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FCERG_MOUSE
ID   FCERG_MOUSE             Reviewed;          86 AA.
AC   P20491;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=High affinity immunoglobulin epsilon receptor subunit gamma;
DE   AltName: Full=Fc receptor gamma-chain;
DE            Short=FcRgamma;
DE   AltName: Full=Fc-epsilon RI-gamma;
DE   AltName: Full=IgE Fc receptor subunit gamma;
DE            Short=FceRI gamma;
DE   Flags: Precursor;
GN   Name=Fcer1g {ECO:0000303|PubMed:14764707, ECO:0000303|PubMed:19098920,
GN   ECO:0000312|MGI:MGI:95496}; Synonyms=Fce1g;
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=2527850; DOI=10.1016/s0021-9258(19)84829-9;
RA   Ra C., Jouvin M.H.E., Kinet J.-P.;
RT   "Complete structure of the mouse mast cell receptor for IgE (Fc epsilon RI)
RT   and surface expression of chimeric receptors (rat-mouse-human) on
RT   transfected cells.";
RL   J. Biol. Chem. 264:15323-15327(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION IN ACTIVATION OF PLATELETS BY COLLAGEN, AND FUNCTION IN PLCG2
RP   PHOSPHORYLATION.
RX   PubMed=9171347; DOI=10.1093/emboj/16.9.2333;
RA   Poole A., Gibbins J.M., Turner M., van Vugt M.J., van de Winkel J.G.,
RA   Saito T., Tybulewicz V.L., Watson S.P.;
RT   "The Fc receptor gamma-chain and the tyrosine kinase Syk are essential for
RT   activation of mouse platelets by collagen.";
RL   EMBO J. 16:2333-2341(1997).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   TYR-65; TYR-76 AND 65-TYR--GLN-86.
RX   PubMed=14764707; DOI=10.4049/jimmunol.172.4.2374;
RA   Sakurai D., Yamasaki S., Arase K., Park S.Y., Arase H., Konno A., Saito T.;
RT   "Fc epsilon RI gamma-ITAM is differentially required for mast cell function
RT   in vivo.";
RL   J. Immunol. 172:2374-2381(2004).
RN   [5]
RP   INTERACTION WITH CLEC6A.
RX   PubMed=17050534; DOI=10.1074/jbc.m606542200;
RA   Sato K., Yang X.L., Yudate T., Chung J.S., Wu J., Luby-Phelps K.,
RA   Kimberly R.P., Underhill D., Cruz P.D. Jr., Ariizumi K.;
RT   "Dectin-2 is a pattern recognition receptor for fungi that couples with the
RT   Fc receptor gamma chain to induce innate immune responses.";
RL   J. Biol. Chem. 281:38854-38866(2006).
RN   [6]
RP   FUNCTION IN INTEGRIN-MEDIATED NEUTROPHIL ACTIVATION, AND INTERACTION WITH
RP   SYK.
RX   PubMed=17086186; DOI=10.1038/ni1407;
RA   Mocsai A., Abram C.L., Jakus Z., Hu Y., Lanier L.L., Lowell C.A.;
RT   "Integrin signaling in neutrophils and macrophages uses adapters containing
RT   immunoreceptor tyrosine-based activation motifs.";
RL   Nat. Immunol. 7:1326-1333(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65; TYR-76 AND THR-78, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   INTERACTION WITH CLEC4E.
RX   PubMed=18776906; DOI=10.1038/ni.1651;
RA   Yamasaki S., Ishikawa E., Sakuma M., Hara H., Ogata K., Saito T.;
RT   "Mincle is an ITAM-coupled activating receptor that senses damaged cells.";
RL   Nat. Immunol. 9:1179-1188(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65 AND TYR-76, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-29; LEU-39; TYR-65 AND TYR-76, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=19098920; DOI=10.1038/ni.1686;
RA   Hida S., Yamasaki S., Sakamoto Y., Takamoto M., Obata K., Takai T.,
RA   Karasuyama H., Sugane K., Saito T., Taki S.;
RT   "Fc receptor gamma-chain, a constitutive component of the IL-3 receptor, is
RT   required for IL-3-induced IL-4 production in basophils.";
RL   Nat. Immunol. 10:214-222(2009).
