FCG3A_BOVIN
ID FCG3A_BOVIN Reviewed; 250 AA.
AC P79107; F1N286; Q2KI63;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A {ECO:0000250|UniProtKB:P08637};
DE Short=IgG Fc receptor III-A;
DE AltName: Full=Fc-gamma RIII-alpha;
DE Short=FcgammaRIIIA {ECO:0000250|UniProtKB:P08637};
DE AltName: CD_antigen=CD16a {ECO:0000250|UniProtKB:P08637};
DE Flags: Precursor;
GN Name=FCGR3A {ECO:0000250|UniProtKB:P08637};
GN Synonyms=FCGR3, FCGRIII {ECO:0000303|PubMed:9089104};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-11; VAL-12; ARG-46;
RP ASP-107; VAL-114 AND ILE-229.
RC TISSUE=Lymph node;
RX PubMed=9089104; DOI=10.1007/s002510050228;
RA Collins R.A., Gelder K.I., Howard C.J.;
RT "Nucleotide sequence of cattle FcGRIII: its identification in gammadelta T
RT cells.";
RL Immunogenetics 45:440-443(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
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 adapters 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 (By similarity). {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}.
CC -!- TISSUE SPECIFICITY: Expressed in gamma-delta T cells.
CC {ECO:0000269|PubMed:9089104}.
CC -!- CAUTION: It is not sure if the variants are due to different alleles or
CC to the existence of at least two genes. {ECO:0000305}.
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DR EMBL; X99695; CAA68026.1; -; Genomic_DNA.
DR EMBL; BC112756; AAI12757.1; -; mRNA.
DR RefSeq; NP_001070870.1; NM_001077402.1.
DR AlphaFoldDB; P79107; -.
DR SMR; P79107; -.
DR STRING; 9913.ENSBTAP00000033639; -.
DR PaxDb; P79107; -.
DR Ensembl; ENSBTAT00000033730; ENSBTAP00000033639; ENSBTAG00000002096.
DR GeneID; 281766; -.
DR KEGG; bta:281766; -.
DR CTD; 2214; -.
DR VEuPathDB; HostDB:ENSBTAG00000002096; -.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; P79107; -.
DR OMA; GDNSTQW; -.
DR OrthoDB; 866496at2759; -.
DR TreeFam; TF335097; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000002096; Expressed in lung and 104 other tissues.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; IgG-binding protein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..250
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /id="PRO_0000015149"
FT TOPO_DOM 17..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 99..189
FT /note="Ig-like C2-type 2"
FT SITE 222
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000250|UniProtKB:P08637"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 128..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 11
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:9089104"
FT VARIANT 12
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:9089104"
FT VARIANT 46
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:9089104"
FT VARIANT 107
FT /note="G -> D"
FT /evidence="ECO:0000269|PubMed:9089104"
FT VARIANT 114
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:9089104"
FT VARIANT 229
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:9089104"
FT CONFLICT 204
FT /note="L -> P (in Ref. 1; CAA68026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28096 MW; 675388BE853F2496 CRC64;
MWQLLPPAAL LLLVSADTQT ADPSKAVVLL DPQWNHVLTN DRVTLKCQGD YPVEDNSTKW
WHNGTLISSQ TPSYFIADVK VQDSGEYKCQ TGLSAPSDPV KLEVHVGWLL LQVAQRVVNV
GKPIRLKCHS WKKTPVAKVQ YFRNGRGKKY SHGNSDFHIP EAKLEHSGSY FCRGIIGSKN
ESSESVQITV QAPETLQTVS SFFLPWHQIT FCLVMGVLFA VDTGLYFSVR RHLQSSEEWR
DGKVTWSKGP
