Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (PubMed:24412922, PubMed:25786175, PubMed:21768335, PubMed:22023369, PubMed:8609432, PubMed:9242542, PubMed:25816339, PubMed:11711607, PubMed:28652325). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory-like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC (PubMed:25786175, PubMed:24412922). Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (PubMed:9916693, PubMed:29967280). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (PubMed:2532305, PubMed:1825220, PubMed:23024279). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (PubMed:23006327, PubMed:10318937). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (PubMed:27670158). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). (Microbial infection) Involved in Dengue virus pathogenesis via antibody-dependent enhancement (ADE) mechanism. Secondary infection with Dengue virus triggers elevated levels of afucosylated non-neutralizing IgG1s with reactivity to viral envelope/E protein. Viral antigen-IgG1 complexes bind with high affinity to FCGR3A, facilitating virus entry in myeloid cells and subsequent viral replication. Forms a heterooligomeric complex with ITAM-containing signaling subunits, either a homodimer of CD247, a homodimer of FCER1G or a heterodimer of CD247 and FCER1G (PubMed:2532305, PubMed:1825220, PubMed:28652325). Interacts (via transmembrane domain) with signaling subunits; this interaction is a prerequisite for receptor complex expression on the cell surface and intracellular signal transduction (PubMed:2532305, PubMed:1825220, PubMed:28652325). Binds the Fc region of antigen-complexed IgG with a preference for IgG1 and IgG3 isotypes (PubMed:22023369, PubMed:21768335, PubMed:8609432, PubMed:9242542, PubMed:11711607). Interacts with CD2; this interaction is involved in NK cell activation and cytotoxicity (PubMed:23006327). Interacts with S100A4; this interaction inhibits PKC-dependent phosphorylation of FCGR3A (PubMed:23024279). Exists also as a soluble receptor. Expressed in natural killer cells (at protein level) (PubMed:2526846). Expressed in a subset of circulating monocytes (at protein level) (PubMed:27670158). Up-regulated in a monocyte subset upon exposure to IL10, TGFB and MCSF. Glycosylated. Contains high mannose- and complex-type oligosaccharides. Glycosylation at Asn-180 is mandatory for high affinity binding to the Fc and for discrimination between fucosylated and afucosylated IgG glycoforms. Undergoes rapid ectodomain shedding upon NK cell stimulation. The soluble form is produced by a proteolytic cleavage mediated by ADAM17. Repeated stimulation causes receptor shedding, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells while avoiding activation-induced NK cell apoptosis. Phosphorylated at RSSTR motif by PKC. The relevant physiological PKCs might be PRKCI, PRKCG, PRKCE, PRKCH and PRKCQ. The disease is caused by variants affecting the gene represented in this entry. Encoded by one of two nearly indentical genes: FCGR3A (shown here) and FCGR3B which are expressed in a tissue-specific manner. The Phe-203 in III-A determines the transmembrane domains whereas the 'Ser-203' in III-B determines the GPI-anchoring. FCGR3A in mammals is the true ortholog of FCGR4 in rodents. The FCGR2A-HSPA6-FCGR4-FCGR2B module was duplicated in great apes through non-allelic homologous recombination, giving rise to two FCGR4-type genes and to FCGR2C, a hybrid gene combining FCGR2A and FCGR2B. While FCGR3A kept the original FCGR4 functionality, FCGR3B rapidly evolved and acquired specific features coding for a GPI-anchored receptor. Extended N-terminus. Extended N-terminus. FCGR3A mutation db