FCERB_RAT
ID FCERB_RAT Reviewed; 243 AA.
AC P13386;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 151.
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;
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 [MRNA], AND PROTEIN SEQUENCE OF 11-29; 37-43 AND
RP 217-243.
RX PubMed=2970642; DOI=10.1073/pnas.85.17.6483;
RA Kinet J.-P., Blank U., Ra C., White K., Metzger H., Kochan J.;
RT "Isolation and characterization of cDNAs coding for the beta subunit of the
RT high-affinity receptor for immunoglobulin E.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6483-6487(1988).
RN [2]
RP INTERACTION WITH FGR, AND SUBCELLULAR LOCATION.
RX PubMed=21746961; DOI=10.4049/jimmunol.1100296;
RA Lee J.H., Kim J.W., Kim do K., Kim H.S., Park H.J., Park D.K., Kim A.R.,
RA Kim B., Beaven M.A., Park K.L., Kim Y.M., Choi W.S.;
RT "The Src family kinase Fgr is critical for activation of mast cells and
RT IgE-mediated anaphylaxis in mice.";
RL J. Immunol. 187:1807-1815(2011).
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 -!- SUBUNIT: Tetramer of an alpha chain, a beta chain, and two disulfide
CC linked gamma chains. Binds LILRB1. Interacts with FES/FPS and LYN (By
CC similarity). Interacts with FGR. {ECO:0000250,
CC ECO:0000269|PubMed:21746961}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21746961}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:21746961}.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MS4A family. {ECO:0000305}.
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DR EMBL; M22923; AAA41149.1; -; mRNA.
DR PIR; A31231; A31231.
DR RefSeq; NP_036977.1; NM_012845.1.
DR AlphaFoldDB; P13386; -.
DR BioGRID; 247355; 4.
DR STRING; 10116.ENSRNOP00000028491; -.
DR iPTMnet; P13386; -.
DR PhosphoSitePlus; P13386; -.
DR PaxDb; P13386; -.
DR PRIDE; P13386; -.
DR ABCD; P13386; 7 sequenced antibodies.
DR GeneID; 25316; -.
DR KEGG; rno:25316; -.
DR UCSC; RGD:2598; rat.
DR CTD; 2206; -.
DR RGD; 2598; Ms4a2.
DR eggNOG; ENOG502TM6F; Eukaryota.
DR HOGENOM; CLU_093202_0_0_1; -.
DR InParanoid; P13386; -.
DR OrthoDB; 1155741at2759; -.
DR PhylomeDB; P13386; -.
DR TreeFam; TF335157; -.
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 PRO; PR:P13386; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P13386; RN.
DR GO; GO:0005768; C:endosome; IDA: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:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0042169; F:SH2 domain binding; IDA:RGD.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IMP:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:RGD.
DR GO; GO:0007165; P:signal transduction; IMP:RGD.
DR InterPro; IPR007237; CD20-like.
DR InterPro; IPR030417; MS4A.
DR InterPro; IPR030420; MS4A2.
DR PANTHER; PTHR23320; PTHR23320; 1.
DR PANTHER; PTHR23320:SF66; PTHR23320:SF66; 1.
DR Pfam; PF04103; CD20; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; IgE-binding protein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..243
FT /note="High affinity immunoglobulin epsilon receptor
FT subunit beta"
FT /id="PRO_0000158631"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20490"
FT MOD_RES 224
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20490"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20490"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20490"
SQ SEQUENCE 243 AA; 26731 MW; 471DFA59B6688E5D CRC64;
MDTENKSRAD LALPNPQESP SAPDIELLEA SPPAKALPEK PASPPPQQTW QSFLKKELEF
LGVTQVLVGL ICLCFGTVVC STLQTSDFDD EVLLLYRAGY PFWGAVLFVL SGFLSIMSER
KNTLYLVRGS LGANIVSSIA AGLGIAILIL NLSNNSAYMN YCKDITEDDG CFVTSFITEL
VLMLLFLTIL AFCSAVLLII YRIGQEFERS KVPDDRLYEE LHVYSPIYSA LEDTREASAP
VVS
