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Low affinity immunoglobulin gamma Fc region receptor II (Fc gamma receptor IIB) (Fc-gamma RII) (Fc-gamma-RIIB) (FcRII) (IgG Fc receptor II beta) (Lymphocyte antigen 17) (Ly-17) (CD antigen CD32)

 FCGR2_MOUSE             Reviewed;         330 AA.
P08101; P08102; P12316; P97917; Q60938; Q60939; Q60940; Q61170;
Q61558;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 167.
RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II;
AltName: Full=Fc gamma receptor IIB;
Short=Fc-gamma RII;
Short=Fc-gamma-RIIB;
Short=FcRII;
AltName: Full=IgG Fc receptor II beta;
AltName: Full=Lymphocyte antigen 17;
Short=Ly-17;
AltName: CD_antigen=CD32;
Flags: Precursor;
Name=Fcgr2; Synonyms=Fcgr2b, Ly-17;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-51 (ISOFORMS
IIB1 AND IIB2).
PubMed=2946078; DOI=10.1126/science.2946078;
Ravetch J.V., Luster A.D., Weinshank R., Kochan J., Pavlovec A.,
Portnoy D.A., Hulmes J., Pan Y.-C.E., Unkeless J.C.;
"Structural heterogeneity and functional domains of murine
immunoglobulin G Fc receptors.";
Science 234:718-725(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
TISSUE=Macrophage;
PubMed=3024012; DOI=10.1038/324372a0;
Lewis V.A., Koch T., Plutner H., Mellman I.;
"A complementary DNA clone for a macrophage-lymphocyte Fc receptor.";
Nature 324:372-375(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM
IIB1).
PubMed=2957319; DOI=10.1007/BF00365906;
Hogarth P.M., Hibbs M.L., Bonadonna L., Scott B.M., Witort E.,
Pietersz G.A., McKenzie I.F.C.;
"The mouse Fc receptor for IgG (Ly-17): molecular cloning and
specificity.";
Immunogenetics 26:161-168(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM IIB1), POLYMORPHISM, AND
VARIANTS.
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=2138587; DOI=10.1007/BF00211557;
Lah M., Quelch K., Deacon N.J., McKenzie I.F., Hogarth P.M.;
"Identification of the mouse beta Fc gamma RII polymorphism by direct
sequencing of amplified genomic DNA.";
Immunogenetics 31:202-206(1990).
[5]
NUCLEOTIDE SEQUENCE (ISOFORMS IIB1 AND IIB2).
PubMed=1824594;
Hogarth P.M., Witort E., Hulett M.D., Bonnerot C., Even J.,
Fridman W.H., McKenzie I.F.C.;
"Structure of the mouse beta Fc gamma receptor II gene.";
J. Immunol. 146:369-376(1991).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB1').
STRAIN=DBA/2J; TISSUE=Mast cell;
PubMed=8683114;
Latour S., Fridman W.H., Daeron M.;
"Identification, molecular cloning, biologic properties, and tissue
distribution of a novel isoform of murine low-affinity IgG receptor
homologous to human Fc gamma RIIB1.";
J. Immunol. 157:189-197(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-330 (ISOFORMS IIB1 AND IIB2).
STRAIN=DBA/2J, and NZB; TISSUE=Spleen;
PubMed=8537115;
Sawchuk D.J., Mahmoudi M., Cairns E., Sinclair N.R.S.;
"Nonsynonymous mutations in an Fc-receptor structural gene in NZB
mice.";
Immunogenetics 43:112-113(1996).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-45.
PubMed=2944118; DOI=10.1073/pnas.83.18.6980;
Hibbs M.L., Walker I.D., Kirszbaum L., Peitersz G.A., Deacon N.J.,
Chambers G.W., McKenzie I.F.C., Hogarth P.M.;
"The murine Fc receptor for immunoglobulin: purification, partial
amino acid sequence, and isolation of cDNA clones.";
Proc. Natl. Acad. Sci. U.S.A. 83:6980-6984(1986).
[9]
CHARACTERIZATION OF ISOFORM IIB3.
TISSUE=Macrophage;
PubMed=8398981; DOI=10.1093/intimm/5.8.859;
Tartour E., de la Salle H., de la Salle C., Teillaud C., Camoin L.,
Galinha A., Latour S., Hanau D., Fridman W.H., Sautes C.;
"Identification, in mouse macrophages and in serum, of a soluble
receptor for the Fc portion of IgG (Fc gamma R) encoded by an
alternatively spliced transcript of the Fc gamma RII gene.";
Int. Immunol. 5:859-868(1993).
[10]
PHOSPHORYLATION, AND INTERACTION WITH LYN.
PubMed=9469421;
Malbec O., Fong D.C., Turner M., Tybulewicz V.L., Cambier J.C.,
Fridman W.H., Daeron M.;
"Fc epsilon receptor I-associated lyn-dependent phosphorylation of Fc
gamma receptor IIB during negative regulation of mast cell
activation.";
J. Immunol. 160:1647-1658(1998).
[11]
PHOSPHORYLATION AT TYR-290; TYR-309 AND TYR-326.
