ID   IL13_CAMBA              Reviewed;         136 AA.
AC   Q865W5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Interleukin-13;
DE            Short=IL-13;
DE   Flags: Precursor;
GN   Name=IL13;
OS   Camelus bactrianus (Bactrian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Odbileg R., Lee S.-I., Yoshida R., Chang K.-S., Ohashi K., Sugimoto C.,
RA   Onuma M.;
RT   "Cloning and sequence analysis of cytokine cDNAs of llama and camel.";
RL   Submitted (APR-2003) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB107658; BAC75395.1; -; mRNA.
DR   RefSeq; NP_001290450.1; NM_001303521.1.
DR   AlphaFoldDB; Q865W5; -.
DR   SMR; Q865W5; -.
DR   GeneID; 105082106; -.
DR   CTD; 3596; -.
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..136
FT                   /note="Interleukin-13"
FT                   /id="PRO_0000015546"
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   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
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   136 AA;  15289 MW;  A3F6F963C1D56D46 CRC64;
     MALWLTVVIA FTCIGGLASP VPTPSPKALK ELIEELVNIT QNQKAPLCNG SMVWSINLTT
     SMYCAARESL INITNCSVIQ RTQRMLNALC PHKLSAKVSS EHVRDTKIEV TQFIKTLLQH
     SRNVFHYRSF NWSKKS