IL10RA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIL10RA, CD210, CD210a, CDW210A, HIL-10R, IL-10R1, IL10R, Interleukin 10 receptor, alpha subunit, interleukin 10 receptor subunit alpha
External IDsOMIM: 146933 MGI: 96538 HomoloGene: 1196 GeneCards: IL10RA
Orthologs
SpeciesHumanMouse
Entrez

3587

16154

Ensembl

ENSG00000110324

ENSMUSG00000032089

UniProt

Q13651

Q61727

RefSeq (mRNA)

NM_001558

NM_008348
NM_001324486

RefSeq (protein)

NP_001549

NP_001311415
NP_032374

Location (UCSC)Chr 11: 117.99 – 118 MbChr 9: 45.17 – 45.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

IL10RA has also been designated CDw210a (cluster of differentiation w210a).

Function

See also: PI 3-kinase/AKT pathway

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 myeloid progenitor 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.[5]

Interactions

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110324 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032089 - 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. ^ "Entrez Gene: IL10RA interleukin 10 receptor, alpha".
  6. ^ 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. Bibcode:1993PNAS...9011267H. doi:10.1073/pnas.90.23.11267. PMC 47963. PMID 8248239.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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

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


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