IGHE_HUMAN
ID IGHE_HUMAN Reviewed; 428 AA.
AC P01854;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Immunoglobulin heavy constant epsilon {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.9};
DE AltName: Full=Ig epsilon chain C region {ECO:0000305};
DE AltName: Full=Ig epsilon chain C region ND {ECO:0000305|Ref.1};
GN Name=IGHE {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.9};
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.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-359.
RX PubMed=6288268; DOI=10.1016/0092-8674(82)90185-4;
RA Max E.E., Battey J., Ney R., Kirsch I.R., Leder P.;
RT "Duplication and deletion in the human immunoglobulin epsilon genes.";
RL Cell 29:691-699(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHE*02).
RX PubMed=6234164; DOI=10.1002/j.1460-2075.1982.tb01223.x;
RA Flanagan J.G., Rabbitts T.H.;
RT "The sequence of a human immunoglobulin epsilon heavy chain constant region
RT gene, and evidence for three non-allelic genes.";
RL EMBO J. 1:655-660(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHE*01), AND VARIANT
RP CYS-43.
RX PubMed=6327276; DOI=10.1002/j.1460-2075.1982.tb01352.x;
RA Ueda S., Nakai S., Nishida Y., Hisajima H., Honjo T.;
RT "Long terminal repeat-like elements flank a human immunoglobulin epsilon
RT pseudogene that lacks introns.";
RL EMBO J. 1:1539-1544(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHE*02).
RX PubMed=6300763; DOI=10.1093/nar/11.3.719;
RA Seno M., Kurokawa T., Ono Y., Onda H., Sasada R., Igarashi K., Kikuchi M.,
RA Sugino Y., Nishida Y., Honjo T.;
RT "Molecular cloning and nucleotide sequencing of human immunoglobulin
RT epsilon chain cDNA.";
RL Nucleic Acids Res. 11:719-726(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHE*04).
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40; 68-114 AND 427-428.
RX PubMed=6815656; DOI=10.1073/pnas.79.21.6661;
RA Kenten J.H., Molgaard H.V., Houghton M., Derbyshire R.B., Viney J.,
RA Bell L.O., Gould H.J.;
RT "Cloning and sequence determination of the gene for the human
RT immunoglobulin epsilon chain expressed in a myeloma cell line.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6661-6665(1982).
RN [8]
RP NOMENCLATURE.
RX PubMed=11340299; DOI=10.1159/000049189;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin heavy (IGH) genes.";
RL Exp. Clin. Immunogenet. 18:100-116(2001).
RN [9]
RP NOMENCLATURE.
RA Lefranc M.P., Lefranc G.;
RT "The Immunoglobulin FactsBook.";
RL (In) Lefranc M.P., Lefranc G. (eds.);
RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN [10]
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 [11]
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 [12]
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).
RN [13]
RP 3D-STRUCTURE MODELING.
RX PubMed=3796618; DOI=10.1016/0161-5890(86)90005-2;
RA Padlan E.A., Davies D.R.;
RT "A model of the Fc of immunoglobulin E.";
RL Mol. Immunol. 23:1063-1075(1986).
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 (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:17576170, PubMed:20176268).
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 -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGHE*04. {ECO:0000305}.
CC -!- CAUTION: For an example of a full-length immunoglobulin epsilon heavy
CC chain see AC P0DOX4.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59395.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB59424.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L00022; AAB59424.1; ALT_INIT; Genomic_DNA.
DR EMBL; J00222; AAB59395.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL928742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A22771; EHHU.
DR PDB; 1F6A; X-ray; 3.50 A; B/D=211-428.
DR PDB; 1FP5; X-ray; 2.30 A; A=211-428.
DR PDB; 1G84; NMR; -; A=106-208.
DR PDB; 1O0V; X-ray; 2.60 A; A/B=104-427.
DR PDB; 2WQR; X-ray; 1.90 A; A/B=105-427.
DR PDB; 2Y7Q; X-ray; 3.40 A; B/D=104-428.
DR PDB; 3H9Y; X-ray; 2.23 A; A/B/E=209-428.
DR PDB; 3H9Z; X-ray; 2.45 A; A/B/C/D=209-428.
DR PDB; 3HA0; X-ray; 2.80 A; A/B/C/D/E/F=209-428.
DR PDB; 4EZM; X-ray; 3.10 A; A/B/C/D/E/F=209-428.
