ID VCL_CORAV Reviewed; 448 AA. AC Q8S4P9; DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 59. DE RecName: Full=Vicilin Cor a 11.0101 {ECO:0000305}; DE AltName: Full=7S globulin {ECO:0000303|PubMed:19006093, ECO:0000303|PubMed:21563837, ECO:0000303|PubMed:21735061, ECO:0000303|PubMed:31753489}; DE AltName: Full=7S seed storage protein {ECO:0000303|PubMed:19006093}; DE AltName: Full=7S vicilin-like protein Cor a 11 {ECO:0000303|PubMed:22812192, ECO:0000303|Ref.12}; DE AltName: Full=Allergen Cor a 11 {ECO:0000303|PubMed:21563837, ECO:0000303|PubMed:22966848, ECO:0000303|PubMed:23411333, ECO:0000303|Ref.12}; DE AltName: Full=Vicilin Cor a 11 {ECO:0000303|PubMed:15233621, ECO:0000303|PubMed:21563837, ECO:0000303|PubMed:21735061, ECO:0000303|PubMed:22616776}; DE AltName: Full=Vicilin HZ.1 {ECO:0000303|PubMed:31753489}; DE AltName: Allergen=Cor a 11.0101 {ECO:0000305}; OS Corylus avellana (European hazel) (Corylus maxima). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fagales; Betulaceae; Corylus. OX NCBI_TaxID=13451 {ECO:0000312|EMBL:AAL86739.1}; RN [1] {ECO:0000312|EMBL:AAL86739.1} RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-59; 56-72; 73-79; 80-89; RP 92-100; 101-127; 130-136; 140-152; 153-174; 175-201; 202-213; 241-251; RP 252-268; 269-278; 279-304; 305-315; 319-349; 353-388; 389-394; 395-403; RP 407-415; 416-419; 420-442 AND 423-445, TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, PTM, IDENTIFICATION BY MASS SPECTROMETRY, ALLERGEN, SITE, RP GLYCOSYLATION AT ASN-301, AND CIRCULAR DICHROISM ANALYSIS. RC STRAIN=cv. Piemonte {ECO:0000312|EMBL:AAL86739.1}; RC TISSUE=Seed {ECO:0000303|PubMed:15233621}; RX PubMed=15233621; DOI=10.1042/bj20041062; RA Lauer I., Foetisch K., Kolarich D., Ballmer-Weber B.K., Conti A., RA Altmann F., Vieths S., Scheurer S.; RT "Hazelnut (Corylus avellana) vicilin Cor a 11: molecular characterization RT of a glycoprotein and its allergenic activity."; RL Biochem. J. 383:327-334(2004). RN [2] RP PROTEIN SEQUENCE OF 1-11; 5-13; 73-89; 141-152; 175-201; 216-228; 305-315 RP AND 395-403, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND RP BIOTECHNOLOGY. RX PubMed=25209075; DOI=10.1021/jf504007d; RA De Ceglie C., Calvano C.D., Zambonin C.G.; RT "Determination of hidden hazelnut oil proteins in extra virgin olive oil by RT cold acetone precipitation followed by in-solution tryptic digestion and RT MALDI-TOF-MS analysis."; RL J. Agric. Food Chem. 62:9401-9409(2014). RN [3] RP PROTEIN SEQUENCE OF 48-62; 73-89; 92-127; 130-136; 140-169; 175-213; RP 241-278; 305-315; 319-345; 353-388; 395-403; 407-415 AND 423-442, SUBUNIT, RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PTM, IDENTIFICATION BY MASS RP SPECTROMETRY, ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS. RC TISSUE=Seed {ECO:0000303|PubMed:19006093}; RX PubMed=19006093; DOI=10.1002/mnfr.200800083; RA Rigby N.M., Marsh J., Sancho A.I., Wellner K., Akkerdaas J., van Ree R., RA Knulst A., Fernandez-Rivas M., Brettlova V., Schilte P.P., Summer C., RA Pumphrey R., Shewry P.R., Mills E.N.; RT "The purification and characterisation of allergenic hazelnut seed RT proteins."; RL Mol. Nutr. Food Res. 52:S251-S261(2008). RN [4] {ECO:0007744|PDB:6L4C} RP PROTEIN SEQUENCE OF 48-67, X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 25-448 RP IN COMPLEX WITH COPPER, FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=31753489; DOI=10.1016/j.bbrc.2019.11.072; RA Shikhi M., Jain A., Salunke D.M.; RT "Comparative study of 7S globulin from Corylus avellana and Solanum RT lycopersicum revealed importance of salicylic acid and Cu-binding loop in RT modulating their function."; RL Biochem. Biophys. Res. Commun. 