FCER1A

FCER1A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1F2Q, 1F6A, 1J86, 1J87, 1J88, 1J89, 1RPQ, 2Y7Q
Identifiers
Aliases	FCER1A , FCE1A, FcERI, Fc fragment of IgE receptor Ia
External IDs	OMIM: 147140 MGI: 95494 HomoloGene: 1516 GeneCards: FCER1A
Gene location (Human)
Chr.	Chromosome 1 (human)
End	159,308,224 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	173,054,781 bp
RNA expression pattern
	Top expressed in
	monocyte; ; cavity of mouth; ; vulva; ; gallbladder; ; bone marrow cells; ; periodontal fiber; ; palpebral conjunctiva; ; mucosa of urinary bladder; ; rectum; ; gums;
	Top expressed in
	blood; ; lip; ; bone marrow; ; esophagus; ; spermatid; ; carotid body; ; skin of abdomen; ; uterus; ; white adipose tissue; ; medulla oblongata;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	IgE binding ;
Cellular component	integral component of membrane ; membrane ; plasma membrane ; cell surface ; integral component of plasma membrane ;
Biological process	Fc-epsilon receptor signaling pathway ;
	Sources:Amigo / QuickGO
Orthologs
	2205
	14125
	ENSG00000179639
	ENSMUSG00000005339
	P12319
	P20489
	NM_002001
	NM_010184
	NP_001992
	NP_034314
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 23, 2023

Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide, also known as FCER1A, is a protein which in humans is encoded by the FCER1A gene.^[5]

Function

The high affinity IgE receptor plays a central role in allergic disease, coupling allergen and mast cell to initiate the inflammatory and immediate hypersensitivity responses that are characteristic of disorders such as hay fever and asthma. The allergic response occurs when 2 or more IgE receptors are crosslinked via IgE molecules that in turn are bound to an allergen (antigen) molecule. A perturbation occurs that brings about the release of histamine and proteases from the granules in the cytoplasm of the mast cell and leads to the synthesis of prostaglandins and leukotrienes—potent effectors of the hypersensitivity response. The IgE receptor consists of 3 subunits: alpha (this protein), beta, and gamma; only the alpha subunit is glycosylated.^[6]

Related Research Articles

Immunoglobulin E (IgE) is a type of antibody that has been found only in mammals. IgE is synthesised by plasma cells. Monomers of IgE consist of two heavy chains and two light chains, with the ε chain containing four Ig-like constant domains (Cε1–Cε4). IgE is thought to be an important part of the immune response against infection by certain parasitic worms, including Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. IgE is also utilized during immune defense against certain protozoan parasites such as Plasmodium falciparum. IgE may have evolved as a defense to protect against venoms.

CD8 is a transmembrane glycoprotein that serves as a co-receptor for the T-cell receptor (TCR). Along with the TCR, the CD8 co-receptor plays a role in T cell signaling and aiding with cytotoxic T cell-antigen interactions.

In immunology, an Fc receptor is a protein found on the surface of certain cells – including, among others, B lymphocytes, follicular dendritic cells, natural killer cells, macrophages, neutrophils, eosinophils, basophils, human platelets, and mast cells – that contribute to the protective functions of the immune system. Its name is derived from its binding specificity for a part of an antibody known as the Fc region. Fc receptors bind to antibodies that are attached to infected cells or invading pathogens. Their activity stimulates phagocytic or cytotoxic cells to destroy microbes, or infected cells by antibody-mediated phagocytosis or antibody-dependent cell-mediated cytotoxicity. Some viruses such as flaviviruses use Fc receptors to help them infect cells, by a mechanism known as antibody-dependent enhancement of infection.

The high-affinity IgE receptor, also known as FcεRI, or Fc epsilon RI, is the high-affinity receptor for the Fc region of immunoglobulin E (IgE), an antibody isotype involved in allergy disorders and parasite immunity. FcεRI is a tetrameric receptor complex that binds Fc portion of the ε heavy chain of IgE. It consists of one alpha, one beta, and two gamma chains connected by two disulfide bridges on mast cells and basophils. It lacks the beta subunit on other cells. It is constitutively expressed on mast cells and basophils and is inducible in eosinophils.

CD11c, also known as Integrin, alpha X (ITGAX), is a gene that encodes for CD11c.

CD64 is a type of integral membrane glycoprotein known as an Fc receptor that binds monomeric IgG-type antibodies with high affinity. It is more commonly known as Fc-gamma receptor 1 (FcγRI). After binding IgG, CD64 interacts with an accessory chain known as the common γ chain, which possesses an ITAM motif that is necessary for triggering cellular activation.

