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IL13_MOUSE
ID   IL13_MOUSE              Reviewed;         131 AA.
AC   P20109;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Interleukin-13;
DE            Short=IL-13;
DE   AltName: Full=T-cell activation protein P600;
DE   Flags: Precursor;
GN   Name=Il13; Synonyms=Il-13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2521353;
RA   Brown K.D., Zurawski S.M., Mosmann T.R., Zurawski G.;
RT   "A family of small inducible proteins secreted by leukocytes are members of
RT   a new superfamily that includes leukocyte and fibroblast-derived
RT   inflammatory agents, growth factors, and indicators of various activation
RT   processes.";
RL   J. Immunol. 142:679-687(1989).
RN   [2]
RP   FUNCTION.
RX   PubMed=8871614;
RA   Takeda K., Kamanaka M., Tanaka T., Kishimoto T., Akira S.;
RT   "Impaired IL-13-mediated functions of macrophages in STAT6-deficient
RT   mice.";
RL   J. Immunol. 157:3220-3222(1996).
RN   [3]
RP   FUNCTION.
RX   PubMed=15361238; DOI=10.1111/j.0105-2896.2004.00192.x;
RA   Finkelman F.D., Shea-Donohue T., Morris S.C., Gildea L., Strait R.,
RA   Madden K.B., Schopf L., Urban J.F. Jr.;
RT   "Interleukin-4- and interleukin-13-mediated host protection against
RT   intestinal nematode parasites.";
RL   Immunol. Rev. 201:139-155(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=25847241; DOI=10.1074/jbc.m114.622126;
RA   Edukulla R., Singh B., Jegga A.G., Sontake V., Dillon S.R., Madala S.K.;
RT   "Th2 Cytokines Augment IL-31/IL-31RA Interactions via STAT6-dependent IL-
RT   31RA Expression.";
RL   J. Biol. Chem. 290:13510-13520(2015).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=29305434; DOI=10.4049/jimmunol.1701256;
RA   Duffen J., Zhang M., Masek-Hammerman K., Nunez A., Brennan A.,
RA   Jones J.E.C., Morin J., Nocka K., Kasaian M.;
RT   "Modulation of the IL-33/IL-13 Axis in Obesity by IL-13Ralpha2.";
RL   J. Immunol. 200:1347-1359(2018).
RN   [6]
RP   FUNCTION.
RX   PubMed=34795444; DOI=10.1038/s41590-021-01067-0;
RA   Mayer J.U., Hilligan K.L., Chandler J.S., Eccles D.A., Old S.I.,
RA   Domingues R.G., Yang J., Webb G.R., Munoz-Erazo L., Hyde E.J.,
RA   Wakelin K.A., Tang S.C., Chappell S.C., von Daake S., Brombacher F.,
RA   Mackay C.R., Sher A., Tussiwand R., Connor L.M., Gallego-Ortega D.,
RA   Jankovic D., Le Gros G., Hepworth M.R., Lamiable O., Ronchese F.;
RT   "Homeostatic IL-13 in healthy skin directs dendritic cell differentiation
RT   to promote TH2 and inhibit TH17 cell polarization.";
RL   Nat. Immunol. 22:1538-1550(2021).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=34789557; DOI=10.4049/jimmunol.2100655;
RA   Zhang M., Duffen J.L., Nocka K.H., Kasaian M.T.;
RT   "IL-13 Controls IL-33 Activity through Modulation of ST2.";
RL   J. Immunol. 0:0-0(2021).
CC   -!- FUNCTION: Cytokine that plays important roles in allergic inflammation
CC       and immune response to parasite infection (PubMed:15361238). Synergizes
CC       with IL2 in regulating interferon-gamma synthesis. Stimulates B-cell
CC       proliferation, and activation of eosinophils, basophils, and mast cells
CC       (By similarity). Plays an important role in controlling IL33 activity
CC       by modulating the production of transmembrane and soluble forms of
CC       interleukin-1 receptor-like 1/IL1RL1 (PubMed:34789557). Displays the
CC       capacity to antagonize Th1-driven proinflammatory immune response and
CC       downregulates synthesis of many proinflammatory cytokines including
CC       IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially
CC       involves suppression of NF-kappa-B (By similarity). Functions also on
CC       nonhematopoietic cells, including endothelial cells where it induces
CC       vascular cell adhesion protein 1/VCAM1, which is important in the
CC       recruitment of eosinophils. Exerts its biological effects through its
CC       receptors which comprises the IL4R chain and the IL13RA1 chain, to
CC       activate JAK1 and TYK2, leading to the activation of STAT6
CC       (PubMed:8871614, PubMed:34795444). Aside from IL13RA1, another receptor
CC       IL13RA2 acts as a high affinity decoy for IL13 and mediates
CC       internalization and depletion of extracellular IL13 (PubMed:29305434).
