ID   IL13_MACTH              Reviewed;         132 AA.
AC   Q5I6E4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Interleukin-13;
DE            Short=IL-13;
DE   Flags: Precursor;
GN   Name=IL13;
OS   Macaca thibetana (Pere David's macaque) (Tibetan macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=54602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wei K., Zou F.D., Yue B.S.;
RT   "Molecular cloning and characterization of the interleukin 13 (IL13) gene
RT   from Tibetan macaque (Macaca thibetana) and its expression in Escherichia
RT   coli.";
RL   Submitted (DEC-2004) 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; AY849927; AAW33961.1; -; mRNA.
DR   AlphaFoldDB; Q5I6E4; -.
DR   SMR; Q5I6E4; -.
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:0006955; P:immune response; IEA:InterPro.
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; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..132
FT                   /note="Interleukin-13"
FT                   /id="PRO_0000015549"
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        72
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"
SQ   SEQUENCE   132 AA;  14337 MW;  C2703F92343178C0 CRC64;
     MALLLTMVIA LTCLGGFASP SPVPPSTALK ELIEELVNIT QNQKAPLCNG SMVWSINLTA
     GVYCAALESL INVSGCSAIE KTQRMLNGFC PHKVSAGQFS SLRVRDTKIE VAQFVKDLLL
     HLKKLFREGQ FN