FCERG_BOVIN
ID FCERG_BOVIN Reviewed; 85 AA.
AC Q9BDR7; Q3SZX3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11557297; DOI=10.1016/s0165-2427(01)00352-x;
RA Morton H.C., Storset A.K., Brandtzaeg P.;
RT "Cloning and sequencing of a cDNA encoding the bovine FcR gamma chain.";
RL Vet. Immunol. Immunopathol. 82:101-106(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; 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. Interacts with CLEC4E. Interacts (via ITAM
CC domain) with SYK (via SH2 domains); activates SYK, enabling integrin-
CC mediated activation of neutrophils and macrophages (By similarity).
CC Interacts with CSF2RB and recruits SYK in response to IL3 stimulation;
CC this 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:P20411,
CC ECO:0000250|UniProtKB:P20491, ECO:0000250|UniProtKB:P30273}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
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DR EMBL; AF316499; AAK15275.1; -; mRNA.
DR EMBL; BC102668; AAI02669.1; -; mRNA.
DR RefSeq; NP_776962.1; NM_174537.3.
DR AlphaFoldDB; Q9BDR7; -.
DR SMR; Q9BDR7; -.
DR STRING; 9913.ENSBTAP00000033956; -.
DR PaxDb; Q9BDR7; -.
DR PRIDE; Q9BDR7; -.
DR Ensembl; ENSBTAT00000034054; ENSBTAP00000033956; ENSBTAG00000024503.
DR GeneID; 282226; -.
DR KEGG; bta:282226; -.
DR CTD; 2207; -.
DR VEuPathDB; HostDB:ENSBTAG00000024503; -.
DR VGNC; VGNC:28931; FCER1G.
DR eggNOG; ENOG502S7XC; Eukaryota.
DR GeneTree; ENSGT00390000003894; -.
DR HOGENOM; CLU_192374_0_0_1; -.
DR InParanoid; Q9BDR7; -.
DR OMA; CRLKIQM; -.
DR OrthoDB; 1577383at2759; -.
DR TreeFam; TF330937; -.
DR Reactome; R-BTA-114604; GPVI-mediated activation cascade.
DR Reactome; R-BTA-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-BTA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-BTA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-BTA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-BTA-5621480; Dectin-2 family.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-75892; Platelet Adhesion to exposed collagen.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000024503; Expressed in monocyte and 104 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0032998; C:Fc-epsilon receptor I complex; IBA:GO_Central.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0019767; F:IgE receptor activity; IBA:GO_Central.
DR GO; GO:0019864; F:IgG binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; IBA:GO_Central.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0038156; P:interleukin-3-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0010543; P:regulation of platelet activation; IBA:GO_Central.
DR GO; GO:0002292; P:T cell differentiation involved in immune response; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; IgE-binding protein; Immunity;
KW Innate immunity; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..85
FT /note="High affinity immunoglobulin epsilon receptor
FT subunit gamma"
FT /id="PRO_0000016499"
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..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..81
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 64
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20491,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30273"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20491,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20491"
FT DISULFID 25
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 85 AA; 9463 MW; A9569879FEF6BECB CRC64;
MIPAVVLLLL LLVEQAAALG EPQLCYILDA ILFLYGIVLT LLYCRLKLQV RKAATASEKS
DGIYTGLSTR TQETYETLKH EKPPQ