The interleukin 4 receptor is a type I cytokine receptor. It is a heterodimer, that is, composed of two subunits. IL4R is the human gene coding for IL-4Rα, the subunit which combines with either common gamma chain or with IL-13Rα1.

T-cell surface glycoprotein CD3 gamma chain is a protein that in humans is encoded by the CD3G gene.

Tryptase alpha-1 and tryptase beta-1 are enzymes that in humans are encoded by the same TPSAB1 gene. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate.

Interferon-alpha/beta receptor beta chain is a protein that in humans is encoded by the IFNAR2 gene.

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

Low affinity immunoglobulin gamma Fc region receptor II-a is a protein that in humans is encoded by the FCGR2A gene.

Interleukin 13 receptor, alpha 1, also known as IL13RA1 and CD213A1, is a human gene.

Killer cell immunoglobulin-like receptor 2DS4 is a protein that in humans is encoded by the KIR2DS4 gene.

CD79b molecule, immunoglobulin-associated beta, also known as CD79B, is a human gene.

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

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

High affinity immunoglobulin gamma Fc receptor I is a protein that in humans is encoded by the FCGR1A gene.

Fc fragment of IgA receptor (FCAR) is a human gene that codes for the transmembrane receptor FcαRI, also known as CD89. FcαRI binds the heavy-chain constant region of Immunoglobulin A (IgA) antibodies. FcαRI is present on the cell surface of myeloid lineage cells, including neutrophils, monocytes, macrophages, and eosinophils, though it is notably absent from intestinal macrophages and does not appear on mast cells. FcαRI plays a role in both pro- and anti-inflammatory responses depending on the state of IgA bound. Inside-out signaling primes FcαRI in order for it to bind its ligand, while outside-in signaling caused by ligand binding depends on FcαRI association with the Fc receptor gamma chain.

High affinity immunoglobulin epsilon receptor subunit beta is a protein that in humans is encoded by the MS4A2 gene.

Fc fragment of IgE, high affinity I, receptor for; gamma polypeptide is a protein that in humans is encoded by the FCER1G gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000179639 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005339 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Pang J, Taylor GR, Munroe DG, Ishaque A, Fung-Leung WP, Lau CY, Liu FT, Zhou L (December 1993). "Characterization of the gene for the human high affinity IgE receptor (Fc epsilon RI) alpha-chain". J. Immunol. 151 (11): 6166–74. doi:10.4049/jimmunol.151.11.6166. PMID 8245459.
↑ "Entrez Gene: FCER1A Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide".

