FCG3A_MUSPF
ID FCG3A_MUSPF Reviewed; 249 AA.
AC M3XWH1; M1EQN2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A {ECO:0000250|UniProtKB:Q28942};
DE Short=IgG Fc receptor III-A;
DE AltName: Full=Fc-gamma RIII-alpha;
DE Short=FcgammaRIIIA {ECO:0000250|UniProtKB:Q28942};
DE AltName: CD_antigen=CD16a {ECO:0000250|UniProtKB:P08637};
DE Flags: Precursor;
GN Name=FCGR3A {ECO:0000250|UniProtKB:P08637};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=23236062; DOI=10.1128/jvi.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S.,
RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., Przyblyski D.,
RA Ribeiro F., Russell P., Sharpe T., Turner-Maier J., Walker B.J., Young S.,
RA Birren B., Lindblad-Toh K.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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). Optimally activated upon binding of clustered antigen-IgG
CC complexes displayed on cell surfaces, triggers lysis of antibody-coated
CC cells, a process known as antibody-dependent cellular cytotoxicity
CC (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate
CC effector cell activation in the absence of antigenic trigger (By
CC similarity). Mediates IgG effector functions on natural killer (NK)
CC cells. Binds antigen-IgG complexes generated upon infection and
CC triggers NK cell-dependent cytokine production and degranulation to
CC limit viral load and propagation (By similarity). Fc-binding subunit
CC that associates with FCER1G adapter to form functional signaling
CC complexes. Following the engagement of antigen-IgG complexes, triggers
CC phosphorylation of immunoreceptor tyrosine-based activation motif
CC (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:0000250|UniProtKB:Q28942}.
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}.
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DR EMBL; JP009914; AER98511.1; -; mRNA.
DR EMBL; AEYP01028609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004751441.2; XM_004751384.2.
DR STRING; 9669.ENSMPUP00000003421; -.
DR Ensembl; ENSMPUT00000003488; ENSMPUP00000003421; ENSMPUG00000003452.
DR GeneID; 101680253; -.
DR KEGG; mpuf:101680253; -.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; M3XWH1; -.
DR OMA; GDNSTQW; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
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 InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; IgG-binding protein; Immunity;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..249
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000454770"
FT TOPO_DOM 17..198
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..104
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 119..172
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT SITE 220
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000250|UniProtKB:P08637"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 47..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 127..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 248..249
FT /note="Missing (in Ref. 1; AER98511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27962 MW; 0170EC4437CFF19D CRC64;
MWQLLPSTAL LLVASARPQA ADLPKAVVVS DPPGNRVLTL DSVTFTCQGA NPSGNHSTRW
LHNGTLISSQ TSYFIRAASV ENSGEYRCQT GLSELSDPVQ LEVHVGWLLL QTPQRVFQEG
EPIRLRCHSW KNKPVWNVQY FQNRRGKKFS YGNSEFYIPA ARSEHNGSYF CRGLIGKRNE
SSEAVDIIIQ GPPVPSTSAL LPFWPHIPFA VVMALLFAVD TGLYFAMQRH LHNSKRAWEN
SKVSWKQDP
