FCGR3A
entrez
2214
canonical
uniprot
P08637
canonical
ensembl
ENSG00000203747
resolver
ensp
ENSP00000356944
resolver
ensp
ENSP00000392047
resolver
ensp
ENSP00000410180
resolver
ensp
ENSP00000416607
resolver
ensp
ENSP00000514356
resolver
ensp
ENSP00000514357
resolver
ensp
ENSP00000514358
resolver
ensp
ENSP00000514361
resolver
ensp
ENSP00000554986
resolver
ensp
ENSP00000616789
resolver
enst
ENST00000367967
resolver
enst
ENST00000426740
resolver
enst
ENST00000436743
resolver
enst
ENST00000443193
resolver
enst
ENST00000699395
resolver
enst
ENST00000699396
resolver
enst
ENST00000699397
resolver
enst
ENST00000699400
resolver
enst
ENST00000884927
resolver
enst
ENST00000946730
resolver
genesymbol
FCGR3A
resolver
genesymbol_syn
CD16A
resolver
genesymbol_syn
FCG3
resolver
genesymbol_syn
FCGR3
resolver
genesymbol_syn
IGFR3
resolver
hgnc
HGNC:3619
resolver
uniprot
A2N6W9
resolver
uniprot
H0Y755
resolver
uniprot
Q53FJ0
resolver
uniprot
Q53FL6
resolver
uniprot
Q5EBR4
resolver
uniprot
Q65ZM6
resolver
uniprot
Q6PIJ0
resolver
uniprot_entry
FCG3A_HUMAN
resolver
uniprot_entry
H0Y755_HUMAN
resolver
uniprot_sec
A2N6W9
resolver
uniprot_sec
Q53FJ0
resolver
uniprot_sec
Q53FL6
resolver
uniprot_sec
Q5EBR4
resolver
uniprot_sec
Q65ZM6
resolver
uniprot_sec
Q6PIJ0
resolver
amino_acid_sequence
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 20 (IMD20) [MIM:615707]: A rare autosomal recessive primary immunodeficiency characterized by functional deficiency of NK cells. Affected individuals typically present with severe herpes viral infections, particularly Epstein Barr virus (EBV), and human papillomavirus (HPV). {ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:8608639, ECO:0000269|PubMed:8609432, ECO:0000269|PubMed:8874200}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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:11711607, PubMed:21768335, PubMed:22023369, PubMed:24412922, PubMed:25786175, PubMed:25816339, PubMed:28652325, PubMed:8609432, PubMed:9242542). 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:24412922, PubMed:25786175). Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (PubMed:29967280, PubMed:9916693). 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:1825220, PubMed:23024279, PubMed:2532305). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (PubMed:10318937, PubMed:23006327). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (PubMed:27670158). Mediates enhanced opsonization and ADCC in response to afucosylated IgGs (PubMed:34485821, PubMed:28566370). {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}.; FUNCTION: (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}.
uniprot
proteins
mass_dalton
29089
uniprot
proteins
mutagenesis
MUTAGEN 197; /note="S->P: Impairs receptor shedding. Impairs the detachment of NK cells from opsonized target cells upon sequential activation."; /evidence="ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:29967280"; MUTAGEN 203; /note="F->P: Disrupts transmembrane anchoring."; /evidence="ECO:0000269|PubMed:1825220"; MUTAGEN 203; /note="F->T,Y,N,E,A,D,K: Enables membrane anchoring via glycosylphosphatidylinositol. Disrupts transmembrane anchoring."; /evidence="ECO:0000269|PubMed:1825220"; MUTAGEN 203; /note="F->V,I,L: Enables only transmembrane anchoring."; /evidence="ECO:0000269|PubMed:1825220"; MUTAGEN 208; /note="Q->A: Decreases the association with either CD247 or FCER1G."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 210; /note="S->A: Has no effect on complex association with CD247 or FCER1G. Decreases cell surface expression; when associated with A-211 and A-212."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 211; /note="F->A: Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-210 and A-212."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 212; /note="C->A: Has no effect on complex formation with CD247 or FCER1G. Decreases cell surface expression; when associated with A-210 and A-211."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 219; /note="F->A: Decreases the association with either CD247 or FCER1G. Decreases cell surface expression."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 222; /note="D->A: Decreases the association with either CD247 or FCER1G. Strongly increases cell surface expression."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 222; /note="D->E,K: Strongly decreases complex formation with CD247 or FCER1G."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 222; /note="D->N: Has little effect on complex formation with CD247 or FCER1G."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 223; /note="T->A: Decreases the association with either CD247 or FCER1G. Decreases cell surface expression."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 226; /note="Y->A: Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-227 and A-228."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 227; /note="F->A: Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-226 and A-228."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 228; /note="S->A: Has little effect on complex formation with CD247 or FCER1G. Decreases cell surface expression; when associated with A-226 and A-227."; /evidence="ECO:0000269|PubMed:28652325"; MUTAGEN 235..237; /note="SST->AAA: Loss of PKC-dependent phosphorylation. Abolishes pro-inflammatory cytokine production while enhancing cell degranulation."; /evidence="ECO:0000269|PubMed:23024279"; MUTAGEN 249..254; /note="Missing: Impairs the interaction with S100A4."; /evidence="ECO:0000269|PubMed:23024279
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22023369}.; PTM: 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. {ECO:0000269|PubMed:24337742, ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:29967280}.; PTM: Phosphorylated at RSSTR motif by PKC. The relevant physiological PKCs might be PRKCI, PRKCG, PRKCE, PRKCH and PRKCQ. {ECO:0000269|PubMed:23024279}.
uniprot
proteins
pubmed
10318937
uniprot
proteins
pubmed
11711607
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16951347
uniprot
proteins
pubmed
1825220
uniprot
proteins
pubmed
21768335
uniprot
proteins
pubmed
22023369
uniprot
proteins
pubmed
23006327
uniprot
proteins
pubmed
23024279
uniprot
proteins
pubmed
24337742
uniprot
proteins
pubmed
24412922
uniprot
proteins
pubmed
2525780
uniprot
proteins
pubmed
2526846
uniprot
proteins
pubmed
2532305
uniprot
proteins
pubmed
25786175
uniprot
proteins
pubmed
25816339
uniprot
proteins
pubmed
27670158
uniprot
proteins
pubmed
28126818
uniprot
proteins
pubmed
28566370
uniprot
proteins
pubmed
28652325
uniprot
proteins
pubmed
29967280
uniprot
proteins
pubmed
30061887
uniprot
proteins
pubmed
31244843
uniprot
proteins
pubmed
34485821
uniprot
proteins
pubmed
37421619
uniprot
proteins
pubmed
7700021
uniprot
proteins
pubmed
7836402
uniprot
proteins
pubmed
7955033
uniprot
proteins
pubmed
8608639
uniprot
proteins
pubmed
8609432
uniprot
proteins
pubmed
8874200
uniprot
proteins
pubmed
9242542
uniprot
proteins
pubmed
9276722
uniprot
proteins
pubmed
9916693
uniprot
proteins
sequence_length
254
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1825220, ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:24337742, ECO:0000269|PubMed:2532305, ECO:0000269|PubMed:28652325, ECO:0000269|PubMed:29967280}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:29967280}. Note=Also exists as a soluble receptor. {ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:29967280}.
uniprot
proteins
transmembrane_region
TRANSMEM 209..229; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins