IGHG2_HUMAN
ID IGHG2_HUMAN Reviewed; 326 AA.
AC P01859; A6NE66;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Immunoglobulin heavy constant gamma 2 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.13};
DE AltName: Full=Ig gamma-2 chain C region {ECO:0000305};
DE AltName: Full=Ig gamma-2 chain C region DOT {ECO:0000305|PubMed:7737190};
DE AltName: Full=Ig gamma-2 chain C region TIL {ECO:0000305|PubMed:6774012};
DE AltName: Full=Ig gamma-2 chain C region ZIE {ECO:0000305|PubMed:113060, ECO:0000305|PubMed:118920};
GN Name=IGHG2 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.13};
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHG2*01), AND VARIANT
RP ALA-257.
RX PubMed=6804948; DOI=10.1073/pnas.79.6.1984;
RA Ellison J.W., Hood L.E.;
RT "Linkage and sequence homology of two human immunoglobulin gamma heavy
RT chain constant region genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1984-1988(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHG2*06).
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 [3]
RP PROTEIN SEQUENCE OF 1-325, AND VARIANT ALA-60.
RX PubMed=6774012;
RA Wang A.-C., Tung E., Fudenberg H.H.;
RT "The primary structure of a human IgG2 heavy chain: genetic, evolutionary,
RT and functional implications.";
RL J. Immunol. 125:1048-1054(1980).
RN [4]
RP PROTEIN SEQUENCE OF 1-121.
RX PubMed=7737190; DOI=10.1111/j.1432-1033.1995.tb20336.x;
RA Stoppini M., Bellotti V., Negri A., Merlini G., Garver F., Ferri G.;
RT "Characterization of the two unique human anti-flavin monoclonal
RT immunoglobulins.";
RL Eur. J. Biochem. 228:886-893(1995).
RN [5]
RP PROTEIN SEQUENCE OF 1-85 AND 132-325, AND VARIANT ALA-60.
RX PubMed=113060; DOI=10.1139/o79-094;
RA Connell G.E., Parr D.M., Hofmann T.;
RT "The amino acid sequences of the three heavy chain constant region domains
RT of a human IgG2 myeloma protein.";
RL Can. J. Biochem. 57:758-767(1979).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 88-115.
RC TISSUE=Fetal liver;
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 [GENOMIC DNA] OF 99-177 AND 310-326.
RC TISSUE=Fetal liver;
RX PubMed=6329676; DOI=10.1002/j.1460-2075.1982.tb01182.x;
RA Krawinkel U., Rabbitts T.H.;
RT "Comparison of the hinge-coding segments in human immunoglobulin gamma
RT heavy chain genes and the linkage of the gamma 2 and gamma 4 subclass
RT genes.";
RL EMBO J. 1:403-407(1982).
RN [8]
RP PROTEIN SEQUENCE OF 238-275.
RX PubMed=118920; DOI=10.1016/0161-5890(79)90091-9;
RA Hofmann T., Parr D.M.;
RT "A note of the amino acid sequence of residues 381-391 of human
RT immunoglobulins gamma chains.";
RL Mol. Immunol. 16:923-925(1979).
RN [9]
RP SEQUENCE REVISION TO 25; 59; 60 AND 264-268.
RA Hofmann T., Parr D.M.;
RL Submitted (MAR-1980) to the PIR data bank.
RN [10]
RP DISULFIDE BONDS.
RX PubMed=4940472; DOI=10.1042/bj1210217;
RA Milstein C., Frangione B.;
RT "Disulphide bridges of the heavy chain of human immunoglobulin G2.";
RL Biochem. J. 121:217-225(1971).
RN [11]
RP DISULFIDE BONDS.
RX PubMed=5782707; DOI=10.1038/221145a0;
RA Frangione B., Milstein C., Pink J.R.L.;
RT "Structural studies of immunoglobulin G.";
RL Nature 221:145-148(1969).
RN [12]
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 [13]
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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [15]
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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176.
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 [17]
RP GLYCOSYLATION AT ASN-176.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [18]
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 [19]
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: 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 -!- INTERACTION:
CC P01859; Q28109; Xeno; NbExp=3; IntAct=EBI-1044662, EBI-8061363;
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 IGHG2*06. {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=AAB59393.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=IGHG2base; Note=IGHG2 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/IGHG2base/";
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DR EMBL; J00230; AAB59393.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL928742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A93906; G2HU.
DR PDB; 2QSC; X-ray; 2.80 A; H=1-99.
DR PDB; 4HAF; X-ray; 2.04 A; A/B=104-326.
DR PDB; 4HAG; X-ray; 3.40 A; A=104-326.
DR PDB; 4L4J; X-ray; 1.92 A; A/B=106-326.
DR PDB; 7LUS; X-ray; 2.45 A; A=116-323, B=116-322.
DR PDBsum; 2QSC; -.
DR PDBsum; 4HAF; -.
DR PDBsum; 4HAG; -.
DR PDBsum; 4L4J; -.
DR PDBsum; 7LUS; -.
DR AlphaFoldDB; P01859; -.
DR SASBDB; P01859; -.
DR SMR; P01859; -.
DR ComplexPortal; CPX-6936; IgG2 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6938; IgG2 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6939; IgG2 - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6940; IgG2 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6941; IgG2 - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6942; IgG2 - Ig lambda 7 immunoglobulin complex, constant regions.
DR IntAct; P01859; 39.
DR MINT; P01859; -.
DR DrugBank; DB07329; 1-[N-4'-NITROBENZYL-N-4'-CARBOXYBUTYLAMINO]METHYLPHOSPHONIC ACID.
