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Signal transducer and activator of transcription 3

 STAT3_RAT               Reviewed;         770 AA.
P52631;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=Signal transducer and activator of transcription 3;
Name=Stat3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8530402; DOI=10.1074/jbc.270.50.29998;
Ripperger J.A., Fritz S., Richter K., Hocke G.M., Lottspeich F.,
Fey G.H.;
"Transcription factors Stat3 and Stat5b are present in rat liver
nuclei late in an acute phase response and bind interleukin-6 response
elements.";
J. Biol. Chem. 270:29998-30006(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH CAV2.
PubMed=19427337; DOI=10.1016/j.bbamcr.2009.04.015;
Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S.,
Pak Y.;
"Caveolin-2 regulation of STAT3 transcriptional activation in response
to insulin.";
Biochim. Biophys. Acta 1793:1325-1333(2009).
-!- FUNCTION: Signal transducer and transcription activator that
mediates cellular responses to interleukins, KITLG/SCF, LEP and
other growth factors. Once activated, recruits coactivators, such
as NCOA1 or MED1, to the promoter region of the target gene. May
mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and
FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements
identified in the promoters of various acute-phase protein genes.
Activated by IL31 through IL31RA. Acts as a regulator of
inflammatory response by regulating differentiation of naive
CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg):
deacetylation and oxidation of lysine residues by LOXL3, leads to
disrupt STAT3 dimerization and inhibit its transcription activity.
Involved in cell cycle regulation by inducing the expression of
key genes for the progression from G1 to S phase, such as CCND1
(By similarity). Mediates the effects of LEP on melanocortin
production, body energy homeostasis and lactation (By similarity).
May play an apoptotic role by transctivating BIRC5 expression
under LEP activation. Cytoplasmic STAT3 represses macroautophagy
by inhibiting EIF2AK2/PKR activity (By similarity). Plays a
crucial role in basal beta cell functions, such as regulation of
insulin secretion (By similarity). {ECO:0000250|UniProtKB:P40763,
ECO:0000250|UniProtKB:P42227}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1,
SIPAR, SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence
of IL23. Interacts (via SH2 domain) with NLK. Interacts with
ARL2BP; the interaction is enhanced by LIF and JAK1 expression (By
similarity). Interacts with KPNA4 and KPNA5; KPNA4 may be the
primary mediator of nuclear import (By similarity). Interacts with
CAV2; the interaction is increased on insulin-induced tyrosine
phosphorylation of CAV2 and leads to STAT3 activation
(PubMed:19427337). Interacts with ARL2BP; interaction is enhanced
with ARL2. Interacts with NEK6 (By similarity). Binds to CDK9 when
activated and nuclear. Interacts with BMX. Interacts with
ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on
stimulation by IL6, CNTF or OSM and inhibits the DNA binding
activity of STAT3. In prostate cancer cells, interacts with STAT3
and promotes DNA binding activity of STAT3. Interacts with STMN3,
antagonizing its microtubule-destabilizing activity. Interacts
with the 'Lys-129' acetylated form of BIRC5/survivin. Interacts
with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the
kinase catalytic domain) (By similarity). Interacts with FGFR4 (By
similarity). Interacts with STAT3; the interaction is independent
of STAT3 TYR-705 phosphorylation status (By similarity). Interacts
with OCAD1 (By similarity). {ECO:0000250|UniProtKB:P40763,
ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:19427337}.
-!- INTERACTION:
O13097:efnb1 (xeno); NbExp=4; IntAct=EBI-10764775, EBI-15667006;
Q9NRF2:SH2B1 (xeno); NbExp=2; IntAct=EBI-10764775, EBI-310491;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Shuttles between the nucleus and the
cytoplasm. Translocated into the nucleus upon tyrosine
phosphorylation and dimerization, in response to signaling by
activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear
presence is independent of tyrosine phosphorylation. Predominantly
present in the cytoplasm without stimuli. Upon leukemia inhibitory
factor (LIF) stimulation, accumulates in the nucleus. The complex
composed of BART and ARL2 plays an important role in the nuclear
translocation and retention of STAT3 (By similarity).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in lung, heart, oviduct, ovary,
uterus and kidney (at protein level). Detected in ovary, oviduct,
and at lower levels in uterus and lung.
-!- PTM: Activated through tyrosine phosphorylation by BMX. Tyrosine
phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF,
CSF1, EGF, PDGF, IFN-alpha and OSM. Activated KIT promotes
phosphorylation on tyrosine residues and subsequent translocation
to the nucleus. Tyrosine phosphorylated in response to
constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4.
Phosphorylated on serine upon DNA damage, probably by ATM or ATR.
Serine phosphorylation is important for the formation of stable
DNA-binding STAT3 homodimers and maximal transcriptional activity.
