IGHG3_HUMAN
ID IGHG3_HUMAN Reviewed; 377 AA.
AC P01860; A0A075B6N8; A2NU35;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Immunoglobulin heavy constant gamma 3 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.9};
DE AltName: Full=HDC;
DE AltName: Full=Heavy chain disease protein;
DE AltName: Full=Ig gamma-3 chain C region {ECO:0000305};
GN Name=IGHG3 {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 (VARIANT WIS), AND SUBUNIT.
RX PubMed=6774747; DOI=10.1021/bi00559a024;
RA Frangione B., Rosenwasser E., Prelli F., Franklin E.C.;
RT "Primary structure of human gamma 3 immunoglobulin deletion mutant: gamma 3
RT heavy-chain disease protein Wis.";
RL Biochemistry 19:4304-4308(1980).
RN [2]
RP SEQUENCE REVISION TO 146-376 (VARIANT WIS/VARIANT ZUC).
RX PubMed=402363; DOI=10.1016/s0021-9258(19)75181-3;
RA Michaelsen T.E., Frangione B., Franklin E.C.;
RT "Primary structure of the 'hinge' region of human IgG3. Probable
RT quadruplication of a 15-amino acid residue basic unit.";
RL J. Biol. Chem. 252:883-889(1977).
RN [3]
RP SEQUENCE REVISION TO 59-289 (VARIANT WIS/VARIANT ZUC).
RX PubMed=823945; DOI=10.1016/0006-291x(76)90741-5;
RA Wolfenstein-Todel C., Frangione B., Prelli F., Franklin E.C.;
RT "The amino acid sequence of 'heavy chain disease' protein ZUC. Structure of
RT the Fc fragment of immunoglobulin G3.";
RL Biochem. Biophys. Res. Commun. 71:907-914(1976).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHG3*01).
RX PubMed=3081877; DOI=10.1093/nar/14.4.1779;
RA Huck S., Fort P., Crawford D.H., Lefranc M.-P., Lefranc G.;
RT "Sequence of a human immunoglobulin gamma 3 heavy chain constant region
RT gene: comparison with the other human C gamma genes.";
RL Nucleic Acids Res. 14:1779-1789(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHG3*10).
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-59.
RX PubMed=6811139; DOI=10.1016/0092-8674(82)90183-0;
RA Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.;
RT "Structure of human immunoglobulin gamma genes: implications for evolution
RT of a gene family.";
RL Cell 29:671-679(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-377 (VARIANT OMM).
RX PubMed=6808505; DOI=10.1073/pnas.79.10.3260;
RA Alexander A., Steinmetz M., Barritault D., Frangione B., Franklin E.C.,
RA Hood L., Buxbaum J.N.;
RT "Gamma heavy chain disease in man: cDNA sequence supports partial gene
RT deletion model.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:3260-3264(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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
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 [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP GLYCOSYLATION AT THR-122; THR-137; THR-152; ASN-227 AND ASN-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26536155; DOI=10.1021/acs.analchem.5b02366;
RA Stavenhagen K., Plomp R., Wuhrer M.;
RT "Site-Specific Protein N- and O-Glycosylation Analysis by a C18-Porous
RT Graphitized Carbon-Liquid Chromatography-Electrospray Ionization Mass
RT Spectrometry Approach Using Pronase Treated Glycopeptides.";
RL Anal. Chem. 87:11691-11699(2015).
RN [17]
RP GLYCOSYLATION AT THR-122; THR-137 AND THR-152, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=25759508; DOI=10.1074/mcp.m114.047381;
RA Plomp R., Dekkers G., Rombouts Y., Visser R., Koeleman C.A.,
RA Kammeijer G.S., Jansen B.C., Rispens T., Hensbergen P.J., Vidarsson G.,
RA Wuhrer M.;
RT "Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).";
RL Mol. Cell. Proteomics 14:1373-1384(2015).
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 -!- PTM: N-linked glycans at Asn-322 are noncore fucosylated and the vast
CC majority are diantennary species with a bisecting GlcNAc. Among them
CC the most dominant glycans are HexNAc5Hex4, HexNAc5Hex5, and
CC HexNAc5Hex5Sia1. {ECO:0000269|PubMed:26536155}.
CC -!- PTM: N-linked glycans at Asn-227 are diantennary core fucosylated
CC structures without bisecting GlcNAc (HexNAc4Hex4Fuc1, HexNAc4Hex5Fuc1,
CC and HexNAc4Hex5Fuc1Sia1). {ECO:0000269|PubMed:26536155}.
CC -!- PTM: O-linked glycans are non-, mono- and disialylated core 1-type O-
CC glycans. {ECO:0000269|PubMed:25759508}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGHG3*10. {ECO:0000305}.
CC -!- CAUTION: For an example of a full-length immunoglobulin gamma heavy
CC chain see AC P0DOX5. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X03604; CAA27268.1; -; Genomic_DNA.
DR EMBL; AC244226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC246787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL122127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00231; AAA52805.1; ALT_INIT; mRNA.
DR PIR; A23511; A23511.
DR PIR; A90442; G3HUWI.
DR PDB; 4WWI; X-ray; 2.31 A; D/E/F=168-377.
DR PDB; 4ZNC; X-ray; 2.28 A; D/E/F=168-377.
DR PDB; 5M3V; X-ray; 1.97 A; A=286-377.
DR PDB; 5W38; X-ray; 1.80 A; A/B=155-377.
DR PDB; 6D58; X-ray; 2.39 A; A/B=164-377.
DR PDB; 6G1E; X-ray; 1.88 A; A=204-377.
DR PDBsum; 4WWI; -.
DR PDBsum; 4ZNC; -.
