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Database: UniProt
Entry: IGHE_MOUSE
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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
//
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