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   25-MAY-2022, entry version 110.
DE   RecName: Full=Ig epsilon chain C region;
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).
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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   STRING; 10090.ENSMUSP00000118012; -.
DR   GlyGen; P06336; 9 sites.
DR   MaxQB; P06336; -.
DR   PaxDb; P06336; -.
DR   PRIDE; P06336; -.
DR   MGI; MGI:2685746; Gm900.
DR   eggNOG; ENOG502R54U; Eukaryota.
DR   InParanoid; P06336; -.
DR   PRO; PR:P06336; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P06336; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR   GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR   GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR   GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR   GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR   GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 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   Pfam; PF07654; C1-set; 3.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00407; IGc1; 4.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS00290; IG_MHC; 3.
PE   4: Predicted;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome.
FT   CHAIN           <1..421
FT                   /note="Ig epsilon chain C region"
FT                   /id="PRO_0000153575"
FT   REGION          1..90
FT                   /note="CH1"
FT   REGION          91..197
FT                   /note="CH2"
FT   REGION          198..304
FT                   /note="CH3"
FT   REGION          305..421
FT                   /note="CH4"
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