IL13RA2 Protein Overview: Sequence, Structure, Function and Protein Interaction

IL13RA2 Protein Overview

Because IL4 and IL13 and their specific signaling pathways are considered attractive targets for the treatment of allergy and asthma, Kelly-Welch et al. (2003) reviewed the signaling connections of these cytokines. IL4 interacts with IL4R with high affinity, leading to dimerization with either the common gamma chain (IL2RG; 308380), a component of receptors for a number of cytokines, to create a type I receptor, or with IL13RA1 to form a type II receptor. IL13, on the other hand, binds with high affinity to IL13RA1, which induces heterodimerization with IL4R to form a complex identical to the type II receptor. Alternatively, IL13 may bind with even greater affinity to IL13RA2, which fails to induce a signal, indicating that it acts as a decoy receptor. The C-terminal tails of the IL4 and IL13 receptor subunits interact with tyrosine kinases of the Janus kinase family (e.g., JAK1; 147795), leading to interaction with STAT6 (601512), which binds to consensus sequences in the promoters of IL4- and IL13-regulated genes. Kelly-Welch et al. (2003) proposed that subtle differences in IL4 and IL13 signaling due to polymorphisms near docking sites in IL4R may have profound implications for allergy and asthma. By in vivo selection, transcriptomic analysis, functional verification, and clinical validation, Minn et al. (2005) identified a set of genes that marks and mediates breast cancer metastasis to the lungs. Some of these genes serve dual functions, providing growth advantages both in the primary tumor and in the lung microenvironment. Others contribute to aggressive growth selectivity in the lung. Among the lung metastasis signature genes identified, several, including IL13RA2, were functionally validated. Those subjects expressing the lung metastasis signature had a significantly poorer lung metastasis-free survival, but not bone metastasis-free survival, compared to subjects without the signature. Ng et al. (2010) showed that paternal high-fat diet exposure programs beta cell dysfunction in rat F1 female offspring through an epigenetic effect. Chronic high-fat diet consumption in Sprague-Dawley fathers induced increased body weight, adiposity, impaired glucose tolerance, and insulin sensitivity. Relative to controls, their female offspring had an early onset of impaired insulin secretion and glucose tolerance that worsened with time, and normal adiposity. Paternal high-fat diet altered the expression of 642 pancreatic islet genes in adult female offspring (P less than 0.01); the genes belonged to 13 functional clusters, including cation and ATP binding, cytoskeleton, and intracellular transport. Broader pathway analysis of 2,492 genes differentially expressed (P less than 0.05) demonstrated involvement of calcium-, MAPK-, and Wnt-signaling pathways, apoptosis, and the cell cycle. Hypomethylation of the Il13ra2 gene, which showed the highest fold difference in expression (1.76-fold increase), was demonstrated. Ng et al. (2010) concluded that this was the first report in mammals of nongenetic, intergenerational transmission of metabolic sequelae of a high-fat diet from father to offspring.

IL13RA2 protein family

Belongs to the type I cytokine receptor family. Type 5 subfamily.

IL13RA2 protein name

Recommended name
Interleukin-13 receptor subunit alpha-2
Short name
IL-13 receptor subunit alpha-2||IL-13R subuni
cancer / testis antigen 19, CD213a2, CT19, IL13BP, IL-13R
Alternative name
Interleukin-13-binding protein CD_antigen: CD213a2

IL13RA2 Gene family protein

IL13RA2 Protein Sequence

Species Human IL13RA2 protein
Length 380
Mass (Da) 44176
Sequence Human IL13RA2 protein sequence
Species Mouse IL13RA2 protein
Length 383
Mass (Da) 44483
Sequence Mouse IL13RA2 protein sequence
Species Rat IL13RA2 protein
Length 385
Mass (Da) 44622
Sequence Rat IL13RA2 protein sequence

IL13RA2 Protein Molecular Weight & PI

Interleukin-13 receptor subunit alpha-2 precursor (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (Interleukin-13-binding protein) (CD213a2 antigen) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 27-380 Interleukin-13 receptor subunit alpha-2.

Molecular weight (Da)


Theoretical pI


IL13RA2 Protein Structure

The structure of IL-13 in complex with IL-13Ralpha2
2010-01-07   Released:  2010-03-16
Deposition Author(s)
Lupardus, P.J., Garcia, K.C., Birnbaum, M.E.
Homo sapiens
Expression System
Trichoplusia ni
Experimental Data Snapshot
3.0500 Å
R-Value Free
R-Value Work
3LB6 From PDB

Human IL13RA2 protein Secondary structure

IL13RA2 Protein Interaction

Recombinant IL13RA2 Protein Feature

IL13RA2 Protein, Human, Recombinant (His & hFc Tag)

High Purity
> 75 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
High Activity
Measured by its binding ability in a functional ELISA. Immobilized human IL13Ra2-Fch (Cat: 10350-H03H) at 2 μg/mL (100 μl/well) can bind biotinylated human IL13 (Cat: 10369-HNAC), The EC50 of bind biotinylated human IL13 (Cat: 10369-HNAC) is 4-20 ng/mL.

Recombinant IL13RA2 protein citations

Therapeutic efficacy of a co-blockade of IL-13 and IL-25 on airway inflammation and remodeling in a mouse model of asthma
Zhang, FQ;Han, XP;Zhang, F;Ma, X;Xiang, D;Yang, XM;Ou-Yang, HF;Li, Z;
Int. Immunopharmacol
Chitinase 3-like 1-CD44 interaction promotes metastasis and epithelial-to-mesenchymal transition through β-catenin/Erk/Akt signaling in gastric cancer
Geng, B;Pan, J;Zhao, T;Ji, J;Zhang, C;Che, Y;Yang, J;Shi, H;Li, J;Zhou, H;Mu, X;Xu, C;Wang, C;Xu, Y;Liu, Z;Wen, H;You, Q;
J. Exp. Clin. Cancer Res.
Drug Conjugates for Targeting Eph Receptors in Glioblastoma
Sharma, P;Roberts, C;Herpai, D;Fokt, I;Priebe, W;Debinski, W;

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