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FCERG_CAVPO
ID   FCERG_CAVPO             Reviewed;          86 AA.
AC   Q07249;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yamashita T.;
RL   Submitted (MAY-1993) 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; D16188; BAA03729.1; -; mRNA.
DR   AlphaFoldDB; Q07249; -.
DR   SMR; Q07249; -.
DR   STRING; 10141.ENSCPOP00000013813; -.
DR   eggNOG; ENOG502S7XC; Eukaryota.
DR   InParanoid; Q07249; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0032998; C:Fc-epsilon receptor I complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR   GO; GO:0019767; F:IgE receptor activity; IEA:InterPro.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0038156; P:interleukin-3-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
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..86
FT                   /note="High affinity immunoglobulin epsilon receptor
FT                   subunit gamma"
FT                   /id="PRO_0000016500"
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         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30273"
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;  9742 MW;  99C873D49C97D45B CRC64;
     MYPAVVLLLL LLVEQAAALG EPQLCYILDA ILFLYGIILT LLYCRLKIQV RKATVASYEK
     PDGIYTGLST RNQETYETLK HEKPPQ
 
 
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