DR PDB; 4GKO; X-ray; 3.30 A; A/B/C/D/E/F=209-428.
DR PDB; 4GRG; X-ray; 4.24 A; C/D=210-428.
DR PDB; 4GT7; X-ray; 2.61 A; A/B/C/D=210-426.
DR PDB; 4J4P; X-ray; 2.91 A; A/B=105-427.
DR PDB; 4KI1; X-ray; 3.20 A; A/B/C/D=209-428.
DR PDB; 5ANM; X-ray; 2.85 A; E/F/G=211-428.
DR PDB; 5HYS; X-ray; 2.50 A; G/I/J/K=209-428.
DR PDB; 5LGJ; X-ray; 2.60 A; A=108-426, B=108-427.
DR PDB; 5LGK; X-ray; 3.50 A; A/B/C/D=114-421.
DR PDB; 5MOI; X-ray; 2.20 A; A/B/C/D/E/F=209-428.
DR PDB; 5MOJ; X-ray; 2.26 A; A/B=209-428.
DR PDB; 5MOK; X-ray; 2.00 A; A/B/C/D=209-428.
DR PDB; 5MOL; X-ray; 1.75 A; A/B=104-428.
DR PDB; 5NQW; X-ray; 3.40 A; A/B=215-426.
DR PDB; 6EYO; X-ray; 3.70 A; A/B=104-428.
DR PDB; 6UQR; X-ray; 3.65 A; B/D=209-426.
DR PDB; 7MXI; X-ray; 2.80 A; A/B=209-426.
DR PDB; 7SHT; EM; 7.29 A; B/D=109-428.
DR PDB; 7SHU; X-ray; 2.75 A; A/B=209-426.
DR PDB; 7SHY; X-ray; 3.00 A; A/B/G/H=209-426.
DR PDB; 7SHZ; X-ray; 3.00 A; A/B/G/H=209-426.
DR PDB; 7SI0; X-ray; 3.00 A; A/B/G/H=209-426.
DR PDBsum; 1F6A; -.
DR PDBsum; 1FP5; -.
DR PDBsum; 1G84; -.
DR PDBsum; 1O0V; -.
DR PDBsum; 2WQR; -.
DR PDBsum; 2Y7Q; -.
DR PDBsum; 3H9Y; -.
DR PDBsum; 3H9Z; -.
DR PDBsum; 3HA0; -.
DR PDBsum; 4EZM; -.
DR PDBsum; 4GKO; -.
DR PDBsum; 4GRG; -.
DR PDBsum; 4GT7; -.
DR PDBsum; 4J4P; -.
DR PDBsum; 4KI1; -.
DR PDBsum; 5ANM; -.
DR PDBsum; 5HYS; -.
DR PDBsum; 5LGJ; -.
DR PDBsum; 5LGK; -.
DR PDBsum; 5MOI; -.
DR PDBsum; 5MOJ; -.
DR PDBsum; 5MOK; -.
DR PDBsum; 5MOL; -.
DR PDBsum; 5NQW; -.
DR PDBsum; 6EYO; -.
DR PDBsum; 6UQR; -.
DR PDBsum; 7MXI; -.
DR PDBsum; 7SHT; -.
DR PDBsum; 7SHU; -.
DR PDBsum; 7SHY; -.
DR PDBsum; 7SHZ; -.
DR PDBsum; 7SI0; -.
DR AlphaFoldDB; P01854; -.
DR SMR; P01854; -.
DR ComplexPortal; CPX-6969; IgE - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6970; IgE - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6971; IgE - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6972; IgE - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6973; IgE - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6974; IgE - Ig lambda 7 immunoglobulin complex, constant regions.
DR DIP; DIP-6167N; -.
DR ChEMBL; CHEMBL1834; -.
DR DrugBank; DB11856; Ligelizumab.
DR DrugCentral; P01854; -.
DR GuidetoPHARMACOLOGY; 2741; -.
DR IMGT_GENE-DB; IGHE; -.
DR GlyConnect; 2970; 39 N-Linked glycans.
DR GlyConnect; 2971; 38 N-Linked glycans.
DR GlyConnect; 765; 104 N-Linked glycans (7 sites).
DR GlyGen; P01854; 8 sites, 81 N-linked glycans (8 sites).
DR iPTMnet; P01854; -.
DR PhosphoSitePlus; P01854; -.
DR BioMuta; IGHE; -.
DR DMDM; 119512; -.
DR jPOST; P01854; -.