522:127-132(2020). RN [5] RP PROTEIN SEQUENCE OF 56-72; 80-89; 92-100; 101-127; 141-152; 153-169; RP 175-201; 202-213; 241-251; 252-268; 269-278; 279-288; 305-315; 395-403; RP 407-415 AND 423-435, TISSUE SPECIFICITY, IDENTIFICATION BY MASS RP SPECTROMETRY, AND BIOTECHNOLOGY. RX PubMed=22966848; DOI=10.1080/19440049.2012.719639; RA Cucu T., De Meulenaer B., Devreese B.; RT "MALDI-based identification of stable hazelnut protein derived tryptic RT marker peptides."; RL Food Addit. Contam. Part A Chem. Anal. Control Expo. Risk Assess. RL 29:1821-1831(2012). RN [6] RP PROTEIN SEQUENCE OF 92-100; 202-213 AND 407-415, TISSUE SPECIFICITY, RP IDENTIFICATION BY MASS SPECTROMETRY, AND BIOTECHNOLOGY. RX PubMed=21735061; DOI=10.1007/s00216-011-5218-6; RA Ansari P., Stoppacher N., Baumgartner S.; RT "Marker peptide selection for the determination of hazelnut by LC-MS/MS and RT occurrence in other nuts."; RL Anal. Bioanal. Chem. 402:2607-2615(2012). RN [7] RP PROTEIN SEQUENCE OF 92-100; 202-213 AND 407-415, TISSUE SPECIFICITY, RP IDENTIFICATION BY MASS SPECTROMETRY, AND BIOTECHNOLOGY. RX PubMed=24577577; DOI=10.1007/s00216-014-7679-x; RA Costa J., Ansari P., Mafra I., Oliveira M.B., Baumgartner S.; RT "Assessing hazelnut allergens by protein- and DNA-based approaches: LC- RT MS/MS, ELISA and real-time PCR."; RL Anal. Bioanal. Chem. 406:2581-2590(2014). RN [8] RP TISSUE SPECIFICITY, AND ALLERGEN. RX PubMed=21563837; DOI=10.1021/jf2007375; RA Iwan M., Vissers Y.M., Fiedorowicz E., Kostyra H., Kostyra E., RA Savelkoul H.F., Wichers H.J.; RT "Impact of Maillard reaction on immunoreactivity and allergenicity of the RT hazelnut allergen Cor a 11."; RL J. Agric. Food Chem. 59:7163-7171(2011). RN [9] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ALLERGEN, AND 3D-STRUCTURE RP MODELING. RX PubMed=22616776; DOI=10.1186/2043-9113-2-12; RA Lopez E., Cuadrado C., Burbano C., Jimenez M.A., Rodriguez J., Crespo J.F.; RT "Effects of autoclaving and high pressure on allergenicity of hazelnut RT proteins."; RL J. Clin. Bioinforma. 2:12-12(2012). RN [10] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ALLERGEN. RX PubMed=22812192; RA Verweij M.M., Hagendorens M.M., Trashin S., Cucu T., De Meulenaer B., RA Devreese B., Bridts C.H., De Clerck L.S., Ebo D.G.; RT "Age-dependent sensitization to the 7S-vicilin-like protein Cor a 11 from RT hazelnut (Corylus avellana) in a birch-endemic region."; RL J. Investig. Allergol. Clin. Immunol. 22:245-251(2012). RN [11] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY. RX PubMed=23411333; DOI=10.1016/j.foodchem.2012.11.036; RA Iniesto E., Jimenez A., Prieto N., Cabanillas B., Burbano C., Pedrosa M.M., RA Rodriguez J., Muzquiz M., Crespo J.F., Cuadrado C., Linacero R.; RT "Real Time PCR to detect hazelnut allergen coding sequences in processed RT foods."; RL Food Chem. 138:1976-1981(2013). RN [12] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY. RX DOI=10.1111/ijfs.12079; RA Garino C., Locatelli M., Coisson J.D., D'Andrea M., Cereti E., RA Travaglia F., Arlorio M.; RT "Gene transcription analysis of hazelnut (C orylus avellana L.) allergens RT Cor a 1, Cor a 8 and Cor a 11: a comparative study."; RL Int. J. Food Sci. Technol. 48:1208-1217(2013). RN [13] RP ALLERGEN. RX PubMed=34146442; DOI=10.1111/pai.13579; RA Nebbia S., Lamberti C., Cirrincione S., Acquadro A., Abba S., Ciuffo M., RA Torello Marinoni D., Manfredi M., Marengo E., Calzedda R., Monti G., RA Cavallarin L., Giuffrida M.G.; RT "Oleosin Cor a 15 is a novel allergen for Italian hazelnut allergic RT children."; RL Pediatr. Allergy Immunol. 32:1743-1755(2021). CC -!- FUNCTION: Seed storage protein (PubMed:15233621, PubMed:19006093, CC PubMed:21563837, PubMed:21735061, PubMed:22966848, PubMed:22616776, CC PubMed:22812192, PubMed:23411333, Ref.12, PubMed:24577577, CC PubMed:25209075). Does not have superoxide dismutase (SOD) activity CC (PubMed:31753489). {ECO:0000269|PubMed:31753489, CC ECO:0000305|PubMed:15233621, ECO:0000305|PubMed:19006093, CC ECO:0000305|PubMed:21563837, ECO:0000305|PubMed:21735061, CC ECO:0000305|PubMed:22616776, ECO:0000305|PubMed:22812192, CC ECO:0000305|PubMed:22966848, ECO:0000305|PubMed:23411333, CC ECO:0000305|PubMed:24577577, ECO:0000305|PubMed:25209075, CC ECO:0000305|Ref.12}. CC -!