| Type: | Conserved_site | Name: | Long hematopoietin receptor, soluble alpha chain, conserved site |
| Description: | A number of receptors for lymphokines, hematopoietic growth factors and growth hormone-related molecules have been found to share a common binding domain. These receptors are designated as hematopoietin receptors [] and the corresponding ligands as hematopoietins. Further, hematopoietins have been subdivided into two major structural groups: Large/long and small/short hematopoietins.One subset of individual receptor chains that are part of receptor complexes for large hematopoietins contain common structural elements in their extracellular parts: an immunoglobulin-like domain at the N-terminal end of the hematopoietin receptor domain (except for the EBCV-induced interleukin-12 beta chain) and a short (or no) cytoplasmic domain. They define a structural subgroup containing the following chains: Interleukin-6 receptor alpha chain (IL6RA). Interleukin-11 receptor alpha chain (IL11RA), Ciliary neurotrophic factor receptor alpha chain (CNTFRA), Interleukin-12 beta chain p40 (IL12BC), Interleukin-12 beta chain induced by Epstein-Barr virus(strain GD1) (HHV-4) (Human herpesvirus 4).Members of this subgroup bind to their cognate cytokines with low affinity and possess transmembrane and short cytoplasmic domains (IL6RA and IL11RA), or are GPi-linked membrane proteins (CNTFRA). Truncated soluble forms of IL-6 and CNTF receptors alpha chains are physiologically active []. IL-12 is an heterodimeric cytokine made of an alpha chain (p35) and a beta chain (p40). p40 (IL12BC) can be regarded as an alpha chain receptor devoid of cytoplasmic domain []. Members of this family have the ability to bind corresponding cytokines with no signalling function. | Short Name: | Hematopoietin_rcpt_L_F3_CS |
