IGHA2_HUMAN
ID IGHA2_HUMAN Reviewed; 340 AA.
AC P01877; A0A075B6N7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Immunoglobulin heavy constant alpha 2 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.7};
DE AltName: Full=Ig alpha-2 chain C region {ECO:0000305};
DE AltName: Full=Ig alpha-2 chain C region BUT {ECO:0000305|PubMed:416441};
DE AltName: Full=Ig alpha-2 chain C region LAN {ECO:0000305|PubMed:286295};
GN Name=IGHA2 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.7};
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.
RX PubMed=416441; DOI=10.1073/pnas.75.2.966;
RA Torano A., Putnam F.W.;
RT "Complete amino acid sequence of the alpha 2 heavy chain of a human IgA2
RT immunoglobulin of the A2m (2) allotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:966-969(1978).
RN [2]
RP PROTEIN SEQUENCE (IMGT ALLELE IGHA2*01), AND VARIANTS PRO-93; PRO-102;
RP PHE-279; ASP-296; VAL-326 AND VAL-335.
RX PubMed=286295; DOI=10.1073/pnas.76.3.1104;
RA Tsuzukida Y., Wang C.-C., Putnam F.W.;
RT "Structure of the A2m(1) allotype of human IgA -- a recombinant molecule.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1104-1108(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHA2*01), AND VARIANTS
RP PRO-93; PRO-102; PHE-279; ASP-296; VAL-326 AND VAL-335.
RX PubMed=6421489; DOI=10.1016/0092-8674(84)90348-9;
RA Flanagan J.G., Lefranc M.-P., Rabbitts T.H.;
RT "Mechanisms of divergence and convergence of the human immunoglobulin alpha
RT 1 and alpha 2 constant region gene sequences.";
RL Cell 36:681-688(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHA2*02).
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 [5]
RP REVIEW ON FUNCTION.
RX PubMed=2241915; DOI=10.1042/bj2710285;
RA Kerr M.A.;
RT "The structure and function of human IgA.";
RL Biochem. J. 271:285-296(1990).
RN [6]
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 [7]
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131 AND ASN-205.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205 AND ASN-327.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
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-47; ASN-92; ASN-131; ASN-205
RP AND ASN-327.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [13]
RP GLYCOSYLATION AT ASN-92; ASN-327 AND ASN-205.
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 [14]
RP LACK OF GLYCOSYLATION AT ASN-92.
RA Kolarich D.;
RL Submitted (JUL-2009) to UniProtKB.
RN [15]
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 [16]
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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 110-340 IN COMPLEX
RP WITH PIGR AND JCHAIN, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=32029686; DOI=10.1126/science.aaz5807;
RA Kumar N., Arthur C.P., Ciferri C., Matsumoto M.L.;
RT "Structure of the secretory immunoglobulin A core.";
RL Science 367:1008-1014(2020).
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 Ig alpha is the major immunoglobulin class in body secretions
CC (PubMed:2241915). {ECO:0000303|PubMed:17576170,
CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
CC ECO:0000303|PubMed:2241915}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked (PubMed:20176268).
CC Monomeric or polymeric (PubMed:2241915). Part of the secretory IgA
CC (sIgA) complex that consists of two, four or five IgA monomers, and two
CC additional non-Ig polypeptides, namely the JCHAIN and the secretory
CC component (the proteoytic product of PIGR).
CC {ECO:0000269|PubMed:32029686, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:2241915}.
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 IGHA2*02. {ECO:0000305}.
CC -!- CAUTION: N-glycosylation was reported in milk on the non-canonical Asn-
CC 92 site (PubMed:18780401). However, according to Ref.14, N-
CC glycosylation from the same tissue was found to be absent at this site.
CC {ECO:0000305|Ref.14}.
CC -!- CAUTION: For an example of a full-length immunoglobulin alpha heavy
CC chain see AC P0DOX2. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J00221; AAB59396.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL928742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B22360; B22360.
DR PDB; 3CM9; X-ray; -; A/B/C/D=2-340.
DR PDB; 6UE8; EM; 3.00 A; A/B/E/F/G/H/K/L=110-340.
DR PDB; 6UE9; EM; 2.90 A; A/B/E/F/G/H/K/L=110-340.
DR PDB; 6UEA; EM; 3.00 A; A/B/E/F/G/H/I/J/K/L=110-340.
DR PDBsum; 3CM9; -.
DR PDBsum; 6UE8; -.
DR PDBsum; 6UE9; -.
DR PDBsum; 6UEA; -.
DR AlphaFoldDB; P01877; -.
DR SMR; P01877; -.
DR ComplexPortal; CPX-6962; IgA2 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6963; IgA2 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6964; IgA2 - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6965; IgA2 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6966; IgA2 - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6967; IgA2 - Ig lambda 7 immunoglobulin complex, constant regions.
DR IntAct; P01877; 43.
DR DrugBank; DB04676; Dansyllysine.
DR IMGT_GENE-DB; IGHA2; -.
DR GlyConnect; 227; 58 N-Linked glycans (1 site), 1 O-Linked glycan.
DR GlyConnect; 2967; 37 N-Linked glycans.
DR GlyConnect; 647; 118 N-Linked glycans (5 sites).
