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Low affinity immunoglobulin gamma Fc region receptor IV (CD16-2) (FcgammaRIV)

 FCGR4_MOUSE             Reviewed;         249 AA.
A0A0B4J1G0; Q3TC44; Q8R2R4; Q8R477;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
04-MAR-2015, sequence version 1.
30-AUG-2017, entry version 28.
RecName: Full=Low affinity immunoglobulin gamma Fc region receptor IV {ECO:0000312|MGI:MGI:2179523};
AltName: Full=CD16-2 {ECO:0000303|PubMed:12389094};
AltName: Full=FcgammaRIV {ECO:0000303|PubMed:16039578};
Flags: Precursor;
Name=Fcgr4 {ECO:0000312|MGI:MGI:2179523};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
[1] {ECO:0000312|EMBL:AAM19249.1}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM19249.1};
TISSUE=Liver {ECO:0000312|EMBL:AAM19249.1};
PubMed=12389094; DOI=10.1007/s00251-002-0486-0;
Mechetina L.V., Najakshin A.M., Alabyev B.Y., Chikaev N.A.,
Taranin A.V.;
"Identification of CD16-2, a novel mouse receptor homologous to
CD16/Fc gamma RIII.";
Immunogenetics 54:463-468(2002).
[2] {ECO:0000312|EMBL:ABS89131.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=NOD/LtJ {ECO:0000312|EMBL:ABS89131.1};
PubMed=18292508; DOI=10.4049/jimmunol.180.5.2863;
Xiu Y., Wong C.P., Bouaziz J.D., Hamaguchi Y., Wang Y., Pop S.M.,
Tisch R.M., Tedder T.F.;
"B lymphocyte depletion by CD20 monoclonal antibody prevents diabetes
in nonobese diabetic mice despite isotype-specific differences in Fc
gamma R effector functions.";
J. Immunol. 180:2863-2875(2008).
[3] {ECO:0000312|EMBL:BAE42113.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD {ECO:0000312|EMBL:BAE42113.1};
TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE42113.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4] {ECO:0000312|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5] {ECO:0000312|EMBL:EDL39140.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000312|EMBL:AAH27310.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II {ECO:0000312|EMBL:AAH27310.1};
TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH27310.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7] {ECO:0000305}
FUNCTION, INTERACTION WITH FCERG, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND GLYCOSYLATION.
PubMed=16039578; DOI=10.1016/j.immuni.2005.05.010;
Nimmerjahn F., Bruhns P., Horiuchi K., Ravetch J.V.;
"FcgammaRIV: a novel FcR with distinct IgG subclass specificity.";
Immunity 23:41-51(2005).
[8] {ECO:0000305}
FUNCTION, INTERACTION WITH FCERG, TISSUE SPECIFICITY, INDUCTION,
PHOSPHORYLATION AT TYR-235, AND MUTAGENESIS OF TYR-235.
PubMed=17558411; DOI=10.1038/ni1477;
Hirano M., Davis R.S., Fine W.D., Nakamura S., Shimizu K., Yagi H.,
Kato K., Stephan R.P., Cooper M.D.;
"IgEb immune complexes activate macrophages through FcgammaRIV
binding.";
Nat. Immunol. 8:762-771(2007).
[9] {ECO:0000305}
FUNCTION, AND GLYCOSYLATION.
PubMed=18949059; DOI=10.1172/JCI36452;
Mancardi D.A., Iannascoli B., Hoos S., England P., Daeron M.,
Bruhns P.;
"FcgammaRIV is a mouse IgE receptor that resembles macrophage
FcepsilonRI in humans and promotes IgE-induced lung inflammation.";
J. Clin. Invest. 118:3738-3750(2008).
[10] {ECO:0000305}
FUNCTION.
PubMed=18097064; DOI=10.4049/jimmunol.180.1.618;
Jakus Z., Nemeth T., Verbeek J.S., Mocsai A.;
"Critical but overlapping role of FcgammaRIII and FcgammaRIV in
activation of murine neutrophils by immobilized immune complexes.";
J. Immunol. 180:618-629(2008).
[11] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19795417; DOI=10.1002/eji.200939884;
Syed S.N., Konrad S., Wiege K., Nieswandt B., Nimmerjahn F.,
Schmidt R.E., Gessner J.E.;
"Both FcgammaRIV and FcgammaRIII are essential receptors mediating
type II and type III autoimmune responses via FcRgamma-LAT-dependent
generation of C5a.";
Eur. J. Immunol. 39:3343-3356(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-235, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13] {ECO:0000305}
FUNCTION.
PubMed=25824719; DOI=10.1038/ncomms7637;
Negishi-Koga T., Gober H.J., Sumiya E., Komatsu N., Okamoto K.,
Sawa S., Suematsu A., Suda T., Sato K., Takai T., Takayanagi H.;
"Immune complexes regulate bone metabolism through FcRgamma
signalling.";
Nat. Commun. 6:6637-6637(2015).