RN   [11]
RP   INTERACTION WITH CD300LH AND CD300LD.
RX   PubMed=20817736; DOI=10.1074/jbc.m110.137166;
RA   Enomoto Y., Yamanishi Y., Izawa K., Kaitani A., Takahashi M., Maehara A.,
RA   Oki T., Takamatsu R., Kajikawa M., Takai T., Kitamura T., Kitaura J.;
RT   "Characterization of leukocyte mono-immunoglobulin-like receptor 7
RT   (LMIR7)/CLM-3 as an activating receptor: its similarities to and
RT   differences from LMIR4/CLM-5.";
RL   J. Biol. Chem. 285:35274-35283(2010).
RN   [12]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=23602766; DOI=10.1016/j.immuni.2013.03.010;
RA   Miyake Y., Toyonaga K., Mori D., Kakuta S., Hoshino Y., Oyamada A.,
RA   Yamada H., Ono K., Suyama M., Iwakura Y., Yoshikai Y., Yamasaki S.;
RT   "C-type lectin MCL is an FcRgamma-coupled receptor that mediates the
RT   adjuvanticity of mycobacterial cord factor.";
RL   Immunity 38:1050-1062(2013).
CC   -!- FUNCTION: Adapter protein containing an immunoreceptor tyrosine-based
CC       activation motif (ITAM) that transduces activation signals from various
CC       immunoreceptors. As a component of the high-affinity immunoglobulin E
CC       (IgE) receptor, mediates allergic inflammatory signaling in mast cells
CC       (PubMed:14764707). As a constitutive component of interleukin-3
CC       receptor complex, selectively mediates interleukin 4/IL4 production by
CC       basophils, priming T-cells toward effector T-helper 2 subset
CC       (PubMed:19098920). Associates with pattern recognition receptors CLEC4D
CC       and CLEC4E to form a functional signaling complex in myeloid cells.
CC       Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this
CC       receptor complex leads to phosphorylation of ITAM, triggering
CC       activation of SYK, CARD9 and NF-kappa-B, consequently driving
CC       maturation of antigen-presenting cells and shaping antigen-specific
CC       priming of T-cells toward effector T-helper 1 and T-helper 17 cell
CC       subtypes (PubMed:23602766) (Probable). May function cooperatively with
CC       other activating receptors. Functionally linked to integrin beta-
CC       2/ITGB2-mediated neutrophil activation (PubMed:17086186). Also involved
CC       in integrin alpha-2/ITGA2-mediated platelet activation
CC       (PubMed:9171347). {ECO:0000269|PubMed:14764707,
CC       ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:19098920,
CC       ECO:0000269|PubMed:23602766, ECO:0000269|PubMed:9171347, ECO:0000305}.
CC   -!- SUBUNIT: IgE Fc receptor is a tetramer of an alpha chain, a beta chain,
CC       and two disulfide linked gamma chains. Associates with FCGR1A; forms a
CC       functional signaling complex (By similarity). The signaling subunit of
CC       immunoglobulin gamma (IgG) Fc receptor complex. As a homodimer or a
CC       heterodimer of CD247 and FCER1G, associates with the ligand binding
CC       subunit FCGR3A to form a functional receptor complex (By similarity).
CC       Associates with CLEC6A (PubMed:17050534). Interacts with CLEC4E
CC       (PubMed:23602766, PubMed:18776906). Interacts (via ITAM domain) with
CC       SYK (via SH2 domains); activates SYK, enabling integrin-mediated
CC       activation of neutrophils and macrophages (PubMed:17086186). Interacts
CC       with CSF2RB and recruits SYK in response to IL3 stimulation; this
CC       interaction is direct (PubMed:19098920). Interacts with CD300LH; the
CC       interaction may be indirect (PubMed:20817736). Interacts with CD300LD
CC       (PubMed:20817736). Interacts with TARM1 (By similarity).
