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IL13_BOVIN
ID   IL13_BOVIN              Reviewed;         132 AA.
AC   Q9XSV9; A9QWR5; Q9TV84;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Interleukin-13;
DE            Short=IL-13;
DE   Flags: Precursor;
GN   Name=IL13;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10436181; DOI=10.1007/s002510050567;
RA   Buitkamp J., Jann O., Fries R.;
RT   "The cattle interleukin-13 gene: genomic organization, chromosomal
RT   location, and evolution of the promoter.";
RL   Immunogenetics 49:872-878(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Belted Galloway; TISSUE=Peripheral blood;
RG   U.S. Veterinary Immune Reagent Network;
RA   Hudgens T., Tompkins D., Baldwin C.L.;
RT   "U.S. veterinary immune reagent network: expressed bovine gene sequences.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-114.
RA   Trigona W.T., Hirano A., Brown W.;
RT   "Biological activities of interleukin-13 (IL-13) on bovine lymphocytes:
RT   implications for signaling through IL-13Ra1.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytokine that plays important roles in allergic inflammation
CC       and immune response to parasite infection. Synergizes with IL2 in
CC       regulating interferon-gamma synthesis. Stimulates B-cell proliferation,
CC       and activation of eosinophils, basophils, and mast cells (By
CC       similarity). Plays an important role in controlling IL33 activity by
CC       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 (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. 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:0000250|UniProtKB:P42203}.
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; AJ132441; CAB46636.1; -; Genomic_DNA.
DR   EMBL; EU276077; ABX72075.1; -; mRNA.
DR   EMBL; AF072807; AAD22748.1; -; mRNA.
DR   RefSeq; NP_776514.1; NM_174089.1.
DR   AlphaFoldDB; Q9XSV9; -.
DR   SMR; Q9XSV9; -.
DR   STRING; 9913.ENSBTAP00000021212; -.
DR   PaxDb; Q9XSV9; -.
DR   PRIDE; Q9XSV9; -.
DR   Ensembl; ENSBTAT00000021212; ENSBTAP00000021212; ENSBTAG00000015953.
DR   GeneID; 281247; -.
DR   KEGG; bta:281247; -.
DR   CTD; 3596; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015953; -.
DR   VGNC; VGNC:30114; IL13.
DR   eggNOG; ENOG502SZKX; Eukaryota.
DR   GeneTree; ENSGT00390000003225; -.
DR   HOGENOM; CLU_158063_0_0_1; -.
DR   InParanoid; Q9XSV9; -.
DR   OMA; MVWSVNL; -.
DR   OrthoDB; 1578920at2759; -.
DR   TreeFam; TF336383; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000015953; Expressed in anterior segment of eyeball and 12 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005126; F:cytokine receptor binding; IEA:InterPro.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR   GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IEA:Ensembl.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
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..132
FT                   /note="Interleukin-13"
FT                   /id="PRO_0000015545"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
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        48..76
FT                   /evidence="ECO:0000250|UniProtKB:P35225"
FT   DISULFID        64..90
FT                   /evidence="ECO:0000250|UniProtKB:P35225"
FT   CONFLICT        84
FT                   /note="R -> K (in Ref. 1; CAB46636)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   132 AA;  14651 MW;  61A662EB85C161F3 CRC64;
     MALLLTAVIV LICFGGLTSP SPVPSATALK ELIEELVNIT QNQKVPLCNG SMVWSLNLTS
     SMYCAALDSL ISISNCSVIQ RTKRMLNALC PHKPSAKQVS SEYVRDTKIE VAQFLKDLLR
     HSRIVFRNER FN
 
 
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