Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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IL4_13 Interleukins 4 and 13

SMART accession number:	SM00190
Description:	Interleukins-4 and -13 are cytokines involved in inflammatory and immune responses. IL-4 stimulates B and T cells.
Interpro abstract (IPR001325):	Interleukin-4 (IL-4) is a cytokine that plays a central role in the control and regulation of the immune and inflammatory system [ (PUBMED:3284813) (PUBMED:1693082) ]. IL-4 is a participant in several B-cell activation processes. It also stimulates other cell types such as T cells or mast cells. IL-4 is a glycoprotein that contains three disulphide bonds [ (PUBMED:1993171) ]. Interleukin-13 (IL-13) is a pleiotropic cytokine which may be important in the regulation of the inflammatory and immune responses [ (PUBMED:8096327) ]. The sequences of IL-4 and IL-13 are distantly related. This entry represetns both IL-4 and IL-13.
GO process:	immune response (GO:0006955)
GO component:	extracellular region (GO:0005576)
GO function:	cytokine receptor binding (GO:0005126)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 277 IL4_13 domains in 277 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing IL4_13 domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with IL4_13 domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing IL4_13 domain in the selected taxonomic class.

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Bamborough P, Duncan D, Richards WG
  • Predictive modelling of the 3-D structure of interleukin-13.
  • Protein Eng. 1994; 7: 1077-82
  • Display abstract

  • Several atomic structures are now available for the family of helical cytokines, which includes growth hormone as well as many of the interleukins. Using structural information from five members of this family, two alternative models of interleukin (IL)-13 are proposed. IL-13 has biological properties similar to those of IL-4 and, like the other interleukins, is a potentially important pharmaceutical target. The model of IL-13 is discussed and compared with the known interleukin structures.

  • Minty A et al.
  • Interleukin-13 is a new human lymphokine regulating inflammatory and immune responses.
  • Nature. 1993; 362: 248-50
  • Display abstract

  • The discovery of new cytokines normally relies on a prior knowledge of at least one of their biological effects, which is used as a criterion either for the purification of the protein or for the isolation of the complementary DNA by expression cloning. However, the redundancy of cytokine activities complicates the discovery of novel cytokines in this way, and the pleiotropic nature of many cytokines means that the principal activities of a new cytokine may bear little relation to that used for its isolation. We have adopted an alternative approach which relies on differential screening of an organized subtracted cDNA library from activated peripheral blood mononuclear cells, using the inducibility of lymphokine messenger RNAs by anti-CD28 as a primary screening criterion. The ligation of the CD28 antigen on the T lymphocyte by a surface antigen, B7/BB-1, expressed on activated B lymphocytes and monocytes is a key step in the activation of T lymphocytes and the accumulation of lymphokine mRNAs. Here we report the discovery by molecular cloning of a new interleukin (interleukin-13 or IL-13) expressed in activated human T lymphocytes. Recombinant IL-13 protein inhibits inflammatory cytokine production induced by lipopolysaccharide in human peripheral blood monocytes. Moreover, it synergizes with IL-2 in regulating interferon-gamma synthesis in large granular lymphocytes. Recent mapping of the IL-13 gene shows that it is closely linked to the IL-4 gene on chromosome 5q 23-31 (ref. 4). Interleukin-13 may be critical in regulating inflammatory and immune responses.

  • Yokota T et al.
  • Molecular biology of interleukin 4 and interleukin 5 genes and biology of their products that stimulate B cells, T cells and hemopoietic cells.
  • Immunol Rev. 1988; 102: 137-87
• Metabolism (metabolic pathways involving proteins which contain this domain)

• % proteins involved KEGG pathway ID Description 33.33 map04664 Fc epsilon RI signaling pathway 33.33 map04060 Cytokine-cytokine receptor interaction 16.67 map04640 Hematopoietic cell lineage 16.67 map04660 T cell receptor signaling pathway This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with IL4_13 domain which could be assigned to a KEGG orthologous group, and not all proteins containing IL4_13 domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of IL4_13 domains in PDB

  PDB code	Main view	Title
  1bbn		THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
  1bcn		THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
  1cyl		ASPECTS OF RECEPTOR BINDING AND SIGNALLING OF INTERLEUKIN-4 INVESTIGATED BY SITE-DIRECTED MUTAGENESIS AND NMR SPECTROSCOPY
  1ga3		NMR STRUCTURE OF INTERLEUKIN-13
  1hij		INTERLEUKIN-4 MUTANT WITH ARG 88 REPLACED WITH GLN (R88Q)
  1hik		INTERLEUKIN-4 (WILD-TYPE)
  1hzi		INTERLEUKIN-4 MUTANT E9A
  1iar		INTERLEUKIN-4 / RECEPTOR ALPHA CHAIN COMPLEX
  1ijz		Solution Structure of Human IL-13
  1ik0		Solution Structure of Human IL-13
  1iti		THE HIGH RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 DETERMINED BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
  1itl		HUMAN INTERLEUKIN 4: THE SOLUTION STRUCTURE OF A FOUR-HELIX-BUNDLE PROTEIN
  1itm		ANALYSIS OF THE SOLUTION STRUCTURE OF HUMAN INTERLEUKIN 4 DETERMINED BY HETERONUCLEAR THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE TECHNIQUES
  1rcb		CRYSTAL STRUCTURE OF HUMAN RECOMBINANT INTERLEUKIN-4 AT 2.25 ANGSTROMS RESOLUTION
  2b8u		Crystal structure of wildtype human Interleukin-4
  2b8x		Crystal stucture of the interleukin-4 variant F82D
  2b8y		Crystal structure of the interleukin-4 variant T13DF82D
  2b8z		Crystal structure of the interleukin-4 variant R85A
  2b90		Crystal structure of the interleukin-4 variant T13DR85A
  2b91		Crystal structure of the interleukin-4 variant F82DR85A
  2cyk		ASPECTS OF RECEPTOR BINDING AND SIGNALLING OF INTERLEUKIN-4 INVESTIGATED BY SITE-DIRECTED MUTAGENESIS AND NMR SPECTROSCOPY
  2d48		Crystal structure of the Interleukin-4 variant T13D
  2int		CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4
  3bpl		Crystal structure of the IL4-IL4R-Common Gamma ternary complex
  3bpn		Crystal structure of the IL4-IL4R-IL13Ra ternary complex
  3bpo		Crystal structure of the IL13-IL4R-IL13Ra ternary complex
  3g6d		Crystal structure of the complex between CNTO607 Fab and IL-13
  3l5w		Crystal structure of the complex between IL-13 and C836 FAB
  3l5x		Crystal structure of the complex between IL-13 and H2L6 FAB
  3lb6		The structure of IL-13 in complex with IL-13Ralpha2
  3qb7		Interleukin-4 mutant RGA bound to cytokine receptor common gamma
  4i77		Lebrikizumab Fab bound to IL-13
  4ps4		Crystal structure of the complex between IL-13 and M1295 FAB
  4ydy		4YDY
  5e4e		5E4E
  5fhx		5FHX

• Links (links to other resources describing this domain)

• INTERPRO	IPR001325
  PFAM	Interleukin4
  PROSITE	INTERLEUKIN_4_13

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