CC       {ECO:0000250|UniProtKB:P20411, ECO:0000250|UniProtKB:P30273,
CC       ECO:0000269|PubMed:17050534, ECO:0000269|PubMed:17086186,
CC       ECO:0000269|PubMed:18776906, ECO:0000269|PubMed:19098920,
CC       ECO:0000269|PubMed:20817736, ECO:0000269|PubMed:23602766}.
CC   -!- INTERACTION:
CC       P20491; Q62120: Jak2; NbExp=2; IntAct=EBI-9306159, EBI-646604;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in mast cells (at protein level)
CC       (PubMed:14764707). Expressed in basophils (at protein level)
CC       (PubMed:19098920). {ECO:0000269|PubMed:14764707,
CC       ECO:0000269|PubMed:19098920}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice are resistant to IgE-mediated
CC       systemic anaphylaxis. {ECO:0000269|PubMed:14764707}.
CC   -!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
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DR   EMBL; J05020; AAA37602.1; -; mRNA.
DR   EMBL; BC034163; AAH34163.1; -; mRNA.
DR   CCDS; CCDS15483.1; -.
DR   RefSeq; NP_034315.1; NM_010185.4.
DR   AlphaFoldDB; P20491; -.
DR   SMR; P20491; -.
DR   BioGRID; 199616; 3.
DR   IntAct; P20491; 1.
DR   STRING; 10090.ENSMUSP00000078875; -.
DR   iPTMnet; P20491; -.
DR   PhosphoSitePlus; P20491; -.
DR   SwissPalm; P20491; -.
DR   jPOST; P20491; -.
DR   MaxQB; P20491; -.
DR   PaxDb; P20491; -.
DR   PeptideAtlas; P20491; -.
DR   PRIDE; P20491; -.
DR   ProteomicsDB; 267364; -.
DR   Antibodypedia; 20505; 168 antibodies from 29 providers.
DR   DNASU; 14127; -.
DR   Ensembl; ENSMUST00000079957; ENSMUSP00000078875; ENSMUSG00000058715.
DR   GeneID; 14127; -.
DR   KEGG; mmu:14127; -.
DR   UCSC; uc007dnl.1; mouse.
DR   CTD; 2207; -.
DR   MGI; MGI:95496; Fcer1g.
DR   VEuPathDB; HostDB:ENSMUSG00000058715; -.
DR   eggNOG; ENOG502S7XC; Eukaryota.
DR   GeneTree; ENSGT00390000003894; -.
DR   HOGENOM; CLU_192374_0_0_1; -.
DR   InParanoid; P20491; -.
DR   OMA; CRLKIQM; -.
DR   OrthoDB; 1577383at2759; -.
DR   PhylomeDB; P20491; -.
DR   TreeFam; TF330937; -.
DR   Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
DR   Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-MMU-5621480; Dectin-2 family.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR   BioGRID-ORCS; 14127; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Fcer1g; mouse.
DR   PRO; PR:P20491; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P20491; protein.
DR   Bgee; ENSMUSG00000058715; Expressed in granulocyte and 147 other tissues.
DR   ExpressionAtlas; P20491; baseline and differential.
DR   Genevisible; P20491; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0032998; C:Fc-epsilon receptor I complex; IMP:MGI.
DR   GO; GO:0033001; C:Fc-gamma receptor III complex; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0019863; F:IgE binding; IDA:MGI.
DR   GO; GO:0019767; F:IgE receptor activity; IDA:MGI.
DR   GO; GO:0019864; F:IgG binding; IMP:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IMP:MGI.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR   GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; IMP:MGI.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; ISO:MGI.
DR   GO; GO:0038094; P:Fc-gamma receptor signaling pathway; IDA:MGI.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR   GO; GO:0045087; P:innate immune response; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0038156; P:interleukin-3-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0045576; P:mast cell activation; IDA:MGI.
