FCG3A_PIG
ID FCG3A_PIG Reviewed; 257 AA.
AC Q28942; Q28940; Q28941;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A {ECO:0000303|PubMed:31323052, ECO:0000303|PubMed:8077673};
DE Short=IgG Fc receptor III-A;
DE AltName: Full=Cytolytic trigger molecule G7 {ECO:0000303|PubMed:8077673};
DE AltName: Full=Fc-gamma RIII;
DE Short=FcRIII;
DE AltName: Full=Fc-gamma RIII-alpha;
DE Short=FcgammaRIIIA {ECO:0000303|PubMed:31323052};
DE AltName: CD_antigen=CD16a {ECO:0000250|UniProtKB:P08637};
DE Flags: Precursor;
GN Name=FCGR3A {ECO:0000250|UniProtKB:P08637}; Synonyms=FCGR3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-47; 92-107 AND 179-188,
RP GLYCOSYLATION AT ASN-181 (VARIANT ASN-181), GLYCOSYLATION AT ASN-64;
RP ASN-134 AND ASN-162, VARIANTS, POLYMORPHISM, AND TISSUE SPECIFICITY.
RC STRAIN=Minnesota miniature;
RX PubMed=8077673;
RA Halloran P.J., Sweeney S.E., Strohmeier C.M., Kim Y.B.;
RT "Molecular cloning and identification of the porcine cytolytic trigger
RT molecule G7 as a Fc gamma RIII alpha (CD16) homologue.";
RL J. Immunol. 153:2631-2641(1994).
RN [2]
RP NOMENCLATURE.
RX PubMed=7955033;
RA Conrad D., Cooper M., Fridman W.H., Kinet J.P., Ravetch J.;
RT "Nomenclature of Fc receptors. IUIS/WHO Subcommittee on Nomenclature of Fc
RT receptors.";
RL Bull. World Health Organ. 72:809-810(1994).
RN [3]
RP FUNCTION.
RX PubMed=31323052; DOI=10.1371/journal.pone.0219999;
RA Bhatti M.M., Cai A.G., Theunissen J.W.;
RT "Binding affinities of human IgG1 and chimerized pig and rabbit derivatives
RT to human, pig and rabbit Fc gamma receptor IIIA.";
RL PLoS ONE 14:e0219999-e0219999(2019).
RN [4]
RP FUNCTION.
RX PubMed=34485821; DOI=10.1093/abt/tbab016;
RA Mao C., Near R., Zhong X., Gao W.;
RT "Cross-species higher sensitivities of FcgammaRIIIA/FcgammaRIV to
RT afucosylated IgG for enhanced ADCC.";
RL Antib Ther 4:159-170(2021).
CC -!- FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin
CC gamma (IgG) (PubMed:31323052). Optimally activated upon binding of
CC clustered antigen-IgG complexes displayed on cell surfaces, triggers
CC lysis of antibody-coated cells, a process known as antibody-dependent
CC cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus
CC avoiding inappropriate effector cell activation in the absence of
CC antigenic trigger (By similarity). Mediates IgG effector functions on
CC natural killer (NK) cells. Binds antigen-IgG complexes generated upon
CC infection and triggers NK cell-dependent cytokine production and
CC degranulation to limit viral load and propagation (By similarity). Fc-
CC binding subunit that associates with FCER1G adapter to form functional
CC signaling complexes. Following the engagement of antigen-IgG complexes,
CC triggers phosphorylation of immunoreceptor tyrosine-based activation
CC motif (ITAM)-containing adapter with subsequent activation of
CC phosphatidylinositol 3-kinase signaling and sustained elevation of
CC intracellular calcium that ultimately drive NK cell activation (By
CC similarity). Mediates enhanced ADCC in response to afucosylated IgGs
CC (PubMed:34485821). {ECO:0000250|UniProtKB:A0A0B4J1G0,
CC ECO:0000250|UniProtKB:P08637, ECO:0000269|PubMed:31323052,
CC ECO:0000269|PubMed:34485821}.
CC -!- SUBUNIT: Forms a heterooligomeric complex with ITAM-containing
CC signaling subunits FCER1G. Interacts (via transmembrane domain) with
CC signaling subunits; this interaction is a prerequisite for receptor
CC complex expression on the cell surface and intracellular signal
CC transduction. Binds the Fc region of antigen-complexed IgG.
CC {ECO:0000250|UniProtKB:P08637}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08637};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in polymorphonuclear leukocytes,
CC pulmonary alveolar macrophages and peripheral blood mononuclear cells
CC (at protein level) (PubMed:8077673). Found in spleen, and at very low
CC levels in lymph nodes but not in thymus or liver (PubMed:8077673).
CC {ECO:0000269|PubMed:8077673}.
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DR EMBL; U08993; AAA57190.1; -; mRNA.
DR EMBL; U08991; AAA57188.1; -; mRNA.
DR EMBL; U08992; AAA57189.1; -; mRNA.
DR PIR; I47165; I47165.
DR AlphaFoldDB; Q28942; -.
DR SMR; Q28942; -.
DR iPTMnet; Q28942; -.
DR PeptideAtlas; Q28942; -.
DR PRIDE; Q28942; -.
DR InParanoid; Q28942; -.
DR ChiTaRS; FCGR3B; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW IgG-binding protein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..257
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /id="PRO_0000015155"
FT TOPO_DOM 20..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..104
FT /note="Ig-like C2-type 1"
FT DOMAIN 108..190
FT /note="Ig-like C2-type 2"
FT SITE 223
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000250|UniProtKB:P08637"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8077673"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8077673"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8077673"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; in variant N-181"
FT /evidence="ECO:0000269|PubMed:8077673"
FT DISULFID 48..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 129..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 55
FT /note="R -> G (in clone 284.4)"
FT VARIANT 149
FT /note="K -> M (in clone 334.8)"
FT VARIANT 181
FT /note="D -> N (in clone 334.8)"
FT VARIANT 186
FT /note="P -> A (in clone 334.8)"
SQ SEQUENCE 257 AA; 29062 MW; 1D038CC1552B97CB CRC64;
MWQLLSPTAL LLLVSVPGTH AEDPPKSVVI LDPPWDRLLE KDSVTLKCQG AYPPRDDSTE
WRWNGTLISN KASSYSITDA TVGNSGEYTC KTGLSAQSDP LRLEVYKGWL LLQAPRWVVQ
EGESIRLRCH TWKNITIQKV QYFQNGMGKK FSHQNFEYHI PNATLKDGGS YFCRGIIKNY
DLSSEPVKVT VQGSKSPSPI LSFFLPWHQI IFCLVMGFLF AVDTGLYFSV RKVLRSSKED
WRNGKVTWSR DPADKGG
