FCER2_HUMAN
ID FCER2_HUMAN Reviewed; 321 AA.
AC P06734;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor;
DE AltName: Full=BLAST-2;
DE AltName: Full=C-type lectin domain family 4 member J;
DE AltName: Full=Fc-epsilon-RII;
DE AltName: Full=Immunoglobulin E-binding factor;
DE AltName: Full=Lymphocyte IgE receptor;
DE AltName: CD_antigen=CD23;
DE Contains:
DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor membrane-bound form;
DE Contains:
DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor soluble form;
GN Name=FCER2; Synonyms=CD23A, CLEC4J, FCE2, IGEBF;
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 [MRNA].
RX PubMed=2949326; DOI=10.1073/pnas.84.3.819;
RA Ikuta K., Takami M., Kim C.W., Honjo T., Miyoshi T., Tagaya Y., Kawabe T.,
RA Yodoi J.;
RT "Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA
RT with animal lectins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:819-823(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2877743; DOI=10.1016/0092-8674(86)90508-8;
RA Kikutani H., Inui S., Sato R., Barsumian E.L., Owaki H., Yamasaki K.,
RA Kaisho T., Uchibayashi N., Hardy R.R., Hirano T., Tsunasawa S.,
RA Sakiyama F., Suemura M., Kishimoto T.;
RT "Molecular structure of human lymphocyte receptor for immunoglobulin E.";
RL Cell 47:657-665(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3034567; DOI=10.1002/j.1460-2075.1987.tb04726.x;
RA Luedin C., Hofstetter H., Sarfati M., Levy C.A., Suter U., Alaimo D.,
RA Kilchherr E., Frost H., Delespesse G.;
RT "Cloning and expression of the cDNA coding for a human lymphocyte IgE
RT receptor.";
RL EMBO J. 6:109-114(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, and Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2972386; DOI=10.1016/0092-8674(88)90219-x;
RA Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E.L., Suemura M.,
RA Kishimoto T.;
RT "Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue-
RT specific and IL-4-specific regulation of gene expression.";
RL Cell 55:611-618(1988).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=1417742; DOI=10.1042/bj2860819;
RA Rose K., Turcatti G., Graber P., Pochon S., Regamey P.-O., Jansen K.U.,
RA Magnenat E., Aubonney N., Bonnefoy J.-Y.;
RT "Partial characterization of natural and recombinant human soluble CD23.";
RL Biochem. J. 286:819-824(1992).
RN [8]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE BY ADAM10.
RX PubMed=17389606; DOI=10.1074/jbc.m608414200;
RA Lemieux G.A., Blumenkron F., Yeung N., Zhou P., Williams J., Grammer A.C.,
RA Petrovich R., Lipsky P.E., Moss M.L., Werb Z.;
RT "The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase
RT ADAM10.";
RL J. Biol. Chem. 282:14836-14844(2007).
RN [9]
RP PALMITOYLATION AT CYS-17 AND CYS-18, AND SUBCELLULAR LOCATION.
RC TISSUE=B-cell;
RX PubMed=22615937; DOI=10.1371/journal.pone.0037187;
RA Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T.,
RA Garin J., Journet A.;
RT "Proteomic analysis of S-acylated proteins in human B cells reveals
RT palmitoylation of the immune regulators CD20 and CD23.";
RL PLoS ONE 7:E37187-E37187(2012).
RN [10]
RP 3D-STRUCTURE MODELING OF LECTIN DOMAIN.
RX PubMed=8142907;
RA Padlan E.A., Helm B.A.;
RT "Modeling of the lectin-homology domains of the human and murine low-
RT affinity Fc epsilon receptor (Fc epsilon RII/CD23).";
RL Receptor 3:325-341(1993).
RN [11]
RP 3D-STRUCTURE MODELING OF 173-285.
RX PubMed=8745401; DOI=10.1002/pro.5560050207;
RA Bajorath J., Aruffo A.;
RT "Structure-based modeling of the ligand binding domain of the human cell
RT surface receptor CD23 and comparison of two independently derived molecular
RT models.";
RL Protein Sci. 5:240-247(1996).
RN [12]
RP STRUCTURE BY NMR OF 156-298, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=16172256; DOI=10.1084/jem.20050811;
RA Hibbert R.G., Teriete P., Grundy G.J., Beavil R.L., Reljic R., Holers V.M.,
RA Hannan J.P., Sutton B.J., Gould H.J., McDonnell J.M.;
RT "The structure of human CD23 and its interactions with IgE and CD21.";
RL J. Exp. Med. 202:751-760(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-321 ALONE AND IN COMPLEX WITH
RP CALCIUM, AND DISULFIDE BONDS.
RX PubMed=16765898; DOI=10.1016/j.str.2006.03.017;
RA Wurzburg B.A., Tarchevskaya S.S., Jardetzky T.S.;
RT "Structural changes in the lectin domain of CD23, the low-affinity IgE
RT receptor, upon calcium binding.";
RL Structure 14:1049-1058(2006).
RN [14]
RP VARIANT PHE-316.
