ID IGHE_MOUSE Reviewed; 421 AA.
AC P06336; P01856;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 24-JAN-2024, entry version 118.
DE RecName: Full=Immunoglobulin heavy constant epsilon;
DE AltName: Full=Ig epsilon chain C region;
GN Name=IGHE {ECO:0000312|MGI:MGI:2685746};
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 [GENOMIC DNA].
RX PubMed=6329728; DOI=10.1002/j.1460-2075.1982.tb01306.x;
RA Ishida N., Ueda S., Hayashida H., Miyata T., Honjo T.;
RT "The nucleotide sequence of the mouse immunoglobulin epsilon gene:
RT comparison with the human epsilon gene sequence.";
RL EMBO J. 1:1117-1123(1982).
RN [2]
RP SEQUENCE REVISION.
RA Honjo T.;
RL Submitted (APR-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-421.
RX PubMed=6818553; DOI=10.1073/pnas.79.24.7852;
RA Liu F.-T., Albrandt K., Sutcliffe J.G., Katz D.H.;
RT "Cloning and nucleotide sequence of mouse immunoglobulin epsilon chain
RT cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7852-7856(1982).
CC -!- FUNCTION: Constant region of immunoglobulin heavy chains.
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens. The antigen binding site is formed by the variable domain of
CC one heavy chain, together with that of its associated light chain.
CC Thus, each immunoglobulin has two antigen binding sites with remarkable
CC affinity for a particular antigen. The variable domains are assembled
CC by a process called V-(D)-J rearrangement and can then be subjected to
CC somatic hypermutations which, after exposure to antigen and selection,
CC allow affinity maturation for a particular antigen.
CC {ECO:0000250|UniProtKB:P01854}.
CC -!- SUBUNIT: The basic structural unit consists of two identical heavy
CC chains and two identical light chains; disulfide-linked. N-terminal
CC variable regions of the heavy and light chains form the antigen binding
CC sites, whereas the C-terminal constant regions of the heavy chains
CC interact with immune receptors to mediate effector functions.
CC {ECO:0000250|UniProtKB:P01854}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01854}. Cell
CC membrane {ECO:0000250|UniProtKB:P01854}.
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DR EMBL; X01857; CAA25977.1; -; Genomic_DNA.
DR EMBL; X01857; CAA25978.1; -; Genomic_DNA.
DR PIR; A02144; EHMS.
DR PIR; A02145; EHMSS.
DR AlphaFoldDB; P06336; -.
DR SMR; P06336; -.
DR GlyGen; P06336; 9 sites.
DR MaxQB; P06336; -.
DR PaxDb; 10090-ENSMUSP00000118012; -.
DR AGR; MGI:2685746; -.
DR MGI; MGI:2685746; Ighe.
DR eggNOG; ENOG502R54U; Eukaryota.
DR InParanoid; P06336; -.
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 PRO; PR:P06336; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P06336; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0071744; C:IgE B cell receptor complex; ISO:MGI.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; ISO:MGI.
DR GO; GO:0090716; P:adaptive immune memory response; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; ISO:MGI.
DR GO; GO:0002450; P:B cell antigen processing and presentation; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; ISO:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0043308; P:eosinophil degranulation; ISO:MGI.
DR GO; GO:0160006; P:Fc receptor-mediated immune complex endocytosis; ISO:MGI.
DR GO; GO:0042116; P:macrophage activation; ISO:MGI.
DR GO; GO:0030225; P:macrophage differentiation; ISO:MGI.
DR GO; GO:0043303; P:mast cell degranulation; ISO:MGI.
DR GO; GO:0090720; P:primary adaptive immune response; ISO:MGI.
DR GO; GO:0042092; P:type 2 immune response; ISO:MGI.
DR GO; GO:0016068; P:type I hypersensitivity; ISO:MGI.
DR CDD; cd05847; IgC1_CH2_IgE; 1.
DR CDD; cd07696; IgC1_CH3_IgAEM_CH2_IgG; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR23411:SF30; IMMUNOGLOBULIN HEAVY CONSTANT EPSILON; 1.
DR PANTHER; PTHR23411; TAPASIN; 1.
DR Pfam; PF07654; C1-set; 3.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00407; IGc1; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 3.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Secreted.
FT CHAIN <1..421
FT /note="Immunoglobulin heavy constant epsilon"
FT /id="PRO_0000153575"
FT DOMAIN 5..97
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 99..184
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 201..301
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 310..410
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 121..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 226..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 330..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 421 AA; 47321 MW; 8F909E1F30A06B47 CRC64;
SIRNPQLYPL KPCKGTASMT LGCLVKDYFP NPVTVTWYSD SLNMSTVNFP ALGSELKVTT
SQVTSWGKSA KNFTCHVTHP PSFNESRTIL VRPVNITEPT LELLHSSCDP NAFHSTIQLY
CFIYGHILND VSVSWLMDDR EITDTLAQTV LIKEEGKLAS TCSKLNITEQ QWMSESTFTC
KVTSQGVDYL AHTRRCPDHE PRGVITYLIP PSPLDLYQNG APKLTCLVVD LESEKNVNVT
WNQEKKTSVS ASQWYTKHHN NATTSITSIL PVVAKDWIEG YGYQCIVDHP DFPKPIVRSI
TKTPGQRSAP EVYVFPPPEE ESEDKRTLTC LIQNFFPEDI SVQWLGDGKL ISNSQHSTTT
PLKSNGSNQG FFIFSRLEVA KTLWTQRKQF TCQVIHEALQ KPRKLEKTIS TSLGNTSLRP
S
//