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Interleukin-4 (IL-4) (B-cell IgG differentiation factor) (B-cell growth factor 1) (B-cell stimulatory factor 1) (BSF-1) (IGG1 induction factor) (Lymphocyte stimulatory factor 1)

 IL4_MOUSE               Reviewed;         140 AA.
P07750;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=Interleukin-4;
Short=IL-4;
AltName: Full=B-cell IgG differentiation factor;
AltName: Full=B-cell growth factor 1;
AltName: Full=B-cell stimulatory factor 1;
Short=BSF-1;
AltName: Full=IGG1 induction factor;
AltName: Full=Lymphocyte stimulatory factor 1;
Flags: Precursor;
Name=Il4; Synonyms=Il-4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3005865; DOI=10.1038/319640a0;
Noma Y., Sideras P., Naito T., Bergstedt-Lindqvist S., Azuma C.,
Severinson E., Tanabe T., Kinashi T., Matsuda F., Yaoita Y., Honjo T.;
"Cloning of cDNA encoding the murine IgG1 induction factor by a novel
strategy using SP6 promoter.";
Nature 319:640-646(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=3029676; DOI=10.1093/nar/15.1.333;
Otsuka T., Villaret D., Yokota T., Takebe Y., Lee F., Arai N.,
Arai K.;
"Structural analysis of the mouse chromosomal gene encoding
interleukin 4 which expresses B cell, T cell and mast cell stimulating
activities.";
Nucleic Acids Res. 15:333-344(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=3083412; DOI=10.1073/pnas.83.7.2061;
Lee F., Yokota T., Otsuka T., Meyerson P., Villaret D., Coffman R.,
Mosmann T., Rennick D., Roehm N., Smith C., Zlotnik A., Arai K.;
"Isolation and characterization of a mouse interleukin cDNA clone that
expresses B-cell stimulatory factor 1 activities and T-cell- and mast-
cell-stimulating activities.";
Proc. Natl. Acad. Sci. U.S.A. 83:2061-2065(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=3498301;
Sideras P., Bergstedt-Lindqvist S., Severinson E., Noma Y., Naito T.,
Azuma C., Tanabe T., Kinashi T., Matsude F., Yaoita Y., Honjo T.;
"IgG1 induction factor: a single molecular entity with multiple
biological functions.";
Adv. Exp. Med. Biol. 213:227-236(1987).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
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).
[6]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=1993171; DOI=10.1021/bi00220a011;
Carr C., Aykent S., Kimack N.M., Levine A.D.;
"Disulfide assignments in recombinant mouse and human interleukin 4.";
Biochemistry 30:1515-1523(1991).
[7]
FUNCTION.
PubMed=25847241; DOI=10.1074/jbc.M114.622126;
Edukulla R., Singh B., Jegga A.G., Sontake V., Dillon S.R.,
Madala S.K.;
"Th2 Cytokines Augment IL-31/IL-31RA Interactions via STAT6-dependent
IL-31RA Expression.";
J. Biol. Chem. 290:13510-13520(2015).
-!- FUNCTION: Participates in at least several B-cell activation
processes as well as of other cell types (PubMed:3083412). It is a
costimulator of DNA-synthesis. It induces the expression of class
II MHC molecules on resting B-cells (PubMed:3498301). It enhances
both secretion and cell surface expression of IgE and IgG1
(PubMed:3498301). It also regulates the expression of the low
affinity Fc receptor for IgE (CD23) on both lymphocytes and
monocytes. Positively regulates IL31RA expression in macrophages
(PubMed:25847241). {ECO:0000269|PubMed:25847241,
ECO:0000269|PubMed:3083412, ECO:0000269|PubMed:3498301}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the IL-4/IL-13 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X03532; CAA27233.1; -; mRNA.
EMBL; X05064; CAA28731.1; -; Genomic_DNA.
EMBL; X05252; CAA28873.1; ALT_SEQ; Genomic_DNA.
EMBL; X05253; CAA28874.1; ALT_SEQ; Genomic_DNA.
EMBL; M13238; AAA39307.1; -; mRNA.
EMBL; M25892; AAA39298.1; -; mRNA.
EMBL; BC027514; AAH27514.1; -; mRNA.
CCDS; CCDS24682.1; -.
PIR; A25870; IIMSG1.
RefSeq; NP_067258.1; NM_021283.2.
UniGene; Mm.276360; -.