PubMed=11035084; DOI=10.4049/jimmunol.165.8.4453;
Fong D.C., Brauweiler A., Minskoff S.A., Bruhns P., Tamir I.,
Mellman I., Daeron M., Cambier J.C.;
"Mutational analysis reveals multiple distinct sites within Fc gamma
receptor IIB that function in inhibitory signaling.";
J. Immunol. 165:4453-4462(2000).
-!- FUNCTION: Receptor for the Fc region of complexed immunoglobulins
gamma. Low affinity receptor. Involved in a variety of effector
and regulatory functions such as phagocytosis of antigen-antibody
complexes from the circulation and modulation of antibody
production by B-cells. Isoform IIB1 and isoform IIB1' form caps
but fail to mediate endocytosis or phagocytosis. Isoform IIB2 can
mediate the endocytosis of soluble immune complexes via clathrin-
coated pits. Isoform IIB1 and isoform IIB2 can down-regulate B-
cell, T-cell, and mast cell activation when coaggregated to B-cell
receptors for AG (BCR), T-cell receptors for AG (TCR), and Fc
receptors, respectively.
-!- SUBUNIT: Interacts with FGR (By similarity). Interacts with LYN.
{ECO:0000250, ECO:0000269|PubMed:9469421}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform IIB1: Cytoplasm, cytoskeleton.
Note=Binds the cytoskeleton and is not localized in endocytotic
pits.
-!- SUBCELLULAR LOCATION: Isoform IIB3: Secreted. Note=Released as a
soluble molecule.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=IIB1; Synonyms=Beta-1;
IsoId=P08101-1; Sequence=Displayed;
Name=IIB2; Synonyms=Beta-2;
IsoId=P08101-2; Sequence=VSP_002640;
Name=IIB1'; Synonyms=Beta-1';
IsoId=P08101-3; Sequence=VSP_002641;
Name=IIB3; Synonyms=Beta-3;
IsoId=P08101-4; Sequence=Not described;
-!- TISSUE SPECIFICITY: Widely expressed by cells of hemopoietic
origin. The isoforms are differentially expressed. Isoform IIB1 is
preferentially expressed by cells of the lymphoid lineage, isoform
IIB2 by cells of the myeloid lineage, and isoform IIB3 is released
by macrophages and is present in the serum. Isoform IIB1' is
expressed in myeloid and lymphoid cell lines, in normal spleen
cells, and in resting or LPS-activated B-cells but is not detected
in mesenteric lymph node cells.
-!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to
as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This
motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases. Another tyrosine-containing sequence,
more C-terminal, accounts for the ability of isoform IIB2 to
trigger the phagocytosis of particulate immuno complexes.
-!- PTM: Glycosylated.
-!- PTM: When coaggregated to BCR, isoform IIB1 and isoform IIB1'
become tyrosine phosphorylated and bind to the SH2 domains of the
protein tyrosine phosphatase PTPC1. Phosphorylated by SRC-type
Tyr-kinases such as LYN, BLK, FYN and SYK (By similarity).
{ECO:0000250}.
-!- POLYMORPHISM: Ly-17 alloantigenic system involves residues 116 and
161. Ly-17.1 mice are Pro-116 and Glu-161; Ly-17.2 mice are Leu-
116 and Leu-161. These polymorphisms do not affect IgG binding.
{ECO:0000269|PubMed:2138587}.
-!- SEQUENCE CAUTION:
Sequence=CAA28309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M16367; AAA37608.1; -; mRNA.
EMBL; M14216; AAA37609.1; -; mRNA.
EMBL; M17515; AAA37607.1; -; mRNA.
EMBL; M31312; AAA37610.1; -; Genomic_DNA.
EMBL; X04648; CAA28309.1; ALT_INIT; mRNA.
EMBL; U31801; AAA92707.1; -; mRNA.
EMBL; U31802; AAA92708.1; -; mRNA.
EMBL; U31803; AAA92709.1; -; mRNA.
EMBL; U31804; AAA92710.1; -; mRNA.
EMBL; M14276; AAA37605.1; -; mRNA.
EMBL; U51629; AAA97464.1; -; mRNA.
PIR; A40071; A40071.
PIR; B40071; FCMSG1.
PIR; I49660; I49660.
RefSeq; NP_034317.1; NM_010187.2.
UniGene; Mm.425062; -.
ProteinModelPortal; P08101; -.
SMR; P08101; -.
BioGrid; 199619; 4.
ELM; P08101; -.
IntAct; P08101; 1.
STRING; 10090.ENSMUSP00000027966; -.
MEROPS; I43.001; -.
iPTMnet; P08101; -.
PhosphoSitePlus; P08101; -.
UniCarbKB; P08101; -.
PaxDb; P08101; -.
PRIDE; P08101; -.
GeneID; 14130; -.
KEGG; mmu:14130; -.
UCSC; uc007dms.2; mouse. [P08101-1]
UCSC; uc007dmt.2; mouse. [P08101-2]
CTD; 2213; -.