Gounni AS (2006). "The high-affinity IgE receptor (FcepsilonRI): a critical regulator of airway smooth muscle cells?". Am. J. Physiol. Lung Cell Mol. Physiol. 291 (3): L312–21. doi:10.1152/ajplung.00005.2006. PMID 16581830.
Padlan EA, Helm BA (1993). "A modeling study of the alpha-subunit of human high-affinity receptor for immunoglobulin-E". Receptor. 2 (2): 129–44. PMID 1472946.
Wang B, Rieger A, Kilgus O, et al. (1992). "Epidermal Langerhans cells from normal human skin bind monomeric IgE via Fc epsilon RI". J. Exp. Med. 175 (5): 1353–65. doi:10.1084/jem.175.5.1353. PMC 2119204 . PMID 1533243.
Küster H, Zhang L, Brini AT, et al. (1992). "The gene and cDNA for the human high affinity immunoglobulin E receptor beta chain and expression of the complete human receptor". J. Biol. Chem. 267 (18): 12782–7. doi: 10.1016/S0021-9258(18)42344-7 . hdl: 2434/199851 . PMID 1535625.
Le Coniat M, Kinet JP, Berger R (1990). "The human genes for the alpha and gamma subunits of the mast cell receptor for immunoglobulin E are located on human chromosome band 1q23". Immunogenetics. 32 (3): 183–6. doi:10.1007/BF02114971. PMID 2146219. S2CID 23874749.
Shimizu A, Tepler I, Benfey PN, et al. (1988). "Human and rat mast cell high-affinity immunoglobulin E receptors: characterization of putative alpha-chain gene products". Proc. Natl. Acad. Sci. U.S.A. 85 (6): 1907–11. Bibcode:1988PNAS...85.1907S. doi: 10.1073/pnas.85.6.1907 . PMC 279890 . PMID 2964640.
Kochan J, Pettine LF, Hakimi J, et al. (1988). "Isolation of the gene coding for the alpha subunit of the human high affinity IgE receptor". Nucleic Acids Res. 16 (8): 3584. doi:10.1093/nar/16.8.3584. PMC 336524 . PMID 2967464.
Yagi S, Yanagida M, Tanida I, et al. (1994). "High-level expression of the truncated alpha chain of human high-affinity receptor for IgE as a soluble form by baculovirus-infected insect cells. Biochemical characterization of the recombinant product". Eur. J. Biochem. 220 (2): 593–8. doi: 10.1111/j.1432-1033.1994.tb18660.x . PMID 8125119.
Pang J, Taylor GR, Munroe DG, et al. (1994). "Characterization of the gene for the human high affinity IgE receptor (Fc epsilon RI) alpha-chain". J. Immunol. 151 (11): 6166–74. doi:10.4049/jimmunol.151.11.6166. PMID 8245459.
Walsh MT, Divane A, Whitehead AS (1996). "Fine mapping of the human pentraxin gene region on chromosome 1q23". Immunogenetics. 44 (1): 62–9. doi:10.1007/BF02602657. PMID 8613143. S2CID 6603996.
Maurer D, Fiebiger S, Ebner C, et al. (1996). "Peripheral blood dendritic cells express Fc epsilon RI as a complex composed of Fc epsilon RI alpha- and Fc epsilon RI gamma-chains and can use this receptor for IgE-mediated allergen presentation". J. Immunol. 157 (2): 607–16. doi:10.4049/jimmunol.157.2.607. PMID 8752908.
Garman SC, Wurzburg BA, Tarchevskaya SS, et al. (2000). "Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha". Nature. 406 (6793): 259–66. doi:10.1038/35018500. PMID 10917520. S2CID 4419790.
Nishiyama C, Hasegawa M, Nishiyama M, et al. (2001). "Cloning of full-length genomic DNA encoding human FcepsilonRI alpha-chain and its transcriptional regulation". Biochem. Biophys. Res. Commun. 284 (4): 1056–64. doi:10.1006/bbrc.2001.5079. PMID 11409901.
Garman SC, Sechi S, Kinet JP, Jardetzky TS (2001). "The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms". J. Mol. Biol. 311 (5): 1049–62. doi:10.1006/jmbi.2001.4929. PMID 11531339.
Shikanai T, Silverman ES, Morse BW, et al. (2002). "Sequence variants in the FcepsilonRI alpha chain gene". J. Appl. Physiol. 93 (1): 37–41. doi:10.1152/japplphysiol.00993.2001. PMID 12070183. S2CID 84256219.
Sada K, Miah SM, Maeno K, et al. (2002). "Regulation of FcepsilonRI-mediated degranulation by an adaptor protein 3BP2 in rat basophilic leukemia RBL-2H3 cells". Blood. 100 (6): 2138–44. doi: 10.1182/blood-2001-12-0340 . PMID 12200378.
Takahashi K, Nishiyama C, Ra C (2003). "Transcriptional regulation of the human high affinity IgE receptor alpha-chain gene". Mol. Immunol. 38 (16–18): 1193–9. doi:10.1016/S0161-5890(02)00062-7. PMID 12217383.
Vangelista L, Cesco-Gaspere M, Lamba D, Burrone O (2002). "Efficient folding of the FcepsilonRI alpha-chain membrane-proximal domain D2 depends on the presence of the N-terminal domain D1". J. Mol. Biol. 322 (4): 815–25. doi:10.1016/S0022-2836(02)00853-7. PMID 12270716.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Hasegawa M, Nishiyama C, Nishiyama M, et al. (2003). "Regulation of the human Fc epsilon RI alpha-chain distal promoter". J. Immunol. 170 (7): 3732–8. doi: 10.4049/jimmunol.170.7.3732 . PMID 12646639.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

This immunology article is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000179639 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005339 - 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.

[pmid8245459-5] Pang J, Taylor GR, Munroe DG, Ishaque A, Fung-Leung WP, Lau CY, Liu FT, Zhou L (December 1993). "Characterization of the gene for the human high affinity IgE receptor (Fc epsilon RI) alpha-chain". J. Immunol. 151 (11): 6166–74. doi:10.4049/jimmunol.151.11.6166. PMID 8245459.

[entrez-6] "Entrez Gene: FCER1A Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide".

[1]

[2]

[3]

[4]

[5]

[6]

FCER1A

Contents

Function

Related Research Articles

References

Further reading