DR GlyGen; P01877; 6 sites, 115 N-linked glycans (6 sites), 2 O-linked glycans (1 site).
DR iPTMnet; P01877; -.
DR PhosphoSitePlus; P01877; -.
DR BioMuta; IGHA2; -.
DR DMDM; 218512088; -.
DR CPTAC; CPTAC-674; -.
DR jPOST; P01877; -.
DR MassIVE; P01877; -.
DR PeptideAtlas; P01877; -.
DR PRIDE; P01877; -.
DR ProteomicsDB; 51501; -.
DR Ensembl; ENST00000390539.2; ENSP00000374981.2; ENSG00000211890.4.
DR GeneCards; IGHA2; -.
DR HGNC; HGNC:5479; IGHA2.
DR HPA; ENSG00000211890; Group enriched (intestine, salivary gland).
DR MIM; 147000; gene.
DR neXtProt; NX_P01877; -.
DR OpenTargets; ENSG00000211890; -.
DR VEuPathDB; HostDB:ENSG00000211890; -.
DR GeneTree; ENSGT00940000161516; -.
DR InParanoid; P01877; -.
DR PhylomeDB; P01877; -.
DR PathwayCommons; P01877; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR SignaLink; P01877; -.
DR ChiTaRS; IGHA2; human.
DR Pharos; P01877; Tbio.
DR PRO; PR:P01877; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01877; protein.
DR Bgee; ENSG00000211890; Expressed in mucosa of transverse colon and 87 other tissues.
DR ExpressionAtlas; P01877; baseline and differential.
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:0071745; C:IgA immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0071748; C:monomeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0071752; C:secretory dimeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
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:0003094; P:glomerular filtration; IMP:UniProtKB.
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 GO; GO:0060267; P:positive regulation of respiratory burst; IDA:UniProtKB.
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 InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF07654; C1-set; 2.
DR Pfam; PF00047; ig; 1.
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..340
FT /note="Immunoglobulin heavy constant alpha 2"
FT /id="PRO_0000153567"
FT DOMAIN 6..98
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 112..207
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 215..317
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:18780401"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490"
FT DISULFID 26..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 101
FT /note="Interchain (with light chain)"
FT DISULFID 109
FT /note="Interchain (with heavy chain)"
FT DISULFID 110..167
FT DISULFID 134..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 169
FT /note="Interchain (with heavy chain)"
FT DISULFID 179
FT /note="Interchain (with heavy chain of another subunit) (or
FT with C-503 of PIGR/the secretory component)"
FT /evidence="ECO:0000250|UniProtKB:P01876,
FT ECO:0000269|PubMed:32029686"
FT DISULFID 237..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339
FT /note="Interchain (with J chain)"
FT VARIANT 93
FT /note="S -> P (in IMGT allele IGHA2*01)"
FT /evidence="ECO:0000269|PubMed:286295,
FT ECO:0000269|PubMed:6421489"
FT /id="VAR_003879"
FT VARIANT 102
FT /note="R -> P (in IMGT allele IGHA2*01)"
FT /evidence="ECO:0000269|PubMed:286295,
FT ECO:0000269|PubMed:6421489"
FT /id="VAR_003880"
FT VARIANT 279
FT /note="Y -> F (in IMGT allele IGHA2*01)"
FT /evidence="ECO:0000269|PubMed:286295,
FT ECO:0000269|PubMed:6421489"
FT /id="VAR_003881"
FT VARIANT 296
FT /note="E -> D (in IMGT allele IGHA2*01)"
FT /evidence="ECO:0000269|PubMed:286295,
FT ECO:0000269|PubMed:6421489"
FT /id="VAR_003882"
FT VARIANT 326
FT /note="I -> V (in IMGT allele IGHA2*01)"
FT /evidence="ECO:0000269|PubMed:286295,
FT ECO:0000269|PubMed:6421489"
FT /id="VAR_003883"
FT VARIANT 335
FT /note="A -> V (in IMGT allele IGHA2*01)"
FT /evidence="ECO:0000269|PubMed:286295,
FT ECO:0000269|PubMed:6421489"
FT /id="VAR_003884"
FT CONFLICT 319
FT /note="M -> L (in Ref. 1; AA sequence, 3; AAB59396 and 2;
FT AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6UE9"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6UE9"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6UEA"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6UE9"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 231..244
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:6UE9"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6UE8"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:6UE9"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6UE9"
SQ SEQUENCE 340 AA; 36591 MW; 2DF338B77F520DCB CRC64;
ASPTSPKVFP LSLDSTPQDG NVVVACLVQG FFPQEPLSVT WSESGQNVTA RNFPPSQDAS
GDLYTTSSQL TLPATQCPDG KSVTCHVKHY TNSSQDVTVP CRVPPPPPCC HPRLSLHRPA
LEDLLLGSEA NLTCTLTGLR DASGATFTWT PSSGKSAVQG PPERDLCGCY SVSSVLPGCA
QPWNHGETFT CTAAHPELKT PLTANITKSG NTFRPEVHLL PPPSEELALN ELVTLTCLAR
GFSPKDVLVR WLQGSQELPR EKYLTWASRQ EPSQGTTTYA VTSILRVAAE DWKKGETFSC
MVGHEALPLA FTQKTIDRMA GKPTHINVSV VMAEADGTCY
