Interleukin 10 receptor, alpha subunit

Last updated

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 OMIM: 146933; MGI: 96538; HomoloGene: 1196; GeneCards: IL10RA; OMA:IL10RA - orthologs
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 Mb Chr 9: 45.17 – 45.18 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Contents

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

Function

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:

Related Research Articles

<span class="mw-page-title-main">Interleukin 10</span> Anti-inflammatory cytokine

Interleukin 10 (IL-10), also known as human cytokine synthesis inhibitory factor (CSIF), is an anti-inflammatory cytokine. In humans, interleukin 10 is encoded by the IL10 gene. IL-10 signals through a receptor complex consisting of two IL-10 receptor-1 and two IL-10 receptor-2 proteins. Consequently, the functional receptor consists of four IL-10 receptor molecules. IL-10 binding induces STAT3 signalling via the phosphorylation of the cytoplasmic tails of IL-10 receptor 1 + IL-10 receptor 2 by JAK1 and Tyk2 respectively.

<span class="mw-page-title-main">Interleukin 22</span> Protein, encoded in humans by IL22 gene

Interleukin-22 (IL-22) is a protein that in humans is encoded by the IL22 gene.

<span class="mw-page-title-main">Glycoprotein 130</span> Mammalian protein found in Homo sapiens

Glycoprotein 130 is a transmembrane protein which is the founding member of the class of tall cytokine receptors. It forms one subunit of the type I cytokine receptor within the IL-6 receptor family. It is often referred to as the common gp130 subunit, and is important for signal transduction following cytokine engagement. As with other type I cytokine receptors, gp130 possesses a WSXWS amino acid motif that ensures correct protein folding and ligand binding. It interacts with Janus kinases to elicit an intracellular signal following receptor interaction with its ligand. Structurally, gp130 is composed of five fibronectin type-III domains and one immunoglobulin-like C2-type (immunoglobulin-like) domain in its extracellular portion.

<span class="mw-page-title-main">Janus kinase 1</span>

JAK1 is a human tyrosine kinase protein essential for signaling for certain type I and type II cytokines. It interacts with the common gamma chain (γc) of type I cytokine receptors, to elicit signals from the IL-2 receptor family, the IL-4 receptor family, the gp130 receptor family. It is also important for transducing a signal by type I (IFN-α/β) and type II (IFN-γ) interferons, and members of the IL-10 family via type II cytokine receptors. Jak1 plays a critical role in initiating responses to multiple major cytokine receptor families. Loss of Jak1 is lethal in neonatal mice, possibly due to difficulties suckling. Expression of JAK1 in cancer cells enables individual cells to contract, potentially allowing them to escape their tumor and metastasize to other parts of the body.

<span class="mw-page-title-main">Interleukin-12 subunit beta</span> Protein-coding gene in the species Homo sapiens

Subunit beta of interleukin 12 is a protein subunit that in humans is encoded by the IL12B gene. IL-12B is a common subunit of interleukin 12 and interleukin 23.

<span class="mw-page-title-main">Interleukin 1 receptor, type I</span> Type of interleukin receptor

Interleukin 1 receptor, type I (IL1R1) also known as CD121a, is an interleukin receptor. IL1R1 also denotes its human gene.

<span class="mw-page-title-main">Interleukin 5 receptor alpha subunit</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">IL1RAP</span> Protein-coding gene in the species Homo sapiens

Interleukin-1 receptor accessory protein is a protein that in humans is encoded by the IL1RAP gene.

<span class="mw-page-title-main">Interleukin 15 receptor, alpha subunit</span> Protein-coding gene in the species Homo sapiens

Interleukin 15 receptor, alpha subunit is a subunit of the interleukin 15 receptor that in humans is encoded by the IL15RA gene.

<span class="mw-page-title-main">Interleukin 12 receptor, beta 2 subunit</span> Protein-coding gene in the species Homo sapiens

Interleukin 12 receptor, beta 2 subunit is a subunit of the interleukin 12 receptor. IL12RB2 is its human gene. IL12RB2 orthologs have been identified in all mammals for which complete genome data are available.

<span class="mw-page-title-main">Interleukin-9 receptor</span> Protein-coding gene in the species Homo sapiens

Interleukin 9 receptor (IL9R) also known as CD129 is a type I cytokine receptor. IL9R also denotes its human gene.

<span class="mw-page-title-main">Interleukin 10 receptor, beta subunit</span> Protein-coding gene in the species Homo sapiens

Interleukin 10 receptor, beta subunit is a subunit for the interleukin-10 receptor. IL10RB is its human gene.

<span class="mw-page-title-main">IL1F10</span> Human protein and coding gene

Interleukin-1 family member 10 is a protein that in humans is encoded by the IL1F10 gene.

<span class="mw-page-title-main">Interleukin 20 receptor, alpha subunit</span> Protein-coding gene in the species Homo sapiens

Interleukin 20 receptor, alpha subunit, is a subunit of the interleukin-20 receptor, the interleukin-26 receptor, and the interleukin-24 receptor. The interleukin 20 receptor, alpha subunit is also referred to as IL20R1 or IL20RA. The IL20RA receptor is involved in both pro-inflammatory and anti-inflammatory responses, signaling through the JAK-STAT pathway.

<span class="mw-page-title-main">IL2RB</span> Protein-coding gene in the species Homo sapiens

Interleukin-2 receptor subunit beta is a protein that in humans is encoded by the IL2RB gene. Also known as CD122; IL15RB; P70-75.

<span class="mw-page-title-main">IL3RA</span> Human gene

Interleukin 3 receptor, alpha (IL3RA), also known as CD123, is a human gene.

The interleukin-5 receptor is a type I cytokine receptor. It is a heterodimer of the interleukin 5 receptor alpha subunit and CSF2RB.

Interleukin-10 receptor (IL-10R) is a type II cytokine receptor. The receptor is tetrameric, composed of 2α and 2β subunits. The α subunit is expressed on haematopoietic cells whilst the β subunit is expressed ubiquitously. The α subunit is exclusive to interleukin-10, however the β subunit is shared with other type II cytokine receptors such as IL-22R, IL-26R and INFλR.

<span class="mw-page-title-main">IL18R1</span> Protein-coding gene in the species Homo sapiens

The interleukin-18 receptor 1 (IL-18R1) is an interleukin receptor of the immunoglobulin superfamily. IL18R1 is its human gene. IL18R1 is also known as CDw218a.

<span class="mw-page-title-main">Interleukin-7 receptor-α</span> Protein-coding gene in the species Homo sapiens

Interleukin-7 receptor subunit alpha (IL7R-α) also known as CD127 is a protein that in humans is encoded by the IL7R gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000110324 – Ensembl, May 2017
  2. 1 2 3 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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