FCAR

FCAR
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1OVZ, 1OW0, 1UCT
Identifiers
Aliases	FCAR, CD89, CTB-61M7.2, FcalphaRI, Fc fragment of IgA receptor
External IDs	HomoloGene: 48064 GeneCards: 2204
Gene ontology Molecular function • IgA binding Cellular component • integral component of membrane • extracellular region • plasma membrane • integral component of plasma membrane • membrane Biological process • immune response Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2204	n/a
Ensembl	n/a	n/a
UniProt	P24071	n/a
RefSeq (mRNA)	NM_002000 NM_133269 NM_133271 NM_133272 NM_133273 NM_133274 NM_133277 NM_133278 NM_133279 NM_133280	n/a
RefSeq (protein)	NP_001991.1 NP_579803.1 NP_579805.1 NP_579806.1 NP_579807.1 NP_579808.1 NP_579811.1 NP_579812.1	n/a
Location (UCSC)	Chr 19: 54.87 – 54.89 Mb	n/a
PubMed search		n/a
Wikidata
View/Edit Human

Fc fragment of IgA receptor (FCAR) also known as CD89 (Cluster of Differentiation 89), is a human gene.

Function

This gene is a member of the immunoglobulin gene superfamily and encodes a receptor for the Fc region of IgA. The receptor is a transmembrane glycoprotein present on the surface of myeloid lineage cells such as neutrophils, monocytes, macrophages, and eosinophils, where it mediates immunologic responses to pathogens. It interacts with IgA-opsonized targets and triggers several immunologic defense processes, including phagocytosis, antibody-dependent cell-mediated cytotoxicity, and stimulation of the release of inflammatory mediators. Alternative splicing of the transcript from this gene produces ten mRNA variants encoding different isoforms.

Interactions

FCAR has been shown to interact with FCGR1A.

See also

• Cluster of differentiation

Further reading

• Morton HC, van Egmond M, van de Winkel JG (1996). "Structure and function of human IgA Fc receptors (Fc alpha R)". Crit. Rev. Immunol. 16 (4): 423–40. PMID 8954257. 
• Morton HC, Brandtzaeg P (2001). "CD89: the human myeloid IgA Fc receptor". Arch. Immunol. Ther. Exp. (Warsz.). 49 (3): 217–29. PMID 11478396. 
• Martin AM, Kulski JK, Witt C, Pontarotti P, Christiansen FT (2002). "Leukocyte Ig-like receptor complex (LRC) in mice and men". Trends Immunol. 23 (2): 81–8. doi:10.1016/S1471-4906(01)02155-X. PMID 11929131. 
• Monteiro RC, Van De Winkel JG (2003). "IgA Fc receptors". Annu. Rev. Immunol. 21: 177–204. doi:10.1146/annurev.immunol.21.120601.141011. PMID 12524384. 
• Kremer EJ, Kalatzis V, Baker E, Callen DF, Sutherland GR, Maliszewski CR (1992). "The gene for the human IgA Fc receptor maps to 19q13.4". Hum. Genet. 89 (1): 107–8. doi:10.1007/BF00207054. PMID 1577457. 
• Maliszewski CR, March CJ, Schoenborn MA, Gimpel S, Shen L (1990). "Expression cloning of a human Fc receptor for IgA". J. Exp. Med. 172 (6): 1665–72. doi:10.1084/jem.172.6.1665. PMC 2188749. PMID 2258698. 
• Pfefferkorn LC, Yeaman GR (1994). "Association of IgA-Fc receptors (Fc alpha R) with Fc epsilon RI gamma 2 subunits in U937 cells. Aggregation induces the tyrosine phosphorylation of gamma 2". J. Immunol. 153 (7): 3228–36. PMID 7522255. 
• de Wit TP, Morton HC, Capel PJ, van de Winkel JG (1995). "Structure of the gene for the human myeloid IgA Fc receptor (CD89)". J. Immunol. 155 (3): 1203–9. PMID 7636188. 
• Dürrbaum-Landmann I, Kaltenhäuser E, Flad HD, Ernst M (1994). "HIV-1 envelope protein gp120 affects phenotype and function of monocytes in vitro". J. Leukoc. Biol. 55 (4): 545–51. PMID 8145026. 
• Monteiro RC, Hostoffer RW, Cooper MD, Bonner JR, Gartland GL, Kubagawa H (1993). "Definition of immunoglobulin A receptors on eosinophils and their enhanced expression in allergic individuals". J. Clin. Invest. 92 (4): 1681–5. doi:10.1172/JCI116754. PMC 288327. PMID 8408621. 
• Morton HC, van den Herik-Oudijk IE, Vossebeld P, Snijders A, Verhoeven AJ, Capel PJ, van de Winkel JG (1995). "Functional association between the human myeloid immunoglobulin A Fc receptor (CD89) and FcR gamma chain. Molecular basis for CD89/FcR gamma chain association". J. Biol. Chem. 270 (50): 29781–7. doi:10.1074/jbc.270.50.29781. PMID 8530370. 
• Morton HC, Schiel AE, Janssen SW, van de Winkel JG (1996). "Alternatively spliced forms of the human myeloid Fc alpha receptor (CD89) in neutrophils". Immunogenetics. 43 (4): 246–7. doi:10.1007/s002510050057. PMID 8575829. 
• Patry C, Sibille Y, Lehuen A, Monteiro RC (1996). "Identification of Fc alpha receptor (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages". J. Immunol. 156 (11): 4442–8. PMID 8666819. 
• Carayannopoulos L, Hexham JM, Capra JD (1996). "Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Calpha2 and Calpha3 in human IgA1". J. Exp. Med. 183 (4): 1579–86. doi:10.1084/jem.183.4.1579. PMC 2192530. PMID 8666916. 
• Pleass RJ, Andrews PD, Kerr MA, Woof JM (1996). "Alternative splicing of the human IgA Fc receptor CD89 in neutrophils and eosinophils". Biochem. J. 318 ( Pt 3) (3): 771–7. PMC 1217685. PMID 8836118. 
• Reterink TJ, Verweij CL, van Es LA, Daha MR (1996). "Alternative splicing of IgA Fc receptor (CD89) transcripts". Gene. 175 (1-2): 279–80. doi:10.1016/0378-1119(96)00152-7. PMID 8917112. 
• van Dijk TB, Bracke M, Caldenhoven E, Raaijmakers JA, Lammers JW, Koenderman L, de Groot RP (1996). "Cloning and characterization of Fc alpha Rb, a novel Fc alpha receptor (CD89) isoform expressed in eosinophils and neutrophils". Blood. 88 (11): 4229–38. PMID 8943858. 
• Toyabe S, Kuwano Y, Takeda K, Uchiyama M, Abo T (1997). "IgA nephropathy-specific expression of the IgA Fc receptors (CD89) on blood phagocytic cells". Clin. Exp. Immunol. 110 (2): 226–32. doi:10.1111/j.1365-2249.1997.tb08321.x. PMC 2265504. PMID 9367406. 
• Gulle H, Samstag A, Eibl MM, Wolf HM (1998). "Physical and functional association of Fc alpha R with protein tyrosine kinase Lyn". Blood. 91 (2): 383–91. PMID 9427690. 

External links

• CD89 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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