ProteinModelPortal; P07750; -.
SMR; P07750; -.
IntAct; P07750; 1.
STRING; 10090.ENSMUSP00000000889; -.
PhosphoSitePlus; P07750; -.
PaxDb; P07750; -.
PRIDE; P07750; -.
Ensembl; ENSMUST00000000889; ENSMUSP00000000889; ENSMUSG00000000869.
GeneID; 16189; -.
KEGG; mmu:16189; -.
UCSC; uc007iwq.2; mouse.
CTD; 3565; -.
MGI; MGI:96556; Il4.
eggNOG; KOG3886; Eukaryota.
eggNOG; ENOG410XQ0R; LUCA.
GeneTree; ENSGT00390000013108; -.
HOGENOM; HOG000254781; -.
HOVERGEN; HBG000290; -.
InParanoid; P07750; -.
KO; K05430; -.
OrthoDB; EOG091G0WDE; -.
PhylomeDB; P07750; -.
TreeFam; TF336383; -.
Reactome; R-MMU-6785807; Interleukin-4 and 13 signaling.
PRO; PR:P07750; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000869; -.
CleanEx; MM_IL4; -.
ExpressionAtlas; P07750; baseline and differential.
Genevisible; P07750; MM.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005125; F:cytokine activity; IDA:MGI.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005136; F:interleukin-4 receptor binding; IEA:InterPro.
GO; GO:0042113; P:B cell activation; IDA:MGI.
GO; GO:0031296; P:B cell costimulation; IDA:MGI.
GO; GO:0071288; P:cellular response to mercury ion; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IMP:UniProtKB.
GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
GO; GO:0097028; P:dendritic cell differentiation; ISO:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0002227; P:innate immune response in mucosa; IDA:BHF-UCL.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; ISO:MGI.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
GO; GO:0002677; P:negative regulation of chronic inflammatory response; IEA:Ensembl.
GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; ISO:MGI.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0043031; P:negative regulation of macrophage activation; IEA:Ensembl.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:MGI.
GO; GO:0050868; P:negative regulation of T cell activation; IDA:MGI.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0070351; P:negative regulation of white fat cell proliferation; IDA:CACAO.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:MGI.
GO; GO:0050871; P:positive regulation of B cell activation; IDA:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IDA:BHF-UCL.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
GO; GO:2000424; P:positive regulation of eosinophil chemotaxis; IEA:Ensembl.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:MGI.
GO; GO:0048295; P:positive regulation of isotype switching to IgE isotypes; IDA:MGI.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IDA:MGI.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:MGI.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IDA:MGI.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; IEA:Ensembl.
GO; GO:1901741; P:positive regulation of myoblast fusion; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045582; P:positive regulation of T cell differentiation; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:MGI.
GO; GO:0050776; P:regulation of immune response; IDA:MGI.
GO; GO:0010155; P:regulation of proton transport; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0002296; P:T-helper 1 cell lineage commitment; IGI:MGI.
GO; GO:0035745; P:T-helper 2 cell cytokine production; ISO:MGI.
GO; GO:0045064; P:T-helper 2 cell differentiation; IDA:MGI.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR002354; IL-4.
InterPro; IPR001325; IL-4/IL-13.
InterPro; IPR018096; IL-4/IL-13_CS.
Pfam; PF00727; IL4; 1.
PIRSF; PIRSF001941; Interleukin_4; 1.
PRINTS; PR00431; INTERLEUKIN4.
SMART; SM00190; IL4_13; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00838; INTERLEUKIN_4_13; 1.
1: Evidence at protein level;
B-cell activation; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Growth factor; Reference proteome; Secreted; Signal.
SIGNAL 1 20
CHAIN 21 140 Interleukin-4.
/FTId=PRO_0000015538.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 107 {ECO:0000269|PubMed:1993171}.
DISULFID 47 87 {ECO:0000269|PubMed:1993171}.
DISULFID 69 114 {ECO:0000269|PubMed:1993171}.
SEQUENCE 140 AA; 15834 MW; E43CE16195DE051F CRC64;
MGLNPQLVVI LLFFLECTRS HIHGCDKNHL REIIGILNEV TGEGTPCTEM DVPNVLTATK
NTTESELVCR ASKVLRIFYL KHGKTPCLKK NSSVLMELQR LFRAFRCLDS SISCTMNESK
STSLKDFLES LKSIMQMDYS


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