ANAO2_ANAOC
ID ANAO2_ANAOC Reviewed; 457 AA.
AC Q8GZP6;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=11S globulin seed storage protein Ana o 2.0101 {ECO:0000305};
DE AltName: Full=11S globulin Ana o 2 {ECO:0000303|PubMed:20362336, ECO:0000303|PubMed:21861454, ECO:0000303|PubMed:23681851, ECO:0000303|PubMed:26769082};
DE AltName: Full=Allergen Ana o 2 {ECO:0000303|PubMed:14555856, ECO:0000303|PubMed:18795784, ECO:0000303|PubMed:20362336, ECO:0000312|EMBL:AAN76862.1};
DE AltName: Full=Anacardein {ECO:0000303|PubMed:18795784, ECO:0000303|PubMed:20362336, ECO:0000303|PubMed:21138244};
DE AltName: Full=Cashew major protein {ECO:0000303|PubMed:18795784};
DE Short=CMP {ECO:0000303|PubMed:18795784};
DE AltName: Full=Legumin Ana o 2 {ECO:0000303|PubMed:18558706, ECO:0000303|PubMed:20362336, ECO:0000303|PubMed:28959544};
DE AltName: Full=Legumin-like protein Ana o 2 {ECO:0000303|PubMed:14555856};
DE AltName: Allergen=Ana o 2.0101 {ECO:0000305};
DE Contains:
DE RecName: Full=11S globulin seed storage protein Ana o 2.0101 acidic chain {ECO:0000305};
DE AltName: Full=11S globulin seed storage protein Ana o 2.0101 large subunit {ECO:0000305};
DE Contains:
DE RecName: Full=11S globulin seed storage protein Ana o 2.0101 basic chain {ECO:0000305};
DE AltName: Full=11S globulin seed storage protein Ana o 2.0101 small subunit {ECO:0000305};
DE Flags: Precursor; Fragment;
OS Anacardium occidentale (Cashew).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Anacardiaceae; Anacardium.
OX NCBI_TaxID=171929 {ECO:0000312|EMBL:AAN76862.1};
RN [1] {ECO:0000312|EMBL:AAN76862.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP ALLERGEN, AND REGIONS.
RC TISSUE=Seed {ECO:0000303|PubMed:14555856};
RX PubMed=14555856; DOI=10.1159/000073262;
RA Wang F., Robotham J.M., Teuber S.S., Sathe S.K., Roux K.H.;
RT "Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the
RT legumin family.";
RL Int. Arch. Allergy Immunol. 132:27-39(2003).
RN [2]
RP PROTEIN SEQUENCE OF 16-58; 57-66; 65-113 AND 129-175, IDENTIFICATION BY
RP MASS SPECTROMETRY, TISSUE SPECIFICITY, PTM, AND ALLERGEN.
RX PubMed=24926808; DOI=10.1021/jf501117p;
RA Mattison C.P., Desormeaux W.A., Wasserman R.L., Yoshioka-Tarver M.,
RA Condon B., Grimm C.C.;
RT "Decreased immunoglobulin E (IgE) binding to cashew allergens following
RT sodium sulfite treatment and heating.";
RL J. Agric. Food Chem. 62:6746-6755(2014).
RN [3]
RP PROTEIN SEQUENCE OF 30-65; 113-125; 175-217; 184-217; 282-322; 302-314;
RP 328-384; 348-360; 368-384; 387-429 AND 410-429, IDENTIFICATION BY MASS
RP SPECTROMETRY, TISSUE SPECIFICITY, PTM, AND ALLERGEN.
RX PubMed=26769082; DOI=10.1021/acs.jafc.5b04401;
RA Reitsma M., Bastiaan-Net S., Sforza S., van der Valk J.P.,
RA van Gerth van Wijk R., Savelkoul H.F., de Jong N.W., Wichers H.J.;
RT "Purification and Characterization of Anacardium occidentale (Cashew)
RT Allergens Ana o 1, Ana o 2, and Ana o 3.";
RL J. Agric. Food Chem. 64:1191-1201(2016).
RN [4]
RP PROTEIN SEQUENCE OF 30-57; 39-57; 175-183; 198-217; 282-291; 292-301;
RP 369-383 AND 390-396, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE
RP SPECIFICITY.
