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VCL_CORAV
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   03-AUG-2022, entry version 56.
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 traces
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 be used
CC       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}.
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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   PRIDE; 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   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; SSF51182; 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
 
 
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