DR DrugBank; DB08618; 3-(HYDROXY-PHENYL-PHOSPHINOYLOXY)-8-METHYL-8-AZA-BICYCLO[3.2.1]OCTANE-2-CARBOXYLIC ACID METHYL ESTER.
DR DrugBank; DB08323; 3-OXO-N-[(3S)-2-OXOPYRROLIDIN-3-YL]DODECANAMIDE.
DR DrugBank; DB08409; 4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINE.
DR DrugBank; DB08510; 5-ALPHA-PREGNANE-3-BETA-OL-HEMISUCCINATE.
DR DrugBank; DB02854; Aetiocholanolone.
DR DrugBank; DB07375; Etiocholanedione.
DR DrugBank; DB15258; Imlifidase.
DR DrugBank; DB04688; Methylecgonine.
DR DrugBank; DB08547; PROGESTERONE-11-ALPHA-OL-HEMISUCCINATE.
DR IMGT_GENE-DB; IGHG2; -.
DR GlyConnect; 233; 111 N-Linked glycans.
DR GlyConnect; 2973; 32 N-Linked glycans.
DR GlyConnect; 2974; 29 N-Linked glycans.
DR GlyConnect; 688; 103 N-Linked glycans (2 sites).
DR GlyConnect; 748; 3 N-Linked glycans (1 site).
DR GlyGen; P01859; 2 sites, 122 N-linked glycans (2 sites).
DR iPTMnet; P01859; -.
DR PhosphoSitePlus; P01859; -.
DR BioMuta; IGHG2; -.
DR DMDM; 218512079; -.
DR UCD-2DPAGE; P01859; -.
DR CPTAC; CPTAC-675; -.
DR EPD; P01859; -.
DR jPOST; P01859; -.
DR MassIVE; P01859; -.
DR MaxQB; P01859; -.
DR PeptideAtlas; P01859; -.
DR PRIDE; P01859; -.
DR ProteomicsDB; 51495; -.
DR ABCD; P01859; 2 sequenced antibodies.
DR Ensembl; ENST00000390545.3; ENSP00000374987.2; ENSG00000211893.4.
DR Ensembl; ENST00000621803.2; ENSP00000480351.2; ENSG00000274497.2.
DR UCSC; uc059gct.1; human.
DR GeneCards; IGHG2; -.
DR HGNC; HGNC:5526; IGHG2.
DR HPA; ENSG00000211893; Tissue enriched (lymphoid).
DR MalaCards; IGHG2; -.
DR MIM; 147110; gene.
DR neXtProt; NX_P01859; -.
DR OpenTargets; ENSG00000211893; -.
DR Orphanet; 183675; Recurrent infections associated with rare immunoglobulin isotypes deficiency.
DR VEuPathDB; HostDB:ENSG00000211893; -.
DR GeneTree; ENSGT00940000162793; -.
DR HOGENOM; CLU_030625_0_2_1; -.
DR InParanoid; P01859; -.
DR PhylomeDB; P01859; -.
DR TreeFam; TF334176; -.
DR PathwayCommons; P01859; -.
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; P01859; -.
DR ChiTaRS; IGHG2; human.
DR EvolutionaryTrace; P01859; -.
DR Pharos; P01859; Tclin.
DR PRO; PR:P01859; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01859; protein.
DR Bgee; ENSG00000211893; Expressed in vermiform appendix and 92 other tissues.
DR ExpressionAtlas; P01859; baseline and differential.
DR Genevisible; P01859; HS.
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; IDA: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 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; Secreted.
FT CHAIN <1..326
FT /note="Immunoglobulin heavy constant gamma 2"
FT /id="PRO_0000153579"
FT DOMAIN 6..99
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 117..216
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 225..321
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..98
FT /note="CH1"
FT REGION 99..110
FT /note="Hinge"
FT REGION 111..219
FT /note="CH2"
FT REGION 220..326
FT /note="CH3"
FT SITE 156
FT /note="At or near the complement-binding site"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT DISULFID 14
FT /note="Interchain (with a light chain)"
FT DISULFID 27..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 102
FT /note="Interchain (with a heavy chain)"
FT DISULFID 103
FT /note="Interchain (with a heavy chain)"
FT DISULFID 106
FT /note="Interchain (with a heavy chain)"
FT DISULFID 109
FT /note="Interchain (with a heavy chain)"
FT DISULFID 140..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 246..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 60
FT /note="S -> A"
FT /evidence="ECO:0000269|PubMed:113060,
FT ECO:0000269|PubMed:6774012"
FT /id="VAR_003889"
FT VARIANT 257
FT /note="S -> A (in IMGT allele IGHG2*01)"
FT /id="VAR_077892"
FT NON_TER 1
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4L4J"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4HAF"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:7LUS"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:4L4J"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4HAF"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4L4J"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 239..254
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:4L4J"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4L4J"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4L4J"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:4L4J"
SQ SEQUENCE 326 AA; 35901 MW; 95DC5D8C6860B7FC CRC64;
ASTKGPSVFP LAPCSRSTSE STAALGCLVK DYFPEPVTVS WNSGALTSGV HTFPAVLQSS
GLYSLSSVVT VPSSNFGTQT YTCNVDHKPS NTKVDKTVER KCCVECPPCP APPVAGPSVF
LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVQFNWYVDG VEVHNAKTKP REEQFNSTFR
VVSVLTVVHQ DWLNGKEYKC KVSNKGLPAP IEKTISKTKG QPREPQVYTL PPSREEMTKN
QVSLTCLVKG FYPSDISVEW ESNGQPENNY KTTPPMLDSD GSFFLYSKLT VDKSRWQQGN
VFSCSVMHEA LHNHYTQKSL SLSPGK
