Purified Membrane Proteins

Low affinity immunoglobulin gamma Fc region receptor III-A (IgG Fc receptor III-A) (CD16-II) (CD16a antigen) (Fc-gamma RIII-alpha) (Fc-gamma RIII) (Fc-gamma RIIIa) (FcRIII) (FcRIIIa) (FcgammaRIIIA) (FcR-10) (IgG Fc receptor III-2) (CD antigen CD16a)

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). {ECO:0000269|PubMed:10318937, ECO:0000269|PubMed:11711607, ECO:0000269|PubMed:1825220, ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22023369, ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:23024279, ECO:0000269|PubMed:24412922, ECO:0000269|PubMed:2532305, ECO:0000269|PubMed:25786175, ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:27670158, ECO:0000269|PubMed:29967280, ECO:0000269|PubMed:34485821, ECO:0000269|PubMed:8609432, ECO:0000269|PubMed:9242542, ECO:0000269|PubMed:9916693}.; (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. {ECO:0000269|PubMed:28126818}.

Native

Stable

Pure

Active protein

Recombinant protein

Human Origin

Entry Name:

FCG3A_HUMAN

Gene Name:

FCGR3A CD16A FCG3 FCGR3 IGFR3

Uniprot Accession:

P08637

Origin:

Homo sapiens (Human)

Protein family:

nd

Full-length:

254

AA

Mass:

29089

Da

MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK

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Expression systems: bacteria, yeast, insect cells, HEK & CHO mammalian cells
Purified formats: detergents, SMALPs, nanodiscs, proteoliposomes