IL5RA
Interleukin-5 receptor subunit alpha
Also known as: CD125, CDw125, IL5R, IL5RA_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q01344
- Gene
- IL5RA
- Ensembl
- ENSG00000091181
- Chromosome
- 3
- Canonical length
- 420 aa
- Protein class
- CD markers, FDA approved drug targets, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins
- Secretome location
- Intracellular and membrane
OverviewNCBI Gene
The protein encoded by this gene is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised 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. Several alternatively spliced transcript variants encoding four distinct isoforms have been reported. [provided by RefSeq, Jul 2011]
Canonical amino-acid sequenceUniProt
420 residues, UniProt reviewed canonical sequence.
>Q01344|IL5RA
1 MIIVAHVLLI LLGATEILQA DLLPDEKISL LPPVNFTIKV TGLAQVLLQW KPNPDQEQRN
61 VNLEYQVKIN APKEDDYETR ITESKCVTIL HKGFSASVRT ILQNDHSLLA SSWASAELHA
121 PPGSPGTSIV NLTCTTNTTE DNYSRLRSYQ VSLHCTWLVG TDAPEDTQYF LYYRYGSWTE
181 ECQEYSKDTL GRNIACWFPR TFILSKGRDW LAVLVNGSSK HSAIRPFDQL FALHAIDQIN
241 PPLNVTAEIE GTRLSIQWEK PVSAFPIHCF DYEVKIHNTR NGYLQIEKLM TNAFISIIDD
301 LSKYDVQVRA AVSSMCREAG LWSEWSQPIY VGNDEHKPLR EWFVIVIMAT ICFILLILSL
361 ICKICHLWIK LFPPIPAPKS NIKDLFVTTN YEKAGSSETE IEVICYIEKP GVETLEDSVFLocalizationUniProt · AlphaFold · HPA
Whether an antibody against IL5RA can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.38
- Highest tissue expression
- 10 nTPM
Expression across tissuesHPA
Tissue
- fallopian tube: 10 nTPM
- choroid plexus: 5.9 nTPM
- lung: 2.6 nTPM
- prostate: 1.7 nTPM
- duodenum: 1.6 nTPM
- spleen: 1.6 nTPM
Single-cell type
- respiratory ciliated cells: 97 nCPM
- ependymal cells: 90 nCPM
- mast cells: 72 nCPM
- endometrial ciliated cells: 53 nCPM
- fallopian tube ciliated cells: 53 nCPM
- epididymal efferent duct ciliated cells: 45 nCPM
Immune cell
- eosinophil: 356 nTPM
- basophil: 179 nTPM
- naive B-cell: 1.4 nTPM
- neutrophil: 1.1 nTPM
- memory CD4 T-cell: 1 nTPM
- gdT-cell: 0.9 nTPM
Brain region
- choroid plexus: 20 nTPM
- medulla oblongata: 12 nTPM
- spinal cord: 11 nTPM
- midbrain: 11 nTPM
- pons: 5 nTPM
- hypothalamus: 3.5 nTPM
ReferencesPubMed · IEDB
Publications for IL5RA from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
3 publications
- Interleukin 5 regulation of peritoneal Ly-1 B lymphocyte proliferation, differentiation and autoantibody secretion.
1989 · Eur J Immunol · RCR 1.3 · 72 citations - Characterization of the interleukin 5-reactive splenic B cell population.
1990 · Eur J Immunol · RCR 0.4 · 20 citations - Interleukin 5 regulation of peritoneal B-cell proliferation and antibody secretion.
1990 · Scand J Immunol · RCR 0.4 · 16 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.06
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.59
- DepMap mean gene effect
- 0.14
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cytokine-mediated signaling pathway
- inflammatory response to antigenic stimulus
- interleukin-5-mediated signaling pathway
- positive regulation of cell population proliferation
- positive regulation of leukocyte proliferation
- signal transduction
- regulation of interleukin-5 production
Molecular functions
- cytokine binding
- cytokine receptor activity
- interleukin-5 receptor activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of IL5RA in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads IL5RA as an antibody target. Whether an autoantibody or antibody against IL5RA could matter depends on whether native IL5RA is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
IL5RA is annotated at the cell surface, where native IL5RA is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label IL5RA as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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