Interleukin 5 receptor alpha subunit

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IL5RA
PDB 1obx EBI.jpg
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIL5RA, CD125, CDw125, HSIL5R3, IL5R, Interleukin 5 receptor alpha subunit, interleukin 5 receptor subunit alpha
External IDsOMIM: 147851 MGI: 96558 HomoloGene: 473 GeneCards: IL5RA
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_008370

RefSeq (protein)

NP_032396

Location (UCSC)Chr 3: 3.07 – 3.13 MbChr 6: 106.71 – 106.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interleukin 5 receptor, alpha (IL5RA) also known as CD125 (Cluster of Differentiation 125) is a subunit of the Interleukin-5 receptor. IL5RA also denotes its human gene.[5]

Function[edit]

The protein encoded by this gene is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is composed of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Six alternatively spliced transcript variants encoding three distinct isoforms have been reported.[5]

Interactions[edit]

Interleukin 5 receptor alpha subunit has been shown to interact with:

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000091181 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005364 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: IL5RA interleukin 5 receptor, alpha".
  6. ^ Woodcock JM, Zacharakis B, Plaetinck G, Bagley CJ, Qiyu S, Hercus TR, Tavernier J, Lopez AF (Nov 1994). "Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF". EMBO J. 13 (21): 5176–85. doi:10.1002/j.1460-2075.1994.tb06848.x. PMC 395466. PMID 7957082.
  7. ^ Johanson K, Appelbaum E, Doyle M, Hensley P, Zhao B, Abdel-Meguid SS, Young P, Cook R, Carr S, Matico R (Apr 1995). "Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins". J. Biol. Chem. 270 (16): 9459–71. doi:10.1074/jbc.270.16.9459. PMID 7721873.
  8. ^ Murata Y, Takaki S, Migita M, Kikuchi Y, Tominaga A, Takatsu K (Feb 1992). "Molecular cloning and expression of the human interleukin 5 receptor". J. Exp. Med. 175 (2): 341–51. doi:10.1084/jem.175.2.341. PMC 2119102. PMID 1732409.
  9. ^ Ogata N, Kouro T, Yamada A, Koike M, Hanai N, Ishikawa T, Takatsu K (Apr 1998). "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and betac subunit, respectively, and are activated upon IL-5 stimulation". Blood. 91 (7): 2264–71. doi:10.1182/blood.V91.7.2264. PMID 9516124.
  10. ^ Cen O, Gorska MM, Stafford SJ, Sur S, Alam R (Mar 2003). "Identification of UNC119 as a novel activator of SRC-type tyrosine kinases". J. Biol. Chem. 278 (10): 8837–45. doi:10.1074/jbc.M208261200. PMID 12496276.
  11. ^ Geijsen N, Uings IJ, Pals C, Armstrong J, McKinnon M, Raaijmakers JA, Lammers JW, Koenderman L, Coffer PJ (Aug 2001). "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein". Science. 293 (5532): 1136–8. doi:10.1126/science.1059157. PMID 11498591. S2CID 28003281.

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.