Jak kinases (TYK2 and
CC       JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and
CC       STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to
CC       form a complex termed ISGF3 transcription factor, that enters the
CC       nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to
CC       activate the transcription of interferon stimulated genes, which drive
CC       the cell in an antiviral state. Acts as a regulator of mitochondrial
CC       fission by modulating the phosphorylation of DNM1L at 'Ser-616' and
CC       'Ser-637' which activate and inactivate the GTPase activity of DNM1L
CC       respectively. {ECO:0000250|UniProtKB:P52630}.
CC   -!- SUBUNIT: Heterodimer with STAT1 upon IFN-alpha/beta induced
CC       phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-
CC       stimulated gene factor 3 complex (ISGF3) with IRF9; interacts with IRF9
CC       in the cytoplasm. Interacts with CRSP2 and CRSP6. Can form a homodimer
CC       upon IFN-alpha induced phosphorylation. Interacts with IFNAR1; the
CC       interaction requires the phosphorylation of IFNAR1 at 'Tyr-467'.
CC       Interacts with IFNAR2. Interacts with ARL2BP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with African swine fever virus
CC       (ASFV) MGF360-9L; this interaction mediates degradation of STAT1
CC       through apoptosis. {ECO:0000269|PubMed:35076286}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Translocated into the nucleus upon activation by IFN-alpha/beta.
CC       {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated in response to IFN-alpha. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
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DR   EMBL; AB004061; BAA20332.1; -; mRNA.
DR   RefSeq; NP_999054.1; NM_213889.1.
DR   AlphaFoldDB; O02799; -.
DR   SMR; O02799; -.
DR   STRING; 9823.ENSSSCP00000069374; -.
DR   PaxDb; 9823-ENSSSCP00000000422; -.
DR   PeptideAtlas; O02799; -.
DR   Ensembl; ENSSSCT00000000428.4; ENSSSCP00000000422.3; ENSSSCG00000000396.5.
DR   GeneID; 396923; -.
DR   KEGG; ssc:396923; -.
DR   CTD; 6773; -.
DR   VGNC; VGNC:93539; STAT2.
DR   eggNOG; KOG3667; Eukaryota.
DR   GeneTree; ENSGT01050000244905; -.
DR   InParanoid; O02799; -.
DR   OMA; HQDDDRV; -.
DR   OrthoDB; 7823at2759; -.
DR   Reactome; R-SSC-8854691; Interleukin-20 family signaling.
DR   Reactome; R-SSC-909733; Interferon alpha/beta signaling.
DR   Reactome; R-SSC-912694; Regulation of IFNA/IFNB signaling.
DR   Proteomes; UP000008227; Chromosome 5.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000000396; Expressed in blood and 40 other cell types or tissues.
DR   ExpressionAtlas; O02799; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070721; C:ISGF3 complex; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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:0090140; P:regulation of mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
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   GO; GO:0060337; P:type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR   CDD; cd10373; SH2_STAT2; 1.
DR   CDD; cd16846; STAT2_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; IPR022756; STAT2_C.
DR   InterPro; IPR035854; STAT2_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:SF41; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12188; STAT2_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; 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.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Host-virus interaction; Nucleus;
KW   Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..864
FT                   /note="Signal transducer and activator of transcription 2"
FT                   /id="PRO_0000182415"
FT   DOMAIN          572..667
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52630"
FT   MOD_RES         690
FT                   /note="Phosphotyrosine; by JAK"
FT                   /evidence="ECO:0000250|UniProtKB:P52630"
FT   MOD_RES         812
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52630"
SQ   SEQUENCE   864 AA;  99061 MW;  2F8CC95569FB5B20 CRC64;
     MAQWEMLQNL DSPFQDQLHQ LYSESLLPVD VRQYLAVWIE DQNWQEAALG NDDSKANMLF
     FHFLDQLNYD CGRCGQDPEC LLLQHNLRKF YRDIQAIPQG PTRLAEMIFN LLLEEKRILI
     QAQRAQLEQQ EPALEAPGEN QQHEIESRIL ELRAMMEKLV KSISQLKDQQ DIFCFRYKIK
     ASAKTHSLDP HRTRQEQVLQ ETLNELDKRR KEVLDASKAL LGRLTTLIEL LLPKLEEWKV
     QQQKACIGAP MDGELEQLEK WFTAEAKLLF HLRQLLKELK GLSSVVKYDE DLLFKGVDLL
     KAQVTELLQR LLHRAFIVET QPCMPQTPHR PLILKTGSKF TVRTRLLVRL QEGNESLTAE
     VSIDRNPPKS QGFRKFNILT SNRKTLTPEK GQSQGLIWDF GYLTLMEQRS GGAGKGNNKG
     PLGVTEELHI ISFTVKYTYQ GLKQELTTDT LPVVIISNMN QLSIAWASIL WFNLLSSDPQ
     NQQFFSSPPK APWNLLGPAL SWQFSSHVGQ GLNSDQLGML RDKLFGQNSS TEGLSLSWVD
     FIKRESPPGK LPFWTWLDKI LDLVHDHLKD LWKDGHIMGF VSRSEERRLL KKTISGTFLL
     RFSETLEGGI TCSWVEHQDD DKVLIYSLQP FTKEVLQSLP LTKIISQYQL LTEENIPENP
     LRFLYPRIPR DEAFGCYNQE KANLQERKKY LKHKLIVVSN RQVDELQQPP ELKLEPDLES
     LELDLGLAPG PEPGVGLDLE PLLEAGLDLG PELEPMLQST LEPVLEPILD EVLQGVPEPN
     LGPELKLEPI LEPVSQPVPE PDLPHDLRHL NTDEMQIFRN SMRIEEIMPN GDPLLASQNT
     NVDEACVFHR SHFYTDGPLI PSDY
//