DR PDBsum; 5M3V; -.
DR PDBsum; 5W38; -.
DR PDBsum; 6D58; -.
DR PDBsum; 6G1E; -.
DR AlphaFoldDB; P01860; -.
DR SMR; P01860; -.
DR ComplexPortal; CPX-6943; IgG3 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6944; IgG3 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6945; IgG3 - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6946; IgG3 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6947; IgG3 - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6948; IgG3 - Ig lambda 7 immunoglobulin complex, constant regions.
DR IntAct; P01860; 13.
DR DrugBank; DB15258; Imlifidase.
DR IMGT_GENE-DB; IGHG3; -.
DR GlyConnect; 1385; 44 N-Linked glycans (2 sites), 3 O-Linked glycans (3 sites).
DR GlyConnect; 233; 111 N-Linked glycans.
DR GlyConnect; 271; 14 N-Linked glycans.
DR GlyConnect; 2959; 4 O-Linked glycans (3 sites).
DR GlyConnect; 2960; 4 O-Linked glycans (3 sites).
DR GlyGen; P01860; 6 sites, 106 N-linked glycans (3 sites), 7 O-linked glycans (4 sites).
DR iPTMnet; P01860; -.
DR PhosphoSitePlus; P01860; -.
DR BioMuta; IGHG3; -.
DR DMDM; 193806361; -.
DR UCD-2DPAGE; P01860; -.
DR jPOST; P01860; -.
DR MassIVE; P01860; -.
DR MaxQB; P01860; -.
DR PeptideAtlas; P01860; -.
DR PRIDE; P01860; -.
DR ProteomicsDB; 51496; -.
DR UCSC; uc059gdk.1; human.
DR GeneCards; IGHG3; -.
DR HGNC; HGNC:5527; IGHG3.
DR MIM; 147120; gene.
DR neXtProt; NX_P01860; -.
DR InParanoid; P01860; -.
DR PhylomeDB; P01860; -.
DR PathwayCommons; P01860; -.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P01860; -.
DR ChiTaRS; IGHG3; human.
DR Pharos; P01860; Tclin.
DR PRO; PR:P01860; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P01860; protein.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0071735; C:IgG 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: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 GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
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; 3.
DR SMART; SM00407; IGc1; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 2.
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..377
FT /note="Immunoglobulin heavy constant gamma 3"
FT /id="PRO_0000153580"
FT DOMAIN 6..99
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REPEAT 116..130
FT REPEAT 131..145
FT REPEAT 146..160
FT DOMAIN 168..267
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 276..372
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..98
FT /note="CH1"
FT REGION 99..160
FT /note="Hinge"
FT REGION 161..270
FT /note="CH2"
FT REGION 271..376
FT /note="CH3"
FT CARBOHYD 122
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:25759508,
FT ECO:0000269|PubMed:26536155"
FT CARBOHYD 137
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:25759508,
FT ECO:0000269|PubMed:26536155"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:25759508,
FT ECO:0000269|PubMed:26536155"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26536155"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26536155"
FT DISULFID 27..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 111
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 114
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 120
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 126
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 129
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 135
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 141
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 144
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 150
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 156
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 159
FT /note="Interchain (with heavy chain dimer)"
FT DISULFID 191..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 297..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 1..76
FT /note="Missing (in variant WIS)"
FT /id="VAR_068695"
FT VARIANT 77..98
FT /note="GTQTYTCNVNHKPSNTKVDKRV -> QMQGVNCTVSS (in variant
FT WIS)"
FT /id="VAR_068696"
FT VARIANT 213
FT /note="E -> Q (in variant WIS)"
FT /id="VAR_068697"
FT VARIANT 221
FT /note="P -> L (in variant OMM)"
FT /id="VAR_003891"
FT VARIANT 224
FT /note="E -> Q (in variant WIS)"
FT /id="VAR_068698"
FT VARIANT 226
FT /note="Y -> F (in variant ZUC and WIS)"
FT /id="VAR_003892"
FT VARIANT 242
FT /note="D -> N (in variant WIS)"
FT /id="VAR_068699"
FT VARIANT 245
FT /note="N -> D (in variant WIS)"
FT /id="VAR_068700"
FT VARIANT 269
FT /note="T -> A (in variant OMM)"
FT /id="VAR_003893"
FT VARIANT 314
FT /note="S -> N (in variant OMM)"
FT /id="VAR_003894"
FT VARIANT 314
FT /note="Missing (in variant ZUC)"
FT /id="VAR_003895"
FT VARIANT 366
FT /note="F -> Y (in variant OMM)"
FT /id="VAR_003896"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5W38"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4WWI"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4WWI"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6D58"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:5W38"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5W38"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 290..305
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:5W38"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:5W38"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:5W38"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:5W38"
SQ SEQUENCE 377 AA; 41287 MW; FEB7F537953F807F CRC64;
ASTKGPSVFP LAPCSRSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV HTFPAVLQSS
GLYSLSSVVT VPSSSLGTQT YTCNVNHKPS NTKVDKRVEL KTPLGDTTHT CPRCPEPKSC
DTPPPCPRCP EPKSCDTPPP CPRCPEPKSC DTPPPCPRCP APELLGGPSV FLFPPKPKDT
LMISRTPEVT CVVVDVSHED PEVQFKWYVD GVEVHNAKTK PREEQYNSTF RVVSVLTVLH
QDWLNGKEYK CKVSNKALPA PIEKTISKTK GQPREPQVYT LPPSREEMTK NQVSLTCLVK
GFYPSDIAVE WESSGQPENN YNTTPPMLDS DGSFFLYSKL TVDKSRWQQG NIFSCSVMHE
ALHNRFTQKS LSLSPGK