ARL2BP may participate in keeping the phosphorylated state of
STAT3 within the nucleus. Tyrosine phosphorylated upon stimulation
with EGF. Upon LPS challenge, phosphorylated within the nucleus by
IRAK1. Phosphorylated on Ser-727 by RPS6KA5 (By similarity).
Phosphorylation at Tyr-705 by FER or PTK6 leads to an increase of
its transcriptional activity. Dephosphorylation on tyrosine
residues by PTPN2 negatively regulates IL6/interleukin-6 signaling
(By similarity). {ECO:0000250}.
-!- PTM: Acetylated on lysine residues by CREBBP. Deacetylation by
LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3
transcription activity. Oxidation of lysine residues to allysine
on STAT3 preferentially takes place on lysine residues that are
acetylated. {ECO:0000250|UniProtKB:P40763}.
-!- PTM: Some lysine residues are oxidized to allysine by LOXL3,
leading to disrupt STAT3 dimerization and inhibit STAT3
transcription activity. Oxidation of lysine residues to allysine
on STAT3 preferentially takes place on lysine residues that are
acetylated. {ECO:0000250|UniProtKB:P40763}.
-!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X91810; CAA62920.1; -; mRNA.
EMBL; BC087025; AAH87025.1; -; mRNA.
RefSeq; NP_036879.1; NM_012747.2.
UniGene; Rn.10247; -.
ProteinModelPortal; P52631; -.
SMR; P52631; -.
BioGrid; 247196; 2.
CORUM; P52631; -.
DIP; DIP-44909N; -.
IntAct; P52631; 5.
MINT; MINT-1529438; -.
STRING; 10116.ENSRNOP00000026760; -.
ChEMBL; CHEMBL1764933; -.
iPTMnet; P52631; -.
PhosphoSitePlus; P52631; -.
PaxDb; P52631; -.
PRIDE; P52631; -.
Ensembl; ENSRNOT00000026760; ENSRNOP00000026760; ENSRNOG00000019742.
GeneID; 25125; -.
KEGG; rno:25125; -.
CTD; 6774; -.
RGD; 3772; Stat3.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOGENOM; HOG000220792; -.
HOVERGEN; HBG055669; -.
InParanoid; P52631; -.
KO; K04692; -.
OMA; NSMSFAE; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P52631; -.
TreeFam; TF318648; -.
Reactome; R-RNO-1266695; Interleukin-7 signaling.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-186763; Downstream signal transduction.
Reactome; R-RNO-447115; Interleukin-12 family signaling.
Reactome; R-RNO-6783589; Interleukin-6 family signaling.
Reactome; R-RNO-6783783; Interleukin-10 signaling.
Reactome; R-RNO-6785807; Interleukin-4 and 13 signaling.
Reactome; R-RNO-8849474; PTK6 Activates STAT3.
Reactome; R-RNO-8854691; Interleukin-20 family signaling.
Reactome; R-RNO-8875791; MET activates STAT3.
Reactome; R-RNO-8983432; Interleukin-15 signaling.
Reactome; R-RNO-8984722; Interleukin-35 Signalling.
PRO; PR:P52631; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000019742; -.
Genevisible; P52631; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0000790; C:nuclear chromatin; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:RGD.
GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:RGD.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:RGD.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:RGD.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:RGD.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:RGD.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; ISO:RGD.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI.
GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0042755; P:eating behavior; ISS:UniProtKB.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:RGD.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:RGD.
GO; GO:0007259; P:JAK-STAT cascade; TAS:RGD.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; ISS:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; ISO:RGD.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:RGD.
GO; GO:0045820; P:negative regulation of glycolytic process; ISO:RGD.
GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD.
GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:RGD.
GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISO:RGD.
GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; IMP:RGD.
GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:RGD.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
GO; GO:0060019; P:radial glial cell differentiation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:RGD.
GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0044321; P:response to leptin; ISS:UniProtKB.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISO:RGD.
CDD; cd10374; SH2_STAT3; 1.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR035855; STAT3_SH2.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_N.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; SH2 domain;
Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P40763}.
CHAIN 2 770 Signal transducer and activator of
transcription 3.
/FTId=PRO_0000182419.
DOMAIN 580 670 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOTIF 150 162 Essential for nuclear import.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 601 601 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 601 601 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 615 615 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 615 615 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 631 631 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 631 631 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 685 685 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 685 685 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 705 705 Phosphotyrosine; by FER and PTK6.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 707 707 N6-acetyllysine.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 714 714 Phosphothreonine.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 727 727 Phosphoserine; by DYRK2, NLK, NEK6,
IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE.
{ECO:0000250|UniProtKB:P40763}.
SEQUENCE 770 AA; 88040 MW; D74A0C76954754ED CRC64;
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL
LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA
TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK
SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL
ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ
HRPMLEERIV DLFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY
QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN
GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY
NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS
GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM
DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN
TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDMD LTSECATSPM


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