-!- FUNCTION: Receptor for the Fc region of immunoglobulin gamma
(PubMed:16039578). Also acts as a receptor for the Fc region of
immunoglobulin epsilon (PubMed:17558411, PubMed:18949059). Binds
with intermediate affinity to both IgG2a and IgG2b
(PubMed:16039578, PubMed:17558411, PubMed:19795417). Can bind to
IgG2a and IgG2b monomers (PubMed:18949059). Does not display
binding to IgG1 or IgG3 (PubMed:16039578). Mediates neutrophil
activation by IgG complexes redundantly with Fcgr3
(PubMed:18097064). Plays a role in promoting bone resorption by
enhancing osteoclast differentiation following binding to IgG2a
(PubMed:25824719). Binds with low affinity to both the a and b
allotypes of IgE (PubMed:18949059). Has also been shown to bind to
IgE allotype a only but not to allotype b (PubMed:17558411). Binds
aggregated IgE but not the monomeric form and bound monomeric IgG
is readily displaced by IgE complexes (PubMed:18949059). Binding
to IgE promotes macrophage-mediated phagocytosis, antigen
presentation to T cells, production of proinflammatory cytokines
and the late phase of cutaneous allergic reactions
(PubMed:17558411, PubMed:18949059). {ECO:0000269|PubMed:16039578,
ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:18097064,
ECO:0000269|PubMed:18949059, ECO:0000269|PubMed:19795417,
ECO:0000269|PubMed:25824719}.
-!- SUBUNIT: Interacts with the Fc receptor gamma chain Fcerg; Fcerg
is required for the cell surface expression of Fcrg4.
{ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039578,
ECO:0000269|PubMed:17558411}; Single-pass type I membrane protein
{ECO:0000255}. Note=Cell surface expression is dependent on the
presence of the Fc receptor gamma chain Fcerg.
{ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411}.
-!- TISSUE SPECIFICITY: Detected on myeloid cells, peripheral blood
monocytes, splenic and bone marrow dendritic cells, and
thioglycollate-elicited macrophages and neutrophils but absent
from lymphoid populations with no expression observed on T cells,
B cells, NK cells or other granulocytes (at protein level)
(PubMed:16039578, PubMed:19795417). Expressed in peripheral blood
leukocytes, spleen, liver, thymus and small intestine
(PubMed:12389094, PubMed:17558411). {ECO:0000269|PubMed:12389094,
ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411,
ECO:0000269|PubMed:19795417}.
-!- INDUCTION: By lipopolysaccharide, interferon beta and IFNG.
{ECO:0000269|PubMed:17558411}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16039578,
ECO:0000269|PubMed:18949059}.
-!- PTM: Phosphorylated following receptor ligation.
{ECO:0000269|PubMed:17558411}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF499613; AAM19249.1; -; mRNA.
EMBL; EU050648; ABS89131.1; -; mRNA.
EMBL; AK170920; BAE42113.1; -; mRNA.
EMBL; AC115959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466520; EDL39140.1; -; Genomic_DNA.
EMBL; BC027310; AAH27310.1; -; mRNA.
CCDS; CCDS15476.1; -.
RefSeq; NP_653142.2; NM_144559.2.
UniGene; Mm.251254; -.
ProteinModelPortal; A0A0B4J1G0; -.
SMR; A0A0B4J1G0; -.
STRING; 10090.ENSMUSP00000077873; -.
PaxDb; A0A0B4J1G0; -.
PRIDE; Q8R477; -.
Ensembl; ENSMUST00000078825; ENSMUSP00000077873; ENSMUSG00000059089.
GeneID; 246256; -.
KEGG; mmu:246256; -.
UCSC; uc007dmw.2; mouse.
CTD; 246256; -.
MGI; MGI:2179523; Fcgr4.
eggNOG; ENOG410IKYD; Eukaryota.
eggNOG; ENOG41114N1; LUCA.
GeneTree; ENSGT00760000119130; -.
HOGENOM; HOG000251632; -.
HOVERGEN; HBG051602; -.
KO; K06463; -.
OMA; FCRGIIG; -.
OrthoDB; EOG091G0JSA; -.
PhylomeDB; A0A0B4J1G0; -.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:A0A0B4J1G0; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000059089; -.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
GO; GO:0019767; F:IgE receptor activity; IDA:UniProtKB.
GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
GO; GO:0019770; F:IgG receptor activity; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042119; P:neutrophil activation; IMP:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; IMP:UniProtKB.
GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
IgE-binding protein; IgG-binding protein; Immunoglobulin domain;
Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 249 Low affinity immunoglobulin gamma Fc
region receptor IV. {ECO:0000255}.
/FTId=PRO_5008204824.
TOPO_DOM 21 203 Extracellular. {ECO:0000305}.
TRANSMEM 204 224 Helical. {ECO:0000255}.
TOPO_DOM 225 249 Cytoplasmic. {ECO:0000305}.
DOMAIN 22 102 Ig-like C2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 119 188 Ig-like C2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
MOD_RES 235 235 Phosphotyrosine.
{ECO:0000244|PubMed:19144319,
ECO:0000269|PubMed:17558411}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 46 88 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 127 171 {ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 235 235 Y->W: Abolishes receptor ligation-induced
phosphorylation.
{ECO:0000269|PubMed:17558411}.
CONFLICT 57 57 I -> T (in Ref. 2; ABS89131 and 3;
BAE42113). {ECO:0000305}.
CONFLICT 141 141 L -> S (in Ref. 6; AAH27310).
{ECO:0000305}.
CONFLICT 157 157 L -> P (in Ref. 1; AAM19249).
{ECO:0000305}.
SEQUENCE 249 AA; 28398 MW; 99BBA7992862E80C CRC64;
MWQLLLPTAL VLTAFSGIQA GLQKAVVNLD PKWVRVLEED SVTLRCQGTF SPEDNSIKWF
HNESLIPHQD ANYVIQSARV KDSGMYRCQT ALSTISDPVQ LEVHMGWLLL QTTKWLFQEG
DPIHLRCHSW QNRPVRKVTY LQNGKGKKYF HENSELLIPK ATHNDSGSYF CRGLIGHNNK
SSASFRISLG DPGSPSMFPP WHQITFCLLI GLLFAIDTVL YFSVRRGLQS PVADYEEPKI
QWSKEPQDK


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