STAT2_PIG
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 03-AUG-2022, entry version 136.
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.ENSSSCP00000000422; -.
DR PaxDb; O02799; -.
DR PeptideAtlas; O02799; -.
DR PRIDE; O02799; -.
DR Ensembl; ENSSSCT00000000428; ENSSSCP00000000422; ENSSSCG00000000396.
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; PMDIRQC; -.
DR OrthoDB; 327469at2759; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000000396; Expressed in blood and 40 other 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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
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 signaling pathway; ISS:UniProtKB.
DR CDD; cd10373; SH2_STAT2; 1.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
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; 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 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 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 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