- SUBUNIT: Homotrimer (PubMed:19006093, PubMed:31753489). Homohexamer CC (PubMed:19006093). {ECO:0000269|PubMed:19006093, CC ECO:0000269|PubMed:31753489}. CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level) CC (PubMed:15233621, PubMed:19006093, PubMed:21563837, PubMed:21735061, CC PubMed:22966848, PubMed:22616776, PubMed:22812192, PubMed:23411333, CC PubMed:24577577, PubMed:25209075, PubMed:31753489). Expressed in seed CC (Ref.12). {ECO:0000269|PubMed:15233621, ECO:0000269|PubMed:19006093, CC ECO:0000269|PubMed:21563837, ECO:0000269|PubMed:21735061, CC ECO:0000269|PubMed:22616776, ECO:0000269|PubMed:22812192, CC ECO:0000269|PubMed:22966848, ECO:0000269|PubMed:23411333, CC ECO:0000269|PubMed:24577577, ECO:0000269|PubMed:25209075, CC ECO:0000269|PubMed:31753489, ECO:0000269|Ref.12}. CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation. Expressed at CC three fruit developmental stages, at early stage (approximately 45 days CC before harvest), at middle stage (approximately 30 days before harvest) CC and at final harvest stage. Expressed more in ripe than in unripe seeds CC (Ref.12). Expressed in raw seeds (PubMed:15233621, PubMed:19006093, CC PubMed:22616776, PubMed:22812192, PubMed:23411333). CC {ECO:0000269|PubMed:15233621, ECO:0000269|PubMed:19006093, CC ECO:0000269|PubMed:22616776, ECO:0000269|PubMed:22812192, CC ECO:0000269|PubMed:23411333, ECO:0000269|Ref.12}. CC -!- PTM: N-glycosylated at Asn-301 mostly with xylosylated paucimannosidic- CC type N-glycan MMX (an N-linked glycan with beta-1,2-xylose residue in CC the structure) and also with MMXF (a complex N-linked glycan with CC alpha-1,3-fucose and beta-1,2-xylose residues in the structure). CC {ECO:0000269|PubMed:15233621}. CC -!- PTM: A mixture of proteolytically processed and unprocessed subunits CC exist. {ECO:0000269|PubMed:19006093}. CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:15233621, CC PubMed:19006093, PubMed:21563837, PubMed:22616776, PubMed:22812192, CC PubMed:34146442). Binds to IgE of patients allergic to hazelnuts CC (PubMed:15233621, PubMed:19006093, PubMed:21563837, PubMed:22616776, CC PubMed:22812192, PubMed:34146442). Natural glycosylated protein binds CC to IgE in 47% and recombinant (non-glycosylated) protein in 43-40% of CC the 65 tested adult patients from Switzerland and Germany CC (PubMed:15233621). Natural protein binds to IgE in 50% of the tested CC patients from Netherlands (PubMed:19006093). The IgE-binding of the CC natural protein can be decreased by glycation (Maillard reaction) of CC the protein at 60 and 145 (routine hazelnut roasting condition), but CC not at 37 degrees Celsius (PubMed:21563837). IgE-binding of the natural CC protein is also strongly reduced by autoclaving at 138 degrees Celsius CC for 15 or 30 minutes, but not by high pressure treatment alone (300 CC Mba, 400 Mba, 500 Mba and 600 Mba) (PubMed:22616776). Allerginicity to CC this protein in a birch-endemic region (Belgium) seems to be CC predominantly found in children with severe hazelnut allergy compared CC to adults or children with milder forms of hazelnut-allergy. Natural CC protein binds to IgE in 36%, 40% and 12.5% of the 22 preschool CC children, 10 schoolchildren and 8 adults tested, respectively, with CC systemic allergic reactions toward hazelnut. In a set of 40 patients (6 CC preschool children, 10 schoolchildren and 24 adults) having oral CC allergy symptoms, only 2 patients (of preschool age) show IgE-binding CC to this protein. Also, only 8% of the 24 hazelnut-allergic infants with CC atopic dermatitis tested show IgE reactivity to this protein CC (PubMed:22812192). Induces histamine release from human basophils CC (PubMed:15233621, PubMed:22812192). Both natural and recombinant CC proteins induce histamine release from human basophils in a similar CC manner indicating that the carbohydrate structures are not involved in CC IgE-binding (PubMed:15233621). Induces beta-hexosaminidase release from CC humanized rat basophilic leukemia (RBL) cells. Heating, with or without CC glucose, at 145 degrees Celsius increases the basophil degranulation CC capacity (PubMed:21563837). {ECO:0000269|PubMed:15233621, CC ECO:0000269|PubMed:19006093, ECO:0000269|PubMed:21563837, CC ECO:0000269|PubMed:22616776, ECO:0000269|PubMed:22812192, CC ECO:0000269|PubMed:34146442}. CC -!