RX PubMed=28959544; DOI=10.1016/j.toxrep.2015.12.009;
RA Mattison C.P., Bren-Mattison Y., Vant-Hull B., Vargas A.M., Wasserman R.L.,
RA Grimm C.C.;
RT "Heat-induced alterations in cashew allergen solubility and IgE binding.";
RL Toxicol. Rep. 3:244-251(2016).
RN [5]
RP PROTEIN SEQUENCE OF 41-55, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=21138244; DOI=10.1021/jf1030899;
RA Kshirsagar H.H., Fajer P., Sharma G.M., Roux K.H., Sathe S.K.;
RT "Biochemical and spectroscopic characterization of almond and cashew nut
RT seed 11S legumins, amandin and anacardein.";
RL J. Agric. Food Chem. 59:386-393(2011).
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ALLERGEN.
RX PubMed=18558706; DOI=10.1021/jf8011618;
RA Comstock S.S., Robotham J.M., Tawde P., Kshirsagar H., Sathe S.K.,
RA Roux K.H., Teuber S.S.;
RT "Immunoglobulin E-reactive proteins in cashew (Anacardium occidentale)
RT apple juice concentrate.";
RL J. Agric. Food Chem. 56:5977-5982(2008).
RN [7]
RP TISSUE SPECIFICITY, ALLERGEN, AND REGION.
RX PubMed=18795784; DOI=10.1021/jf801199q;
RA Venkatachalam M., Monaghan E.K., Kshirsagar H.H., Robotham J.M.,
RA O'Donnell S.E., Gerber M.S., Roux K.H., Sathe S.K.;
RT "Effects of processing on immunoreactivity of cashew nut (Anacardium
RT occidentale L.) seed flour proteins.";
RL J. Agric. Food Chem. 56:8998-9005(2008).
RN [8]
RP SUBUNIT, 3D-STRUCTURE MODELING, REGION, SITE, AND MUTAGENESIS OF GLU-34;
RP ASP-36; ARG-38; VAL-39; GLU-40; GLU-42; ASP-50; ASN-52; HIS-53; GLU-54 AND
RP ARG-57.
RX PubMed=20362338; DOI=10.1016/j.molimm.2010.01.018;
RA Xia L., Willison L.N., Porter L., Robotham J.M., Teuber S.S., Sathe S.K.,
RA Roux K.H.;
RT "Mapping of a conformational epitope on the cashew allergen Ana o 2: a
RT discontinuous large subunit epitope dependent upon homologous or
RT heterologous small subunit association.";
RL Mol. Immunol. 47:1808-1816(2010).
RN [9]
RP TISSUE SPECIFICITY, PTM, AND ALLERGEN.
RX PubMed=20362336; DOI=10.1016/j.molimm.2009.12.009;
RA Robotham J.M., Xia L., Willison L.N., Teuber S.S., Sathe S.K., Roux K.H.;
RT "Characterization of a cashew allergen, 11S globulin (Ana o 2),
RT conformational epitope.";
RL Mol. Immunol. 47:1830-1838(2010).
RN [10]
RP SUBUNIT, 3D-STRUCTURE MODELING, AND REGIONS.
RX PubMed=21861454; DOI=10.1021/ac201501z;
RA Zhang Q., Willison L.N., Tripathi P., Sathe S.K., Roux K.H., Emmett M.R.,
RA Blakney G.T., Zhang H.M., Marshall A.G.;
RT "Epitope mapping of a 95 kDa antigen in complex with antibody by solution-
RT phase amide backbone hydrogen/deuterium exchange monitored by Fourier
RT transform ion cyclotron resonance mass spectrometry.";
RL Anal. Chem. 83:7129-7136(2011).
RN [11]
RP 3D-STRUCTURE MODELING, AND REGIONS.
RX PubMed=23681851; DOI=10.1007/s13361-013-0644-7;
RA Zhang Q., Noble K.A., Mao Y., Young N.L., Sathe S.K., Roux K.H.,
RA Marshall A.G.;
RT "Rapid screening for potential epitopes reactive with a polycolonal
RT antibody by solution-phase H/D exchange monitored by FT-ICR mass
RT spectrometry.";
RL J. Am. Soc. Mass Spectrom. 24:1016-1025(2013).
