Interleukin 10 receptor, alpha subunit

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IL10RA
Protein IL10RA PDB 1j7v.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases IL10RA, CD210, CD210a, CDW210A, HIL-10R, IL-10R1, IL10R, Interleukin 10 receptor, alpha subunit, interleukin 10 receptor subunit alpha
External IDs MGI: 96538 HomoloGene: 1196 GeneCards: 3587
RNA expression pattern
PBB GE IL10RA 204912 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001558

NM_008348
NM_001324486

RefSeq (protein)

NP_001549.2

NP_032374.1

Location (UCSC) Chr 11: 117.99 – 118 Mb Chr 9: 45.25 – 45.27 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Interleukin 10 receptor, alpha subunit is a subunit for the interleukin-10 receptor. IL10RA, is its human gene.

IL10RA has also recently been designated CDW210A (cluster of differentiation W210A).

Function[edit]

The protein encoded by this gene is a receptor for interleukin 10. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. This receptor is reported to promote survival of progenitor myeloid cells through the insulin receptor substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor leads to tyrosine phosphorylation of JAK1 and TYK2 kinases.[1]

Interactions[edit]

Interleukin 10 receptor, alpha subunit has been shown to interact with:

References[edit]

  1. ^ "Entrez Gene: IL10RA interleukin 10 receptor, alpha". 
  2. ^ Ho AS, Liu Y, Khan TA, Hsu DH, Bazan JF, Moore KW (December 1993). "A receptor for interleukin 10 is related to interferon receptors". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 11267–71. doi:10.1073/pnas.90.23.11267. PMC 47963. PMID 8248239. 
  3. ^ Josephson K, Logsdon NJ, Walter MR (July 2001). "Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site". Immunity 15 (1): 35–46. doi:10.1016/s1074-7613(01)00169-8. PMID 11485736. 
  4. ^ Tan JC, Braun S, Rong H, DiGiacomo R, Dolphin E, Baldwin S, Narula SK, Zavodny PJ, Chou CC (May 1995). "Characterization of recombinant extracellular domain of human interleukin-10 receptor". J. Biol. Chem. 270 (21): 12906–11. doi:10.1074/jbc.270.21.12906. PMID 7759550. 
  5. ^ Josephson K, McPherson DT, Walter MR (December 2001). "Purification, crystallization and preliminary X-ray diffraction of a complex between IL-10 and soluble IL-10R1". Acta Crystallogr. D 57 (Pt 12): 1908–11. doi:10.1107/s0907444901016249. PMID 11717514. 
  6. ^ Hoover DM, Schalk-Hihi C, Chou CC, Menon S, Wlodawer A, Zdanov A (May 1999). "Purification of receptor complexes of interleukin-10 stoichiometry and the importance of deglycosylation in their crystallization". Eur. J. Biochem. 262 (1): 134–41. doi:10.1046/j.1432-1327.1999.00363.x. PMID 10231374. 
  7. ^ Usacheva A, Sandoval R, Domanski P, Kotenko SV, Nelms K, Goldsmith MA, Colamonici OR (December 2002). "Contribution of the Box 1 and Box 2 motifs of cytokine receptors to Jak1 association and activation". J. Biol. Chem. 277 (50): 48220–6. doi:10.1074/jbc.M205757200. PMID 12374810. 
  8. ^ Usacheva A, Kotenko S, Witte MM, Colamonici OR (August 2002). "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. 169 (3): 1302–8. doi:10.4049/jimmunol.169.3.1302. PMID 12133952. 

Further reading[edit]

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