RX PubMed=23424103; DOI=10.1002/ana.23832;
RA Hersheson J., Mencacci N.E., Davis M., Macdonald N., Trabzuni D., Ryten M.,
RA Pittman A., Paudel R., Kara E., Fawcett K., Plagnol V., Bhatia K.P.,
RA Medlar A.J., Stanescu H.C., Hardy J., Kleta R., Wood N.W., Houlden H.;
RT "Mutations in the autoregulatory domain of beta-tubulin 4a cause hereditary
RT dystonia.";
RL Ann. Neurol. 73:546-553(2013).
CC -!- FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and
CC CR2/CD21. Has essential roles in the regulation of IgE production and
CC in the differentiation of B-cells (it is a B-cell-specific antigen).
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16172256,
CC ECO:0000269|PubMed:16765898}.
CC -!- INTERACTION:
CC P06734; P17544: ATF7; NbExp=3; IntAct=EBI-10199985, EBI-765623;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Cell membrane; Lipid-anchor. Secreted. Note=Also exists as a
CC soluble excreted form, sCD23.
CC -!- PTM: N- and O-glycosylated.
CC -!- PTM: The secreted form sCD23 is produced by ADAM10-mediated ectodomain
CC shedding.
CC -!- MISCELLANEOUS: There are two kinds of Fc receptors for IgE, which
CC differ in both structure and function: high affinity receptors on
CC basophils and mast cells and low affinity receptors on lymphocytes and
CC monocytes.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=CD23;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_221";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FCER2ID44222ch19p13.html";
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DR EMBL; M15059; AAA52434.1; -; mRNA.
DR EMBL; M14766; AAA52435.1; -; mRNA.
DR EMBL; X04772; CAA28465.1; -; mRNA.
DR EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014108; AAH14108.1; -; mRNA.
DR EMBL; BC062591; AAH62591.1; -; mRNA.
DR EMBL; M23562; AAA52433.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS12184.1; -.
DR PIR; A26067; LNHUER.
DR RefSeq; NP_001193948.2; NM_001207019.2.
DR RefSeq; NP_001207429.1; NM_001220500.1.
DR RefSeq; NP_001993.2; NM_002002.4.
DR RefSeq; XP_005272519.1; XM_005272462.4.
DR PDB; 1T8C; NMR; -; A=156-298.
DR PDB; 1T8D; NMR; -; A=156-298.
DR PDB; 2H2R; X-ray; 1.50 A; A/B=150-321.
DR PDB; 2H2T; X-ray; 1.30 A; B=150-321.
DR PDB; 4EZM; X-ray; 3.10 A; G/H/I/J/K/L=156-298.
DR PDB; 4G96; X-ray; 2.25 A; A/B/C/D=156-298.
DR PDB; 4G9A; X-ray; 2.00 A; A/B/C/D=156-298.
DR PDB; 4GI0; X-ray; 2.27 A; A/B/C=156-298.
DR PDB; 4GJ0; X-ray; 1.95 A; A/B/C/D=156-298.
DR PDB; 4GJX; X-ray; 2.80 A; A/B/C/D/E/F/G/H=156-298.
DR PDB; 4GK1; X-ray; 2.24 A; A/B/C/D/E/F/G=156-298.
DR PDB; 4GKO; X-ray; 3.30 A; G/H/I/J/K/L=156-298.
DR PDB; 4J6J; X-ray; 1.90 A; A/B/C/D=156-298.
DR PDB; 4J6K; X-ray; 2.30 A; A/B/C/D/E/F/G/H=156-298.
DR PDB; 4J6L; X-ray; 3.15 A; A/B/C/D/E/F/G/H=156-298.
DR PDB; 4J6M; X-ray; 2.48 A; A/B/C/D/E/F/G/H=156-298.
DR PDB; 4J6N; X-ray; 2.85 A; A/B=156-298.
DR PDB; 4J6P; X-ray; 1.90 A; A/B/C/D=156-298.
DR PDB; 4J6Q; X-ray; 2.54 A; A=156-298.
DR PDB; 4KI1; X-ray; 3.20 A; E/F/G/H=156-298.
DR PDB; 5LGK; X-ray; 3.50 A; E/F=165-284.
DR PDB; 6Y0L; X-ray; 1.65 A; A=156-298.
DR PDB; 6Y0M; X-ray; 1.50 A; A=156-298.
DR PDBsum; 1T8C; -.
DR PDBsum; 1T8D; -.
DR PDBsum; 2H2R; -.
DR PDBsum; 2H2T; -.
DR PDBsum; 4EZM; -.
DR PDBsum; 4G96; -.
DR PDBsum; 4G9A; -.
DR PDBsum; 4GI0; -.
DR PDBsum; 4GJ0; -.
DR PDBsum; 4GJX; -.
DR PDBsum; 4GK1; -.
DR PDBsum; 4GKO; -.
DR PDBsum; 4J6J; -.
DR PDBsum; 4J6K; -.
DR PDBsum; 4J6L; -.
DR PDBsum; 4J6M; -.
DR PDBsum; 4J6N; -.
DR PDBsum; 4J6P; -.
DR PDBsum; 4J6Q; -.
DR PDBsum; 4KI1; -.
