ID FCER2_MOUSE Reviewed; 331 AA. AC P20693; Q61556; Q61557; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 11-NOV-2015, entry version 147. DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor; DE AltName: Full=Fc-epsilon-RII; DE AltName: Full=Lymphocyte IgE receptor; DE AltName: CD_antigen=CD23; GN Name=Fcer2; Synonyms=Fcer2a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2529542; DOI=10.1073/pnas.86.19.7566; RA Bettler B., Hofstetter H., Rao M., Yokoyama W.M., Kilchherr F., RA Conrad D.H.; RT "Molecular structure and expression of the murine lymphocyte low- RT affinity receptor for IgE (Fc epsilon RII)."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7566-7570(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2137845; RA Gollnick S.O., Trounstine M.L., Yamashita L.C., Kehry M.R., RA Moore K.W.; RT "Isolation, characterization, and expression of cDNA clones encoding RT the mouse Fc receptor for IgE (Fc epsilon RII)1."; RL J. Immunol. 144:1974-1982(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RC STRAIN=DBA/2J; RX PubMed=8086828; RA Kondo H., Ichikawa Y., Nakamura K., Tsuchiya S.; RT "Cloning of cDNAs for new subtypes of murine low-affinity Fc receptor RT for IgE (Fc epsilon RII/CD23)."; RL Int. Arch. Allergy Immunol. 105:38-48(1994). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [5] RP 3D-STRUCTURE MODELING OF LECTIN DOMAIN. RX PubMed=8142907; RA Padlan E.A., Helm B.A.; RT "Modeling of the lectin-homology domains of the human and murine low- RT affinity Fc epsilon receptor (Fc epsilon RII/CD23)."; RL Receptor 3:325-341(1993). CC -!- FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and CC CR2/CD21. Has essential roles in the regulation of IgE production CC and in the differentiation of B-cells (it is a B-cell-specific CC antigen). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass CC type II membrane protein {ECO:0000250}. Cell membrane CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=A; CC IsoId=P20693-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=P20693-2; Sequence=VSP_003058; CC Name=3; Synonyms=C; CC IsoId=P20693-3; Sequence=VSP_003059; CC -!- PTM: N- and O-glycosylated. {ECO:0000250}. CC -!- MISCELLANEOUS: There are two kinds of Fc receptors for IgE, which CC differ in both structure and function: high affinity receptors on CC basophils and mast cells and low affinity receptors on lymphocytes CC and monocytes. CC -!- SIMILARITY: Contains 1 C-type lectin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00040}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=CD23; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_222"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M99371; AAA74898.1; -; mRNA. DR EMBL; M34163; AAA37603.1; -; mRNA. DR EMBL; X64223; CAA45532.1; -; mRNA. DR EMBL; X64224; CAA45533.1; -; mRNA. DR CCDS; CCDS22071.1; -. [P20693-1] DR PIR; A43518; LNMSER. DR RefSeq; NP_001240666.1; NM_001253737.1. [P20693-2] DR RefSeq; NP_001240668.1; NM_001253739.1. [P20693-3] DR RefSeq; NP_001240672.1; NM_001253743.1. DR RefSeq; NP_001240674.1; NM_001253745.1. DR RefSeq; NP_001240675.1; NM_001253746.1. DR RefSeq; NP_001240676.1; NM_001253747.1. DR RefSeq; NP_038545.1; NM_013517.4. [P20693-1] DR UniGene; Mm.1233; -. DR PDB; 1HLJ; Model; -; A=196-308. DR PDBsum; 1HLJ; -. DR ProteinModelPortal; P20693; -. DR SMR; P20693; 147-311. DR STRING; 10090.ENSMUSP00000005678; -. DR PhosphoSite; P20693; -. DR PaxDb; P20693; -. DR PRIDE; P20693; -. DR Ensembl; ENSMUST00000005678; ENSMUSP00000005678; ENSMUSG00000005540. [P20693-1] DR GeneID; 14128; -. DR KEGG; mmu:14128; -. DR UCSC; uc009ksl.1; mouse. [P20693-3] DR UCSC; uc009ksm.1; mouse. [P20693-2] DR UCSC; uc009ksn.1; mouse. [P20693-1] DR CTD; 14128; -. DR MGI; MGI:95497; Fcer2a. DR eggNOG; ENOG410IS34; Eukaryota. DR eggNOG; ENOG410XZ77; LUCA. DR GeneTree; ENSGT00760000118924; -. DR HOGENOM; HOG000089951; -. DR HOVERGEN; HBG051599; -. DR InParanoid; P20693; -. DR KO; K06468; -. DR OMA; GQWNDAF; -. DR OrthoDB; EOG7FV3QQ; -. DR PhylomeDB; P20693; -. DR TreeFam; TF333341; -. DR NextBio; 285218; -. DR PRO; PR:P20693; -. DR Proteomes; UP000000589; Chromosome 8. DR Bgee; P20693; -. DR Genevisible; P20693; MM. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI. DR GO; GO:0051712; P:positive regulation of killing of cells of other organism; ISO:MGI. DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:MGI. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR001304; C-type_lectin. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR018378; C-type_lectin_CS. DR InterPro; IPR016187; C-type_lectin_fold. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; KW Complete proteome; Disulfide bond; Glycoprotein; IgE-binding protein; KW Lectin; Lipoprotein; Membrane; Metal-binding; Palmitate; Receptor; KW Reference proteome; Repeat; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1 331 Low affinity immunoglobulin epsilon Fc FT receptor. FT /FTId=PRO_0000046640. FT TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 24 49 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 50 331 Extracellular. {ECO:0000255}. FT REPEAT 71 91 FT REPEAT 92 112 FT REPEAT 113 133 FT DOMAIN 185 298 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT METAL 272 272 Calcium. {ECO:0000250}. FT METAL 292 292 Calcium. {ECO:0000250}. FT METAL 293 293 Calcium. {ECO:0000250}. FT LIPID 17 17 S-palmitoyl cysteine. {ECO:0000250}. FT LIPID 18 18 S-palmitoyl cysteine. {ECO:0000250}. FT CARBOHYD 65 65 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 114 114 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 183 311 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 186 197 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 214 305 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT DISULFID 282 296 {ECO:0000255|PROSITE-ProRule:PRU00040}. FT VAR_SEQ 1 7 MEENEYS -> MNSQNQ (in isoform 2). FT {ECO:0000303|PubMed:8086828}. FT /FTId=VSP_003058. FT VAR_SEQ 1 7 MEENEYS -> MDTHHT (in isoform 3). FT {ECO:0000303|PubMed:8086828}. FT /FTId=VSP_003059. SQ SEQUENCE 331 AA; 37648 MW; B8C6D65F34ACCDB2 CRC64; MEENEYSGYW EPPRKRCCCA RRGTQLMLVG LLSTAMWAGL LALLLLWHWE TEKNLKQLGD TAIQNVSHVT KDLQKFQSNQ LAQKSQVVQM SQNLQELQAE QKQMKAQDSR LSQNLTGLQE DLRNAQSQNS KLSQNLNRLQ DDLVNIKSLG LNEKRTASDS LEKLQEEVAK LWIEILISKG TACNICPKNW LHFQQKCYYF GKGSKQWIQA RFACSDLQGR LVSIHSQKEQ DFLMQHINKK DSWIGLQDLN MEGEFVWSDG SPVGYSNWNP GEPNNGGQGE DCVMMRGSGQ WNDAFCRSYL DAWVCEQLAT CEISAPLASV TPTRPTPKSE P //