- BIOTECHNOLOGY: In order to protect patients that are allergic to CC hazelnuts, it is extremely important to find ways to detect trace CC amounts of hazelnut in foods that should not contain it for the food CC labeling and safety purposes. This protein is used in the development CC of these methods (PubMed:21735061, PubMed:22966848, PubMed:23411333, CC PubMed:24577577, PubMed:25209075). For the detection of hazelnut, a CC liquid chromatography tandem mass spectrometry (LC-MS/MS) method in CC selected reaction monitoring (SRM) mode is developed by using selected CC marker peptides from this protein as standards (PubMed:21735061). It is CC found that LC-MS/MS performs well in detecting these peptides in CC prepared model chocolates spiked with hazelnut. The sensitivity level CC is approximately 1 mg/kg (PubMed:24577577). A stable peptide (residues CC 395-403) from this protein is identified by MALDI-MS and it can s be CC used as an analytical target for the development of robust quantitative CC analytical methods. This peptide is identifiable even when the protein CC goes through a number of changes at the molecular level, such as CC denaturation, the Maillard reaction and oxidation, reactions that CC typically occur during food processing (PubMed:22966848). A CC quantitative method is developed, where the coding DNA of this protein CC is first extracted based on hexadecyltrimethylammonium bromide (CTAB)- CC phenol-chloroform method and then detected by Real-Time PCR (RT-PCR) in CC commercial foods such as chocolates, biscuits, cereal snacks, cookies CC and nougat with 100% specificity and with 1 ppm sensitivity limit of CC detection of raw hazelnut. The reliability of the method is even more CC improved if two other hazelnut target genes (allergens Cor a 9 and Cor CC a 13) are amplified in addition to this one. The detection is proven to CC be accurate even when the quality and quantity of the DNA is greatly CC diminished by roasting and autoclaving. High-hydrostatic pressure CC treatment has no effect on DNA (PubMed:23411333). The transcription CC level of the gene encoding this protein is investigated by a relative CC quantitative RT-PCR technique in order to compare the transcript CC amounts between different cultivars, and in one of the cultivars also CC in relation to different years of harvest and ripening stages. Each CC hazelnut sample is classified by the Principal Components Analysis CC (PCA) to better interpret the results. The method may help in choosing CC hypoallergenic genotypes of hazelnut for both growers and consumers CC (Ref.12). Cold acetone extraction of proteins followed by in-solution CC tryptic digestion and MALDI-TOF-MS (in alpha-cyano-4-chlorocinnamic CC acid matrix) is found as a rapid and sensitive method to detect CC residual amounts of hazelnut proteins in extra virgin olive oil CC samples, which have been adulterated with cold-pressed hazelnut oil. CC Peptides from this protein can be used as stable markers in this CC technique serving as a direct proof of illegal hazelnut existence in CC olive oil (PubMed:25209075). {ECO:0000269|PubMed:21735061, CC ECO:0000269|PubMed:22966848, ECO:0000269|PubMed:23411333, CC ECO:0000269|PubMed:24577577, ECO:0000269|PubMed:25209075, CC ECO:0000269|Ref.12}. CC -!