DR PDBsum; 5LGK; -.
DR PDBsum; 6Y0L; -.
DR PDBsum; 6Y0M; -.
DR AlphaFoldDB; P06734; -.
DR BMRB; P06734; -.
DR SMR; P06734; -.
DR BioGRID; 108502; 5.
DR CORUM; P06734; -.
DR IntAct; P06734; 1.
DR STRING; 9606.ENSP00000264072; -.
DR BindingDB; P06734; -.
DR ChEMBL; CHEMBL2940; -.
DR DrugBank; DB06162; Lumiliximab.
DR GuidetoPHARMACOLOGY; 2935; -.
DR GlyGen; P06734; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P06734; -.
DR PhosphoSitePlus; P06734; -.
DR SwissPalm; P06734; -.
DR BioMuta; FCER2; -.
DR DMDM; 119862; -.
DR jPOST; P06734; -.
DR MassIVE; P06734; -.
DR MaxQB; P06734; -.
DR PaxDb; P06734; -.
DR PeptideAtlas; P06734; -.
DR PRIDE; P06734; -.
DR ProteomicsDB; 51921; -.
DR ABCD; P06734; 1 sequenced antibody.
DR Antibodypedia; 2294; 1713 antibodies from 50 providers.
DR DNASU; 2208; -.
DR Ensembl; ENST00000346664.9; ENSP00000264072.6; ENSG00000104921.15.
DR Ensembl; ENST00000597921.6; ENSP00000471974.1; ENSG00000104921.15.
DR GeneID; 2208; -.
DR KEGG; hsa:2208; -.
DR MANE-Select; ENST00000597921.6; ENSP00000471974.1; NM_001220500.2; NP_001207429.1.
DR UCSC; uc002mhm.3; human.
DR CTD; 2208; -.
DR DisGeNET; 2208; -.
DR GeneCards; FCER2; -.
DR HGNC; HGNC:3612; FCER2.
DR HPA; ENSG00000104921; Tissue enriched (lymphoid).
DR MIM; 151445; gene.
DR neXtProt; NX_P06734; -.
DR OpenTargets; ENSG00000104921; -.
DR PharmGKB; PA28058; -.
DR VEuPathDB; HostDB:ENSG00000104921; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162574; -.
DR HOGENOM; CLU_049894_7_2_1; -.
DR InParanoid; P06734; -.
DR OMA; TCNTCPE; -.
DR OrthoDB; 985894at2759; -.
DR PhylomeDB; P06734; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; P06734; -.
DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P06734; -.
DR SIGNOR; P06734; -.
DR BioGRID-ORCS; 2208; 6 hits in 1064 CRISPR screens.
DR EvolutionaryTrace; P06734; -.
DR GeneWiki; CD23; -.
DR GenomeRNAi; 2208; -.
DR Pharos; P06734; Tchem.
DR PRO; PR:P06734; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P06734; protein.
DR Bgee; ENSG00000104921; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; P06734; baseline and differential.
DR Genevisible; P06734; HS.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IDA:BHF-UCL.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR DisProt; DP02975; -.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; IgE-binding protein; Lectin; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Receptor; Reference proteome; Repeat;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..321
FT /note="Low affinity immunoglobulin epsilon Fc receptor
FT membrane-bound form"
FT /id="PRO_0000017391"
FT CHAIN 150..321
FT /note="Low affinity immunoglobulin epsilon Fc receptor
FT soluble form"
FT /id="PRO_0000017392"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 69..89
FT REPEAT 90..110
FT REPEAT 111..131
FT DOMAIN 162..284
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 66..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16765898"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16765898"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16765898"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16765898"
FT SITE 149..150
FT /note="Cleavage"
FT LIPID 17
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22615937"
FT LIPID 18
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22615937"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..288
FT DISULFID 163..174
FT DISULFID 191..282
FT DISULFID 259..273
FT VARIANT 62
FT /note="R -> W (in dbSNP:rs2228137)"
FT /id="VAR_035387"
FT VARIANT 284
FT /note="R -> Q (in dbSNP:rs8102872)"
FT /id="VAR_035388"
FT VARIANT 316
FT /note="S -> F"
FT /evidence="ECO:0000269|PubMed:23424103"
FT /id="VAR_069800"
FT CONFLICT 269
FT /note="N -> T (in Ref. 3; CAA28465)"
FT /evidence="ECO:0000305"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2H2R"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1T8C"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:2H2T"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4J6N"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1T8C"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2H2T"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2H2T"
FT TURN 247..252
FT /evidence="ECO:0007829|PDB:4GK1"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6Y0M"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:5LGK"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:2H2T"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2H2R"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:1T8C"
SQ SEQUENCE 321 AA; 36469 MW; F86708C0E6515B87 CRC64;
MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT QSLKQLEERA
ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ RLKSQDLELS WNLNGLQADL
SSFKSQELNE RNEASDLLER LREEVTKLRM ELQVSSGFVC NTCPEKWINF QRKCYYFGKG
TKQWVHARYA CDDMEGQLVS IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV
DYSNWAPGEP TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM
GPDSRPDPDG RLPTPSAPLH S