MGI; MGI:95499; Fcgr2b.
eggNOG; ENOG410J9AP; Eukaryota.
eggNOG; ENOG410YXNK; LUCA.
HOVERGEN; HBG051602; -.
InParanoid; P08101; -.
KO; K12560; -.
PhylomeDB; P08101; -.
PRO; PR:P08101; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_FCGR2B; -.
GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
GO; GO:0019864; F:IgG binding; IDA:MGI.
GO; GO:0019772; F:low-affinity IgG receptor activity; ISO:MGI.
GO; GO:0044877; F:macromolecular complex binding; ISO:MGI.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; TAS:MGI.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; IMP:MGI.
GO; GO:0021549; P:cerebellum development; IMP:ARUK-UCL.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0016358; P:dendrite development; IMP:ARUK-UCL.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; ISO:MGI.
GO; GO:0006955; P:immune response; IMP:MGI.
GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IMP:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
GO; GO:0050777; P:negative regulation of immune response; IMP:MGI.
GO; GO:0002638; P:negative regulation of immunoglobulin production; IMP:MGI.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:MGI.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:MGI.
GO; GO:0050765; P:negative regulation of phagocytosis; IMP:MGI.
GO; GO:0001811; P:negative regulation of type I hypersensitivity; IMP:MGI.
GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; IMP:ARUK-UCL.
GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
GO; GO:1905898; P:positive regulation of response to endoplasmic reticulum stress; IMP:ARUK-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:ARUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
GO; GO:1902950; P:regulation of dendritic spine maintenance; IMP:ARUK-UCL.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:ARUK-UCL.
GO; GO:0009617; P:response to bacterium; IMP:MGI.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF13895; Ig_2; 2.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disulfide bond; Glycoprotein;
IgG-binding protein; Immunoglobulin domain; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 29
CHAIN 30 330 Low affinity immunoglobulin gamma Fc
region receptor II.
/FTId=PRO_0000015143.
TOPO_DOM 30 210 Extracellular. {ECO:0000255}.
TRANSMEM 211 231 Helical. {ECO:0000255}.
TOPO_DOM 232 330 Cytoplasmic. {ECO:0000255}.
DOMAIN 50 106 Ig-like C2-type 1.
DOMAIN 131 189 Ig-like C2-type 2.
MOTIF 307 312 ITIM motif.
MOD_RES 290 290 Phosphotyrosine.
{ECO:0000269|PubMed:11035084}.
MOD_RES 309 309 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000250}.
MOD_RES 326 326 Phosphotyrosine.
{ECO:0000269|PubMed:11035084}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 99 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 138 182 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 243 290 ALPGNPDHREMGETLPEEVGEYRQPSGGSVPVSPGPPSGLE
PTSSSPY -> D (in isoform IIB2).
{ECO:0000303|PubMed:3024012,
ECO:0000303|PubMed:8537115}.
/FTId=VSP_002640.
VAR_SEQ 262 290 GEYRQPSGGSVPVSPGPPSGLEPTSSSPY -> D (in
isoform IIB1').
{ECO:0000303|PubMed:8683114}.
/FTId=VSP_002641.
VARIANT 116 116 S -> L (in strain: DBA/2; Ly17.2
allotype). {ECO:0000269|PubMed:2138587}.
VARIANT 116 116 S -> P (in strain: NZB; Ly17.1 allotype).
{ECO:0000269|PubMed:2138587}.
VARIANT 145 145 L -> P.
VARIANT 161 161 H -> L (in strain: DBA/2; Ly17.2
allotype). {ECO:0000269|PubMed:2138587}.
VARIANT 161 161 H -> Q (in strain: NZB; Ly17.1 allotype).
{ECO:0000269|PubMed:2138587}.
VARIANT 190 190 L -> Q.
VARIANT 195 195 P -> T (in strain: NZB).
VARIANT 287 287 S -> I (in strain: NZB).
CONFLICT 270 278 GSVPVSPGP -> LSACQPRA (in Ref. 1;
AAA37608). {ECO:0000305}.
CONFLICT 299 299 A -> P (in Ref. 3 and 4). {ECO:0000305}.
SEQUENCE 330 AA; 36695 MW; A463B9EFF2717511 CRC64;
MESNWTVHVF SRTLCHMLLW TAVLNLAAGT HDLPKAVVKL EPPWIQVLKE DTVTLTCEGT
HNPGNSSTQW FHNGRSIRSQ VQASYTFKAT VNDSGEYRCQ MEQTRLSDPV DLGVISDWLL
LQTPQLVFLE GETITLRCHS WRNKLLNRIS FFHNEKSVRY HHYSSNFSIP KANHSHSGDY
YCKGSLGRTL HQSKPVTITV QGPKSSRSLP VLTIVAAVTG IAVAAIVIIL VSLVYLKKKQ
VPALPGNPDH REMGETLPEE VGEYRQPSGG SVPVSPGPPS GLEPTSSSPY NPPDLEEAAK
TEAENTITYS LLKHPEALDE ETEHDYQNHI


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