FCGR3_MOUSE
ID FCGR3_MOUSE Reviewed; 261 AA.
AC P08508;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 165.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III;
DE Short=IgG Fc receptor III;
DE AltName: Full=Fc-gamma RIII;
DE Short=FcRIII;
DE AltName: CD_antigen=CD16;
DE Flags: Precursor;
GN Name=Fcgr3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2946078; DOI=10.1126/science.2946078;
RA Ravetch J.V., Luster A.D., Weinshank R., Kochan J., Pavlovec A.,
RA Portnoy D.A., Hulmes J., Pan Y.-C.E., Unkeless J.C.;
RT "Structural heterogeneity and functional domains of murine immunoglobulin G
RT Fc receptors.";
RL Science 234:718-725(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-29.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Soares H.J., Onken M.D., Kulczycki A. Jr.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-22.
RX PubMed=8070412; DOI=10.1002/j.1460-2075.1994.tb06696.x;
RA Feinman R., Qiu W.Q., Pearse R.N., Nikolajczyk B.S., Sen R., Sheffery M.,
RA Ravetch J.V.;
RT "PU.1 and an HLH family member contribute to the myeloid-specific
RT transcription of the Fc gamma RIIIA promoter.";
RL EMBO J. 13:3852-3860(1994).
RN [4]
RP INTERACTION WITH INPP5D.
RX PubMed=12393695; DOI=10.1182/blood-2002-04-1058;
RA Galandrini R., Tassi I., Mattia G., Lenti L., Piccoli M., Frati L.,
RA Santoni A.;
RT "SH2-containing inositol phosphatase (SHIP-1) transiently translocates to
RT raft domains and modulates CD16-mediated cytotoxicity in human NK cells.";
RL Blood 100:4581-4589(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17558411; DOI=10.1038/ni1477;
RA Hirano M., Davis R.S., Fine W.D., Nakamura S., Shimizu K., Yagi H.,
RA Kato K., Stephan R.P., Cooper M.D.;
RT "IgEb immune complexes activate macrophages through FcgammaRIV binding.";
RL Nat. Immunol. 8:762-771(2007).
RN [6]
RP FUNCTION.
RX PubMed=18097064; DOI=10.4049/jimmunol.180.1.618;
RA Jakus Z., Nemeth T., Verbeek J.S., Mocsai A.;
RT "Critical but overlapping role of FcgammaRIII and FcgammaRIV in activation
RT of murine neutrophils by immobilized immune complexes.";
RL J. Immunol. 180:618-629(2008).
CC -!- FUNCTION: Receptor for the Fc region of complexed immunoglobulins
CC gamma. Low affinity receptor which binds to IgG1, IgG2a and IgG2b
CC (PubMed:17558411). Mediates neutrophil activation by IgG complexes
CC redundantly with Fcgr4 (PubMed:18097064). {ECO:0000269|PubMed:17558411,
CC ECO:0000269|PubMed:18097064}.
CC -!- SUBUNIT: Interacts with INPP5D/SHIP1. {ECO:0000269|PubMed:12393695}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17558411};
CC Single-pass type I membrane protein {ECO:0000305}.
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DR EMBL; M14215; AAA37604.1; -; mRNA.
DR EMBL; X60929; CAA43266.1; -; Genomic_DNA.
DR PIR; S29360; S29360.
DR AlphaFoldDB; P08508; -.
DR SMR; P08508; -.
DR STRING; 10090.ENSMUSP00000131938; -.
DR GlyGen; P08508; 4 sites.
DR PhosphoSitePlus; P08508; -.
DR jPOST; P08508; -.
DR MaxQB; P08508; -.
DR PaxDb; P08508; -.
DR PeptideAtlas; P08508; -.
DR PRIDE; P08508; -.
DR ProteomicsDB; 267724; -.
DR ABCD; P08508; 21 sequenced antibodies.
DR MGI; MGI:95500; Fcgr3.
DR eggNOG; ENOG502SVEW; Eukaryota.
DR InParanoid; P08508; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR ChiTaRS; Fcgr3; mouse.
DR PRO; PR:P08508; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P08508; protein.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019864; F:IgG binding; IMP:MGI.
DR GO; GO:0019770; F:IgG receptor activity; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IMP:MGI.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR GO; GO:0045576; P:mast cell activation; IDA:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0001812; P:positive regulation of type I hypersensitivity; IDA:MGI.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IMP:MGI.
DR GO; GO:0001805; P:positive regulation of type III hypersensitivity; IMP:MGI.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR GO; GO:0001820; P:serotonin secretion; IDA:MGI.
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; Disulfide bond; Glycoprotein; IgG-binding protein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..261
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III"
FT /id="PRO_0000015154"
FT TOPO_DOM 31..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..110
FT /note="Ig-like C2-type 1"
FT DOMAIN 116..198
FT /note="Ig-like C2-type 2"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 261 AA; 30036 MW; 757FB83668E41069 CRC64;
MFQNAHSGSQ WLLPPLTILL LFAFADRQSA ALPKAVVKLD PPWIQVLKED MVTLMCEGTH
NPGNSSTQWF HNGRSIRSQV QASYTFKATV NDSGEYRCQM EQTRLSDPVD LGVISDWLLL
QTPQRVFLEG ETITLRCHSW RNKLLNRISF FHNEKSVRYH HYKSNFSIPK ANHSHSGDYY
CKGSLGSTQH QSKPVTITVQ DPATTSSISL VWYHTAFSLV MCLLFAVDTG LYFYVRRNLQ
TPREYWRKSL SIRKHQAPQD K