DR MassIVE; P01854; -.
DR PeptideAtlas; P01854; -.
DR PRIDE; P01854; -.
DR ProteomicsDB; 51493; -.
DR ABCD; P01854; 81 sequenced antibodies.
DR Ensembl; ENST00000390541.2; ENSP00000374983.2; ENSG00000211891.6.
DR Ensembl; ENST00000610670.2; ENSP00000481089.1; ENSG00000276192.2.
DR UCSC; uc059gcp.1; human.
DR GeneCards; IGHE; -.
DR HGNC; HGNC:5522; IGHE.
DR HPA; ENSG00000211891; Tissue enhanced (intestine, lymphoid tissue, thyroid gland).
DR MIM; 147180; gene.
DR neXtProt; NX_P01854; -.
DR OpenTargets; ENSG00000211891; -.
DR VEuPathDB; HostDB:ENSG00000211891; -.
DR GeneTree; ENSGT00940000163076; -.
DR HOGENOM; CLU_030625_0_2_1; -.
DR InParanoid; P01854; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P01854; -.
DR TreeFam; TF334176; -.
DR PathwayCommons; P01854; -.
DR Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P01854; -.
DR EvolutionaryTrace; P01854; -.
DR Pharos; P01854; Tclin.
DR PRO; PR:P01854; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01854; protein.
DR Bgee; ENSG00000211891; Expressed in bone marrow cell and 71 other tissues.
DR ExpressionAtlas; P01854; baseline and differential.
DR Genevisible; P01854; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IC:ComplexPortal.
DR GO; GO:0071742; C:IgE immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
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:0006955; P:immune response; NAS:UniProtKB.
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 Pfam; PF07654; C1-set; 4.
DR SMART; SM00407; IGc1; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Secreted.
FT CHAIN <1..428
FT /note="Immunoglobulin heavy constant epsilon"
FT /id="PRO_0000153574"
FT DOMAIN 6..103
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 112..210
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 214..318
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 324..423
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6234164"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6234164"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6234164"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6234164"
FT DISULFID 14
FT /note="Interchain (with a light chain)"
FT DISULFID 15..105
FT DISULFID 29..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 121
FT /note="Interchain (with a heavy chain)"
FT DISULFID 135..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 209
FT /note="Interchain (with a heavy chain)"
FT DISULFID 239..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 345..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 43
FT /note="W -> C (in IMGT allele IGHE*01)"
FT /evidence="ECO:0000269|PubMed:6327276"
FT /id="VAR_044229"
FT VARIANT 359
FT /note="W -> L (likely benign variant)"
FT /evidence="ECO:0000269|PubMed:6288268"
FT /id="VAR_003885"
FT CONFLICT 1..5
FT /note="ASTQS -> GAWTL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="G -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166..168
FT /note="TQE -> ESQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Q -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="E -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="E -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..399
FT /note="EQ -> QE (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1G84"
FT STRAND 129..140
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5LGJ"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:5MOL"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:5MOL"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:5MOL"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:5MOL"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3H9Y"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:5MOL"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:1FP5"
FT STRAND 340..353
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:5MOL"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 380..393
FT /evidence="ECO:0007829|PDB:5MOL"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1F6A"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:5MOL"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:5MOL"
SQ SEQUENCE 428 AA; 47019 MW; 25C4CA072AA558A0 CRC64;
ASTQSPSVFP LTRCCKNIPS NATSVTLGCL ATGYFPEPVM VTWDTGSLNG TTMTLPATTL
TLSGHYATIS LLTVSGAWAK QMFTCRVAHT PSSTDWVDNK TFSVCSRDFT PPTVKILQSS
CDGGGHFPPT IQLLCLVSGY TPGTINITWL EDGQVMDVDL STASTTQEGE LASTQSELTL
SQKHWLSDRT YTCQVTYQGH TFEDSTKKCA DSNPRGVSAY LSRPSPFDLF IRKSPTITCL
VVDLAPSKGT VNLTWSRASG KPVNHSTRKE EKQRNGTLTV TSTLPVGTRD WIEGETYQCR
VTHPHLPRAL MRSTTKTSGP RAAPEVYAFA TPEWPGSRDK RTLACLIQNF MPEDISVQWL
HNEVQLPDAR HSTTQPRKTK GSGFFVFSRL EVTRAEWEQK DEFICRAVHE AASPSQTVQR
AVSVNPGK