- SIMILARITY: Belongs to the 7S seed storage protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF441864; AAL86739.1; -; mRNA. DR PDB; 6L4C; X-ray; 3.19 A; A/B/C=25-448. DR PDBsum; 6L4C; -. DR AlphaFoldDB; Q8S4P9; -. DR SMR; Q8S4P9; -. DR Allergome; 3216; Cor a 11.0101. DR Allergome; 690; Cor a 11. DR iPTMnet; Q8S4P9; -. DR GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB. DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB. DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB. DR CDD; cd02245; cupin_7S_vicilin-like_C; 1. DR CDD; cd02244; cupin_7S_vicilin-like_N; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR31189:SF13; CUPINCIN; 1. DR PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1. DR Pfam; PF00190; Cupin_1; 2. DR SMART; SM00835; Cupin_1; 2. DR SUPFAM; SSF51182; RmlC-like cupins; 2. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Copper; Direct protein sequencing; Glycoprotein; KW Metal-binding; Repeat; Seed storage protein; Storage protein. FT CHAIN 1..448 FT /note="Vicilin Cor a 11.0101" FT /id="PRO_0000451919" FT DOMAIN 84..220 FT /note="Cupin type-1 1" FT /evidence="ECO:0000255" FT DOMAIN 263..418 FT /note="Cupin type-1 2" FT /evidence="ECO:0000255" FT REGION 1..66 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 333 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000269|PubMed:31753489, FT ECO:0007744|PDB:6L4C" FT BINDING 335 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000269|PubMed:31753489, FT ECO:0007744|PDB:6L4C" FT BINDING 362 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000269|PubMed:31753489, FT ECO:0007744|PDB:6L4C" FT SITE 47..48 FT /note="Cleavage" FT /evidence="ECO:0000305|PubMed:19006093, FT ECO:0000305|PubMed:31753489" FT SITE 85 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:15233621" FT CARBOHYD 47 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000269|PubMed:15233621" FT CONFLICT 49 FT /note="S -> E (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="K -> E (in Ref. 1; AA sequence and 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="E -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="E -> N (in Ref. 1; AA sequence and 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 64 FT /note="F -> L (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 69..75 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 78..83 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 110..128 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 137..145 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 170..181 FT /evidence="ECO:0007829|PDB:6L4C" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 205..212 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 216..222 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:6L4C" FT TURN 238..242 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 271..274 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 295..302 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 306..315 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 317..325 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 327..336 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 344..350 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 355..358 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 374..382 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:6L4C" FT TURN 397..400 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 403..410 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 414..417 FT /evidence="ECO:0007829|PDB:6L4C" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:6L4C" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:6L4C" SQ SEQUENCE 448 AA; 50856 MW; D748661592AA55F0 CRC64; MLPKEDPELK KCKHKCRDER QFDEQQRRDG KQICEEKARE RQQEEGNSSE ESYGKEQEEN PYVFQDEHFE SRVKTEEGRV QVLENFTKRS RLLSGIENFR LAILEANPHT FISPAHFDAE LVLFVAKGRA TITMVREEKR ESFNVEHGDI IRIPAGTPVY MINRDENEKL FIVKILQPVS APGHFEAFYG AGGEDPESFY RAFSWEVLEA ALKVRREQLE KVFGEQSKGS IVKASREKIR ALSQHEEGPP RIWPFGGESS GPINLLHKHP SQSNQFGRLY EAHPDDHKQL QDLDLMVSFA NITKGSMAGP YYNSRATKIS VVVEGEGFFE MACPHLSSSS GSYQKISARL RRGVVFVAPA GHPVAVIASQ NNNLQVLCFE VNAHGNSRFP LAGKGNIVNE FERDAKELAF NLPSREVERI FKNQDQAFFF PGPNKQQEEG GRGGRAFE //