ID A0A0G2JX93_RAT Unreviewed; 1205 AA.
AC A0A0G2JX93;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Signal transducer and activator of transcription 4 {ECO:0000313|Ensembl:ENSRNOP00000070183.2};
GN Name=Stat1 {ECO:0000313|RGD:3771};
GN Synonyms=Stat4 {ECO:0000313|Ensembl:ENSRNOP00000070183.2,
GN ECO:0000313|RGD:1305747};
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 {ECO:0000313|Ensembl:ENSRNOP00000070183.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000070183.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070183.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000070183.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070183.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000256|ARBA:ARBA00005586}.
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DR AlphaFoldDB; A0A0G2JX93; -.
DR STRING; 10116.ENSRNOP00000070183; -.
DR jPOST; A0A0G2JX93; -.
DR Ensembl; ENSRNOT00000080522.2; ENSRNOP00000070183.2; ENSRNOG00000014079.8.
DR AGR; RGD:1305747; -.
DR AGR; RGD:3771; -.
DR RGD; 3771; Stat1.
DR RGD; 1305747; Stat4.
DR VEuPathDB; HostDB:ENSRNOG00000014079; -.
DR GeneTree; ENSGT01050000244905; -.
DR InParanoid; A0A0G2JX93; -.
DR Reactome; R-RNO-1059683; Interleukin-6 signaling.
DR Reactome; R-RNO-1169408; ISG15 antiviral mechanism.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-RNO-877300; Interferon gamma signaling.
DR Reactome; R-RNO-877312; Regulation of IFNG signaling.
DR Reactome; R-RNO-8854691; Interleukin-20 family signaling.
DR Reactome; R-RNO-8984722; Interleukin-35 Signalling.
DR Reactome; R-RNO-8985947; Interleukin-9 signaling.
DR Reactome; R-RNO-9020956; Interleukin-27 signaling.
DR Reactome; R-RNO-9020958; Interleukin-21 signaling.
DR Reactome; R-RNO-909733; Interferon alpha/beta signaling.
DR Reactome; R-RNO-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-RNO-9833482; PKR-mediated signaling.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014079; Expressed in testis and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JX93; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0070721; C:ISGF3 complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
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:0031730; F:CCR5 chemokine receptor binding; IPI:RGD.
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; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:RGD.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
DR GO; GO:0008015; P:blood circulation; IMP: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:0032869; P:cellular response to insulin stimulus; IDA:RGD.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0071346; P:cellular response to type II interferon; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0006351; P:DNA-templated transcription; ISO:RGD.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISO:RGD.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISO:RGD.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:RGD.
DR GO; GO:0038113; P:interleukin-9-mediated signaling pathway; ISO:RGD.
DR GO; GO:0070661; P:leukocyte proliferation; ISO:RGD.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0046725; P:negative regulation by virus of viral protein levels in host cell; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0034240; P:negative regulation of macrophage fusion; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0061326; P:renal tubule development; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR GO; GO:0034097; P:response to cytokine; IDA:RGD.
DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0035456; P:response to interferon-beta; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR GO; GO:0034340; P:response to type I interferon; ISO:RGD.
DR GO; GO:0034341; P:response to type II interferon; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; ISO:RGD.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; ISO:RGD.
DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; ISO:RGD.
DR CDD; cd10372; SH2_STAT1; 1.
DR CDD; cd16851; STAT1_CCD; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 6.10.250.3310; signal transducer and activator of transcription 1; 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; IPR038295; STAT1_C_sf.
DR InterPro; IPR035859; STAT1_SH2.
DR InterPro; IPR022752; STAT1_TAZ2-bd_C.
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:SF18; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 1-ALPHA_BETA; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF12162; STAT1_TAZ2bind; 1.
DR Pfam; PF01017; STAT_alpha; 1.
DR Pfam; PF02864; STAT_bind; 2.
DR Pfam; PF02865; STAT_int; 1.
DR Pfam; PF21354; STAT_linker; 2.
DR SMART; SM00964; STAT_int; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF47655; STAT; 1.
DR SUPFAM; SSF48092; Transcription factor STAT-4 N-domain; 1.
DR PROSITE; PS50001; SH2; 2.
PE 1: Evidence at protein level;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JX93};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 232..327
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 971..1068
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
SQ SEQUENCE 1205 AA; 138999 MW; 25F8CEC8E699FB65 CRC64;
MTYEGDPIPA QRVHLLERAT FLIYNLFKKL LIKLPELNYQ VKVKASIDNN RRFVLCGTHI
KAMSSEESSN GSLSVEFRHL GCHMVTEELH SITFETQICL YGLTINLETS SLPVVMISNV
SQLPNAWASI IWYNVSTNDS QNLVFFNNPP SVTLGQLLEV MSWQFSSYVG RGLNSDQLNM
LAEKLTVQSN YSDGHLTWAK FCKEHLPGKT FTFWTWLEAI LDLIKKHILP LWIDGYIMGF
VSKEKERLLL KDKMPGTFLL RFSESHLGGI TFTWVDQSEN GEVRFHSVEP YNKARLSALP
FADILRDYKV IMAENIPENP LKYLYPDIPK DKAFGKHYSS QPCEVPRKHV VRLFPAAASL
PPQFANRVAA APPVANLWFL WKSEEGTRYP GTGVGNRHDG TANPTPVLCK GKFFLTAELR
PKALGWKFRL ELEVSFTCVL FLQRMSQWYE LQQLDSKFLE QVHQLYDDSF PMEIRQYLAQ
WLEKQDWEHA AYDVSFATIR FHDLLSQLDD QYSRFSLENN FLLQHNIRKS KRNLQDNFQE
DPVQMSMIIH NCLKEERKIL ENAQRFNQAQ EGNIQNTVML DKQKELDSKV RNVKDQVMCI
EHEIKTLEDL QDEYDFKCKT SQNRESEANG VAKSDQKQEQ LLLHKMFLML DNKRKEIIHK
IRELLNSIEL TQNTLINDEL VEWKRRQQSA CIGGPPNACL DQLQSWFTIV AESLQQVRQQ
LKKLEELEQK FTYEQDPITK NKQVLSDRTF VLFQQLIQRL LVKLQELNYN LKVKVSFDKD
VNEKNTVKGS KHFKDLCLAL YRFRKFNILG THTKVMNMEE STNGSLAAEF RHLQLKEQKN
AGNRTNETTS LPVVVISNVS QLPSGWASIL WYNMLVTEPR NLSFFLNPPC AWWSQLSEVL
SWQFSSVTKR GLNADQLSML GEKLLGPNAG PDGLIPWTRF CKENINDKNF SFWPWIDTIL
ELIKKHLLCL WNDGCIMGFI SKERERALLK DQQPGTFLLR FSESSREGAI TFTWVERSQN
GGEPDFHAVE PYTKKELSAV TFPDIIRNYK VMAAENIPEN PLKYLYPNID KDHAFGKYYS
RPKEAPEPME LDDPKRTGYI KTELISVSEV HPSRLQSTEN LLPMSPEEFD EMSKIVGSEF
DSMVSSVAGV FPPWEDLRQA GTASDLESAV RSPEKGLSLS LFLSPPPSPY LRPSPPLSLM
SLCFS
//