CC       {ECO:0000250|UniProtKB:P35225, ECO:0000250|UniProtKB:P42203,
CC       ECO:0000269|PubMed:15361238, ECO:0000269|PubMed:29305434,
CC       ECO:0000269|PubMed:34789557, ECO:0000269|PubMed:34795444,
CC       ECO:0000269|PubMed:8871614}.
CC   -!- SUBUNIT: Interacts with IL13RA2. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P20109; O88786: Il13ra2; NbExp=4; IntAct=EBI-20559598, EBI-20260800;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DISRUPTION PHENOTYPE: Deletion mice have increased eosinophilic
CC       inflammation and splenomegaly (PubMed:29305434). In addition, mice show
CC       exacerbated effects of IL33 administration, including increased immune
CC       cell infiltration in the peritoneum with expanded eosinophil and ILC2
CC       populations, and reduced circulating and peritoneal sST2
CC       (PubMed:34789557). {ECO:0000269|PubMed:29305434,
CC       ECO:0000269|PubMed:34789557}.
CC   -!- SIMILARITY: Belongs to the IL-4/IL-13 family. {ECO:0000305}.
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DR   EMBL; M23504; AAA40149.1; -; mRNA.
DR   CCDS; CCDS24683.1; -.
DR   PIR; E30552; E30552.
DR   RefSeq; NP_032381.1; NM_008355.3.
DR   AlphaFoldDB; P20109; -.
DR   SMR; P20109; -.
DR   IntAct; P20109; 2.
DR   STRING; 10090.ENSMUSP00000020650; -.
DR   GlyGen; P20109; 3 sites.
DR   PaxDb; P20109; -.
DR   PRIDE; P20109; -.
DR   ProteomicsDB; 267315; -.
DR   ABCD; P20109; 1 sequenced antibody.
DR   Antibodypedia; 14499; 1206 antibodies from 43 providers.
DR   DNASU; 16163; -.
DR   Ensembl; ENSMUST00000020650; ENSMUSP00000020650; ENSMUSG00000020383.
DR   GeneID; 16163; -.
DR   KEGG; mmu:16163; -.
DR   UCSC; uc007iwr.2; mouse.
DR   CTD; 3596; -.
DR   MGI; MGI:96541; Il13.
DR   VEuPathDB; HostDB:ENSMUSG00000020383; -.
DR   eggNOG; ENOG502SZKX; Eukaryota.
DR   GeneTree; ENSGT00390000003225; -.
DR   HOGENOM; CLU_158063_0_0_1; -.
DR   InParanoid; P20109; -.
DR   OMA; MVWSVNL; -.
DR   OrthoDB; 1578920at2759; -.
DR   PhylomeDB; P20109; -.
DR   TreeFam; TF336383; -.
DR   BioGRID-ORCS; 16163; 1 hit in 75 CRISPR screens.
DR   PRO; PR:P20109; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P20109; protein.
DR   Bgee; ENSMUSG00000020383; Expressed in secondary oocyte and 8 other tissues.
DR   Genevisible; P20109; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005144; F:interleukin-13 receptor binding; ISO:MGI.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0042116; P:macrophage activation; ISO:MGI.
DR   GO; GO:0001774; P:microglial cell activation; ISO:MGI.
DR   GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; ISO:MGI.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; ISO:MGI.
DR   GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR   GO; GO:0071635; P:negative regulation of transforming growth factor beta production; ISO:MGI.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0032723; P:positive regulation of connective tissue growth factor production; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:MGI.
DR   GO; GO:0043270; P:positive regulation of ion transport; ISO:MGI.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; IMP:BHF-UCL.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:MGI.
DR   GO; GO:2000231; P:positive regulation of pancreatic stellate cell proliferation; ISO:MGI.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR   GO; GO:0010155; P:regulation of proton transport; ISO:MGI.
DR   GO; GO:0035094; P:response to nicotine; ISO:MGI.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR020470; IL-13.
DR   InterPro; IPR001325; IL-4/IL-13.
DR   InterPro; IPR018096; IL-4/IL-13_CS.
DR   Pfam; PF03487; IL13; 1.
DR   PRINTS; PR01929; INTRLEUKIN13.
DR   SMART; SM00190; IL4_13; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00838; INTERLEUKIN_4_13; 1.
PE   1: Evidence at protein level;
KW   Cytokine; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..131
FT                   /note="Interleukin-13"
FT                   /id="PRO_0000015550"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..79
FT                   /evidence="ECO:0000250|UniProtKB:P35225"
FT   DISULFID        67..93
FT                   /evidence="ECO:0000250|UniProtKB:P35225"
SQ   SEQUENCE   131 AA;  14108 MW;  954F93F105713FED CRC64;
     MALWVTAVLA LACLGGLAAP GPVPRSVSLP LTLKELIEEL SNITQDQTPL CNGSMVWSVD
     LAAGGFCVAL DSLTNISNCN AIYRTQRILH GLCNRKAPTT VSSLPDTKIE VAHFITKLLS
     YTKQLFRHGP F
 
 
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