ID   FCERB_MOUSE             Reviewed;         235 AA.
AC   P20490;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=High affinity immunoglobulin epsilon receptor subunit beta;
DE            Short=FcERI;
DE   AltName: Full=Fc epsilon receptor I beta-chain;
DE   AltName: Full=IgE Fc receptor subunit beta;
DE   AltName: Full=Membrane-spanning 4-domains subfamily A member 2;
GN   Name=Ms4a2; Synonyms=Fce1b, Fcer1b, Ms4a1;
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 [GENOMIC DNA].
RC   STRAIN=129;
RA   Hiraoka S., Watanabe M., Takagaki Y., Fujita-Suzuki K., Shinohara N.,
RA   Okumura K., Ra C.;
RT   "The genomic structure of the allergy associated Fc receptor beta subunit
RT   and its high content of SINEs.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION, AND INTERACTION WITH LYN.
RX   PubMed=16272347; DOI=10.4049/jimmunol.175.10.6885;
RA   Xiao W., Nishimoto H., Hong H., Kitaura J., Nunomura S., Maeda-Yamamoto M.,
RA   Kawakami Y., Lowell C.A., Ra C., Kawakami T.;
RT   "Positive and negative regulation of mast cell activation by Lyn via the
RT   FcepsilonRI.";
RL   J. Immunol. 175:6885-6892(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210; TYR-216; SER-217 AND
RP   TYR-220, AND 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   [5]
RP   FUNCTION, AND INTERACTION WITH FES/FPS.
RX   PubMed=19001085; DOI=10.1128/mcb.00904-08;
RA   McPherson V.A., Everingham S., Karisch R., Smith J.A., Udell C.M.,
RA   Zheng J., Jia Z., Craig A.W.;
RT   "Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase for
RT   coupling to the FcepsilonRI pathway in mast cells.";
RL   Mol. Cell. Biol. 29:389-401(2009).
CC   -!- FUNCTION: High affinity receptor that binds to the Fc region of
CC       immunoglobulins epsilon. Aggregation of FCER1 by multivalent antigens
CC       is required for the full mast cell response, including the release of
CC       preformed mediators (such as histamine) by degranulation and de novo
CC       production of lipid mediators and cytokines. Also mediates the
CC       secretion of important lymphokines. Binding of allergen to receptor-
CC       bound IgE leads to cell activation and the release of mediators
CC       responsible for the manifestations of allergy.
CC       {ECO:0000269|PubMed:19001085}.
CC   -!- SUBUNIT: Tetramer of an alpha chain, a beta chain, and two disulfide
CC       linked gamma chains. Binds LILRB1. Interacts with FGR (By similarity).
CC       Interacts with FGR and FES/FPS. Interacts with LYN. {ECO:0000250,
CC       ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:19001085}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated on tyrosine residues by LYN.
CC       {ECO:0000269|PubMed:16272347}.
CC   -!- SIMILARITY: Belongs to the MS4A family. {ECO:0000305}.
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DR   EMBL; J05019; AAA37601.1; -; mRNA.
DR   EMBL; AB033617; BAA94839.1; -; Genomic_DNA.
DR   CCDS; CCDS29604.1; -.
DR   PIR; B34342; B34342.
DR   RefSeq; NP_038544.1; NM_013516.2.
DR   AlphaFoldDB; P20490; -.
DR   SMR; P20490; -.
DR   BioGRID; 199615; 2.
DR   STRING; 10090.ENSMUSP00000127373; -.
DR   iPTMnet; P20490; -.
DR   PhosphoSitePlus; P20490; -.
DR   PaxDb; 10090-ENSMUSP00000127373; -.
DR   Antibodypedia; 27859; 84 antibodies from 16 providers.
DR   DNASU; 14126; -.
DR   Ensembl; ENSMUST00000164792.8; ENSMUSP00000127373.2; ENSMUSG00000024680.13.
DR   GeneID; 14126; -.
DR   KEGG; mmu:14126; -.
DR   UCSC; uc008gsn.2; mouse.
DR   AGR; MGI:95495; -.
DR   CTD; 2206; -.
DR   MGI; MGI:95495; Ms4a2.
DR   VEuPathDB; HostDB:ENSMUSG00000024680; -.
DR   eggNOG; ENOG502TM6F; Eukaryota.
DR   GeneTree; ENSGT00940000161985; -.
DR   InParanoid; P20490; -.
DR   OMA; AYIYNCQ; -.
DR   OrthoDB; 5264412at2759; -.
DR   PhylomeDB; P20490; -.
DR   TreeFam; TF335157; -.
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   BioGRID-ORCS; 14126; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Ms4a1; mouse.
DR   PRO; PR:P20490; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P20490; Protein.
DR   Bgee; ENSMUSG00000024680; Expressed in renal corpuscle and 36 other cell types or tissues.
DR   ExpressionAtlas; P20490; baseline and differential.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0032998; C:Fc-epsilon receptor I complex; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR   GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; IEA:GOC.
DR   GO; GO:0006955; P:immune response; ISO:MGI.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:MGI.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
DR   InterPro; IPR007237; CD20-like.
DR   InterPro; IPR030417; MS4A.
DR   PANTHER; PTHR23320:SF66; HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR SUBUNIT BETA; 1.
DR   PANTHER; PTHR23320; MEMBRANE-SPANNING 4-DOMAINS SUBFAMILY A MS4A -RELATED; 1.
DR   Pfam; PF04103; CD20; 1.
DR   Genevisible; P20490; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; IgE-binding protein; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..235
FT                   /note="High affinity immunoglobulin epsilon receptor
FT                   subunit beta"
FT                   /id="PRO_0000158630"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         210
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         216
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         220
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
SQ   SEQUENCE   235 AA;  25963 MW;  1C2D6BF195738168 CRC64;
     MDTENRSRAD LALPNPQESS SAPDIELLEA SPAKAAPPKQ TWRTFLKKEL EFLGATQILV
     GLICLCFGTI VCSVLYVSDF DEEVLLLYKL GYPFWGAVLF VLSGFLSIIS ERKNTLYLVR
     GSLGANIVSS IAAGTGIAML ILNLTNNFAY MNNCKNVTED DGCFVASFTT ELVLMMLFLT
     ILAFCSAVLF TIYRIGQELE SKKVPDDRLY EELNVYSPIY SELEDKGETS SPVDS
//