DR   GO; GO:0033024; P:mast cell apoptotic process; IDA:MGI.
DR   GO; GO:0043303; P:mast cell degranulation; IDA:MGI.
DR   GO; GO:0033026; P:negative regulation of mast cell apoptotic process; IDA:MGI.
DR   GO; GO:0002283; P:neutrophil activation involved in immune response; IMP:UniProtKB.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR   GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
DR   GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:MGI.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:MGI.
DR   GO; GO:0032765; P:positive regulation of mast cell cytokine production; IDA:MGI.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:MGI.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR   GO; GO:0001812; P:positive regulation of type I hypersensitivity; IMP: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:0072659; P:protein localization to plasma membrane; IDA:MGI.
DR   GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR   GO; GO:0010543; P:regulation of platelet activation; IMP:UniProtKB.
DR   GO; GO:0002554; P:serotonin secretion by platelet; IMP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
DR   GO; GO:0002292; P:T cell differentiation involved in immune response; IMP:MGI.
DR   InterPro; IPR021663; CD3_zeta/IgE_Fc_rcpt_gamma.
DR   InterPro; IPR042340; FCER1G.
DR   InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR   PANTHER; PTHR16803; PTHR16803; 1.
DR   Pfam; PF02189; ITAM; 1.
DR   Pfam; PF11628; TCR_zetazeta; 1.
DR   SMART; SM00077; ITAM; 1.
DR   PROSITE; PS51055; ITAM_1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; IgE-binding protein; Immunity;
KW   Innate immunity; Membrane; Metal-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..86
FT                   /note="High affinity immunoglobulin epsilon receptor
FT                   subunit gamma"
FT                   /id="PRO_0000016503"
FT   TOPO_DOM        19..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..82
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOD_RES         65
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660,
FT                   ECO:0007744|PubMed:19144319"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660,
FT                   ECO:0007744|PubMed:19144319"
FT   MOD_RES         78
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   DISULFID        25
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         29
FT                   /note="D->A: Increases IL3-induced production of IL4 by
FT                   basophils."
FT                   /evidence="ECO:0000269|PubMed:19098920"
FT   MUTAGEN         39
FT                   /note="L->A: Impairs interaction with CSF2RB. Impairs IL3-
FT                   induced production of IL4 by basophils."
FT                   /evidence="ECO:0000269|PubMed:19098920"
FT   MUTAGEN         65..86
FT                   /note="Missing: Impairs IgE-induced mast cell activation in
FT                   the presence of antigen; Impairs IgE-induced mast cell
FT                   survival in the absence of antigen."
FT                   /evidence="ECO:0000269|PubMed:14764707"
FT   MUTAGEN         65
FT                   /note="Y->P: Impairs IgE-induced mast cell activation in
FT                   the presence of antigen; Impairs IgE-induced mast cell
FT                   survival in the absence of antigen; when associated with P-
FT                   76. Impairs IL3-induced production of IL4 by basophils;
FT                   when associated with P-76."
FT                   /evidence="ECO:0000269|PubMed:14764707,
FT                   ECO:0000269|PubMed:19098920"
FT   MUTAGEN         76
FT                   /note="Y->P: Impairs IgE-induced mast cell activation in
FT                   the presence of antigen; Impairs IgE-induced mast cell
FT                   survival in the absence of antigen; when associated with P-
FT                   65. Impairs IL3-induced production of IL4 by basophils;
FT                   when associated with P-65."
FT                   /evidence="ECO:0000269|PubMed:14764707,
FT                   ECO:0000269|PubMed:19098920"
SQ   SEQUENCE   86 AA;  9652 MW;  83184DE22FCC9ECB CRC64;
     MISAVILFLL LLVEQAAALG EPQLCYILDA VLFLYGIVLT LLYCRLKIQV RKAAIASREK
     ADAVYTGLNT RSQETYETLK HEKPPQ
 
 
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