IGE_HUMAN
ID IGE_HUMAN Reviewed; 547 AA.
AC P0DOX4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Immunoglobulin epsilon heavy chain {ECO:0000305};
DE AltName: Full=Immunoglobulin epsilon heavy chain ND {ECO:0000305|Ref.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-145; ASN-173; ASN-219; ASN-265; ASN-371; ASN-383 AND
RP ASN-394.
RA Bennich H.H., Johansson S.G.O., von Bahr-Lindstroem H.;
RL (In) Bach M.K. (eds.);
RL Immediate hypersensitivity: modern concepts and developments, pp.1-36,
RL Marcel Dekker, New York (1978).
RN [2]
RP REVIEW ON SOMATIC HYPERMUTATION.
RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA Teng G., Papavasiliou F.N.;
RT "Immunoglobulin somatic hypermutation.";
RL Annu. Rev. Genet. 41:107-120(2007).
RN [3]
RP REVIEW ON IMMUNOGLOBULINS.
RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA Schroeder H.W. Jr., Cavacini L.;
RT "Structure and function of immunoglobulins.";
RL J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN [4]
RP REVIEW ON FUNCTION.
RX PubMed=22158414; DOI=10.1038/nri3128;
RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT "Molecular programming of B cell memory.";
RL Nat. Rev. Immunol. 12:24-34(2012).
CC -!- FUNCTION: Immunoglobulins, also known as antibodies, are membrane-bound
CC or 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 (PubMed:22158414, PubMed:20176268). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:20176268, PubMed:17576170).
CC {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked.
CC {ECO:0000303|PubMed:20176268}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}. Cell membrane
CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- CAUTION: This sequence is an example of a full-length immunoglobulin
CC epsilon heavy chain. {ECO:0000305}.
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DR AlphaFoldDB; P0DOX4; -.
DR SMR; P0DOX4; -.
DR iPTMnet; P0DOX4; -.
DR PhosphoSitePlus; P0DOX4; -.
DR jPOST; P0DOX4; -.
DR PRIDE; P0DOX4; -.
DR Pharos; P0DOX4; Tdark.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 5.
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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 4.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00407; IGc1; 4.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
DR PROSITE; PS00290; IG_MHC; 3.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Pyrrolidone carboxylic acid; Repeat;
KW Secreted.
FT CHAIN 1..547
FT /note="Immunoglobulin epsilon heavy chain"
FT /id="PRO_0000439285"
FT DOMAIN 1..120
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 130..223
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 232..329
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 333..437
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 443..542
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..124
FT /note="Variable (V) domain, involved in antigen
FT recognition"
FT /evidence="ECO:0000305"
FT REGION 125..547
FT /note="Constant (C) domain"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 22..96
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 138
FT /note="Interchain (with a light chain)"
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 139..225
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 153..207
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 241
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 254..312
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 328
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 358..418
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 464..524
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 547 AA; 60323 MW; 865E343B2D159BA6 CRC64;
QVQLVQSGAE VRKPGASVRV SCKASGYTFI DSYVGWIRQA PGHGLEWIHW INPNSGGTNY
APRFQGRVTM TRDASFSTAY MDLRSLRSDD SAVFYCAKSD PFWSDYNFDY SSSEEGTEVT
YTVSGAWTLP SVFPLTRCCK NIPSNATSVT LGCLATGYFP EPVMVTWDTG SLNGTTLPAT
TLTLSGHYAT ISLLTVSGAW AKQMFTCRVA HTPSSTVDNK TFSVCSRDFT PPTVKILQSS
CDGLGHFPPT IQLCLVSGYT PGTINITWLE DGQVMDVDLS TASTESQGEL ASTESQLTLS
QKHWLSDRTY TCQVTYQGHT FQDSTKKCAD SNPRGVSAYL SRPSPFDLFI RKSPTITCLV
VDLAPSKGTV NLTWSRASGK PVNHSTRKEE KQRNGTLTVT STLPVGTRDW IEGETYQCRV
THPHLPRALM RSTTKTSGPR AAPEVYAFAT PEWPGSRDKR TLACLIQNFM PEDISVQWLH
NEVQLPDARH STTQPRKTKG SGFFVFSRLE VTRAEWQEKD EFICRAVHEA ASPSQTVQRA
VSVNPGK
