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IL13_RAT
ID   IL13_RAT                Reviewed;         131 AA.
AC   P42203;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 136.
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   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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney cortex;
RX   PubMed=7916615; DOI=10.1006/bbrc.1993.2523;
RA   Lakkis F.G., Cruet E.N.;
RT   "Cloning of rat interleukin-13 (IL-13) cDNA and analysis of IL-13 gene
RT   expression in experimental glomerulonephritis.";
RL   Biochem. Biophys. Res. Commun. 197:612-618(1993).
RN   [2]
RP   FUNCTION.
RX   PubMed=9366558; DOI=10.1172/jci119786;
RA   Lentsch A.B., Shanley T.P., Sarma V., Ward P.A.;
RT   "In vivo suppression of NF-kappa B and preservation of I kappa B alpha by
RT   interleukin-10 and interleukin-13.";
RL   J. Clin. Invest. 100:2443-2448(1997).
CC   -!- FUNCTION: Cytokine that plays important roles in allergic inflammation
CC       and immune response to parasite infection (PubMed:9366558). 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 (By similarity). 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 (PubMed:9366558). 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. Aside from
CC       IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for
CC       IL13 and mediates internalization and depletion of extracellular IL13
CC       (By similarity). {ECO:0000250|UniProtKB:P20109,
CC       ECO:0000250|UniProtKB:P35225, ECO:0000269|PubMed:9366558}.
CC   -!- SUBUNIT: Interacts with IL13RA2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the IL-4/IL-13 family. {ECO:0000305}.
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DR   EMBL; L26913; AAA16478.1; -; mRNA.
DR   PIR; I52290; I52290.
DR   RefSeq; NP_446280.1; NM_053828.1.
DR   AlphaFoldDB; P42203; -.
DR   SMR; P42203; -.
DR   STRING; 10116.ENSRNOP00000010121; -.
DR   GlyGen; P42203; 4 sites.
DR   PaxDb; P42203; -.
DR   Ensembl; ENSRNOT00000010121; ENSRNOP00000010121; ENSRNOG00000007652.
DR   GeneID; 116553; -.
DR   KEGG; rno:116553; -.
DR   UCSC; RGD:68949; rat.
DR   CTD; 3596; -.
DR   RGD; 68949; Il13.
DR   eggNOG; ENOG502SZKX; Eukaryota.
DR   GeneTree; ENSGT00390000003225; -.
DR   HOGENOM; CLU_158063_0_0_1; -.
DR   InParanoid; P42203; -.
DR   OMA; MVWSVNL; -.
DR   OrthoDB; 1578920at2759; -.
DR   PhylomeDB; P42203; -.
DR   TreeFam; TF336383; -.
DR   PRO; PR:P42203; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000007652; Expressed in thymus and 5 other tissues.
DR   Genevisible; P42203; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005144; F:interleukin-13 receptor binding; IPI:RGD.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:RGD.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:0042116; P:macrophage activation; ISO:RGD.
DR   GO; GO:0001774; P:microglial cell activation; IMP:RGD.
DR   GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; ISO:RGD.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IMP:RGD.
DR   GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR   GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IDA:RGD.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:RGD.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0032723; P:positive regulation of connective tissue growth factor production; IDA:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:RGD.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
DR   GO; GO:0043270; P:positive regulation of ion transport; IDA:RGD.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:RGD.
DR   GO; GO:2000231; P:positive regulation of pancreatic stellate cell proliferation; IDA:RGD.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IDA:RGD.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:RGD.
DR   GO; GO:0010155; P:regulation of proton transport; IDA:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0035094; P:response to nicotine; IDA:RGD.
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   2: Evidence at transcript 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_0000015553"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..80
FT                   /evidence="ECO:0000250|UniProtKB:P35225"
FT   DISULFID        68..94
FT                   /evidence="ECO:0000250|UniProtKB:P35225"
SQ   SEQUENCE   131 AA;  14093 MW;  E5008CAB8DE8C201 CRC64;
     MALWVTAVLA LACLGGLATP GPVRRSTSPP VALRELIEEL SNITQDQKTS LCNSSMVWSV
     DLTAGGFCAA LESLTNISSC NAIHRTQRIL NGLCNQKASD VASSPPDTKI EVAQFISKLL
     NYSKQLFRYG H
 
 
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