FCERG_RAT
ID FCERG_RAT Reviewed; 86 AA.
AC P20411;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 150.
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; Synonyms=Fce1g;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2521376; DOI=10.1038/337187a0;
RA Blank U., Ra C., Miller L., White K., Metzger H., Kinet J.-P.;
RT "Complete structure and expression in transfected cells of high affinity
RT IgE receptor.";
RL Nature 337:187-189(1989).
RN [2]
RP SUBUNIT, AND INTERACTION WITH FCGR3A AND CD247.
RX PubMed=1825220;
RA Lanier L.L., Yu G., Phillips J.H.;
RT "Analysis of Fc gamma RIII (CD16) membrane expression and association with
RT CD3 zeta and Fc epsilon RI-gamma by site-directed mutation.";
RL J. Immunol. 146:1571-1576(1991).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17728245; DOI=10.1074/jbc.m705950200;
RA Ganguly S., Grodzki C., Sugden D., Moller M., Odom S., Gaildrat P.,
RA Gery I., Siraganian R.P., Rivera J., Klein D.C.;
RT "Neural adrenergic/cyclic AMP regulation of the immunoglobulin E receptor
RT alpha-subunit expression in the mammalian pinealocyte: a
RT neuroendocrine/immune response link?";
RL J. Biol. Chem. 282:32758-32764(2007).
RN [4]
RP SUBUNIT.
RX PubMed=23921530; DOI=10.1002/eji.201343752;
RA Lobato-Pascual A., Saether P.C., Fossum S., Dissen E., Daws M.R.;
RT "Mincle, the receptor for mycobacterial cord factor, forms a functional
RT receptor complex with MCL and FcepsilonRI-gamma.";
RL Eur. J. Immunol. 43:3167-3174(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 As a constitutive component of interleukin-3 receptor complex,
CC selectively mediates interleukin 4/IL4 production by basophils priming
CC T-cells toward effector T-helper 2 subset. Associates with pattern
CC recognition receptors CLEC4D and CLEC4E to form a functional signaling
CC complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-
CC dimycolate (TDM) to this receptor complex leads to phosphorylation of
CC ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently
CC driving maturation of antigen-presenting cells and shaping antigen-
CC specific priming of T-cells toward effector T-helper 1 and T-helper 17
CC cell subtypes. May function cooperatively with other activating
CC receptors. Functionally linked to integrin beta-2/ITGB2-mediated
CC neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated
CC platelet activation. {ECO:0000250|UniProtKB:P20491}.
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 to form a
CC functional receptor 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 (PubMed:1825220).
CC Associates with CLEC6A. Interacts with CLEC4E (PubMed:23921530).
CC Interacts (via ITAM domain) with SYK (via SH2 domains); activates SYK,
CC enabling integrin-mediated activation of neutrophils and macrophages
CC (By similarity). Interacts with common beta chain of interleukin 3
CC receptor CSF2RB and recruits SYK in response to IL3 stimulation; this
CC interaction is direct (By similarity). Interacts with CD300LH; the
CC interaction may be indirect. Interacts with CD300LD (By similarity).
CC Interacts with TARM1 (By similarity). {ECO:0000250|UniProtKB:P20491,
CC ECO:0000250|UniProtKB:P30273, ECO:0000269|PubMed:1825220,
CC ECO:0000269|PubMed:23921530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leukocytes and pinealocytes.
CC Expression in the pineal gland does not undergo circadian variations.
CC {ECO:0000269|PubMed:17728245}.
CC -!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
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DR EMBL; L04306; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; S02118; S02118.
DR RefSeq; NP_001124473.1; NM_001131001.1.
DR AlphaFoldDB; P20411; -.
DR SMR; P20411; -.
DR BioGRID; 247476; 2.
DR IntAct; P20411; 1.
DR MINT; P20411; -.
DR STRING; 10116.ENSRNOP00000036716; -.
DR iPTMnet; P20411; -.
DR PhosphoSitePlus; P20411; -.
DR PaxDb; P20411; -.
DR PRIDE; P20411; -.
DR ABCD; P20411; 2 sequenced antibodies.
DR GeneID; 25441; -.
DR KEGG; rno:25441; -.
DR UCSC; RGD:2599; rat.
DR CTD; 2207; -.
DR RGD; 2599; Fcer1g.
DR VEuPathDB; HostDB:ENSRNOG00000024159; -.
DR eggNOG; ENOG502S7XC; Eukaryota.
DR HOGENOM; CLU_192374_0_0_1; -.
DR InParanoid; P20411; -.
DR OMA; CRLKIQM; -.
DR OrthoDB; 1577383at2759; -.
DR PhylomeDB; P20411; -.
DR TreeFam; TF330937; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-RNO-5621480; Dectin-2 family.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
DR PRO; PR:P20411; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000024159; Expressed in spleen and 20 other tissues.
DR ExpressionAtlas; P20411; baseline and differential.
DR Genevisible; P20411; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0032998; C:Fc-epsilon receptor I complex; ISO:RGD.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019863; F:IgE binding; ISO:RGD.
DR GO; GO:0019767; F:IgE receptor activity; ISO:RGD.
DR GO; GO:0019864; F:IgG binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; ISO:RGD.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; ISO:RGD.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; ISO:RGD.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; ISO:RGD.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0038156; P:interleukin-3-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045576; P:mast cell activation; ISO:RGD.
DR GO; GO:0033026; P:negative regulation of mast cell apoptotic process; ISO:RGD.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0050778; P:positive regulation of immune response; ISO:RGD.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0032765; P:positive regulation of mast cell cytokine production; ISO:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0001812; P:positive regulation of type I hypersensitivity; ISO:RGD.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; ISO:RGD.
DR GO; GO:0001805; P:positive regulation of type III hypersensitivity; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; ISO:RGD.
DR GO; GO:0010543; P:regulation of platelet activation; ISO:RGD.
DR GO; GO:0002554; P:serotonin secretion by platelet; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0002292; P:T cell differentiation involved in immune response; ISO:RGD.
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; Direct protein sequencing; Disulfide bond;
KW IgE-binding protein; Immunity; Innate immunity; Membrane; Phosphoprotein;
KW Receptor; 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_0000016505"
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:0000250|UniProtKB:P20491,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20491,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20491"
FT DISULFID 25
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 86 AA; 9765 MW; BD7B12E804311687 CRC64;
MIPAVILFLL LLVEEAAALG EPQLCYILDA ILFLYGIVLT LLYCRLKIQV RKADIASREK
SDAVYTGLNT RNQETYETLK HEKPPQ