RN [12]
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=25766831; DOI=10.1016/j.foodchem.2015.02.056;
RA Chung S.Y., Mattison C.P., Reed S., Wasserman R.L., Desormeaux W.A.;
RT "Treatment with oleic acid reduces IgE binding to peanut and cashew
RT allergens.";
RL Food Chem. 180:295-300(2015).
RN [13]
RP ALLERGEN, AND REGIONS.
RX PubMed=27129138; DOI=10.1111/cea.12746;
RA Archila L.D., Chow I.T., McGinty J.W., Renand A., Jeong D., Robinson D.,
RA Farrington M.L., Kwok W.W.;
RT "Ana o 1 and Ana o 2 cashew allergens share cross-reactive CD4(+) T cell
RT epitopes with other tree nuts.";
RL Clin. Exp. Allergy 46:871-883(2016).
RN [14]
RP TISSUE SPECIFICITY, ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=27513566; DOI=10.1111/cea.12794;
RA van der Valk J.P., Gerth van Wijk R., Vergouwe Y., Steyerberg E.W.,
RA Reitsma M., Wichers H.J., Savelkoul H.F., Vlieg-Boerstra B., de Groot H.,
RA Dubois A.E., de Jong N.W.;
RT "sIgE Ana o 1, 2 and 3 accurately distinguish tolerant from allergic
RT children sensitized to cashew nuts.";
RL Clin. Exp. Allergy 47:113-120(2017).
CC -!- FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681,
CC ECO:0000305|PubMed:14555856, ECO:0000305|PubMed:18558706,
CC ECO:0000305|PubMed:18795784, ECO:0000305|PubMed:20362336,
CC ECO:0000305|PubMed:21138244, ECO:0000305|PubMed:24926808,
CC ECO:0000305|PubMed:25766831, ECO:0000305|PubMed:26769082,
CC ECO:0000305|PubMed:27513566, ECO:0000305|PubMed:28959544}.
CC -!- SUBUNIT: Homotrimer (PubMed:21861454). Hexamer (PubMed:20362338). Each
CC subunit is composed of an acidic and a basic chain derived from a
CC single precursor and linked by a disulfide bond (By similarity).
CC {ECO:0000250|UniProtKB:P04776, ECO:0000269|PubMed:20362338,
CC ECO:0000269|PubMed:21861454}.
CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level)
CC (PubMed:14555856, PubMed:18558706, PubMed:18795784, PubMed:20362336,
CC PubMed:21138244, PubMed:25766831, PubMed:26769082, PubMed:24926808,
CC PubMed:28959544, PubMed:27513566). Expressed in the juice of the cashew
CC apple (at protein level) (PubMed:18558706).
CC {ECO:0000269|PubMed:14555856, ECO:0000269|PubMed:18558706,
CC ECO:0000269|PubMed:18795784, ECO:0000269|PubMed:20362336,
CC ECO:0000269|PubMed:21138244, ECO:0000269|PubMed:24926808,
CC ECO:0000269|PubMed:25766831, ECO:0000269|PubMed:26769082,
CC ECO:0000269|PubMed:27513566, ECO:0000269|PubMed:28959544}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation
CC (PubMed:14555856). Expressed in mature raw cashew nut (PubMed:18558706,
CC PubMed:21138244). {ECO:0000269|PubMed:14555856,
CC ECO:0000269|PubMed:18558706, ECO:0000269|PubMed:21138244}.
CC -!- PTM: Proteolytically processed from a single precursor to produce an
CC acidic and a basic chain that are linked by a disulfide bond
CC (PubMed:14555856, PubMed:20362336, PubMed:24926808, PubMed:26769082).
CC Not glycosylated (PubMed:26769082). {ECO:0000269|PubMed:20362336,
CC ECO:0000269|PubMed:24926808, ECO:0000269|PubMed:26769082,
CC ECO:0000305|PubMed:14555856}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:14555856,
CC PubMed:18558706, PubMed:20362336, PubMed:24926808, PubMed:25766831,
CC PubMed:27129138, PubMed:26769082, PubMed:27513566). Binds to IgE of
CC patients allergic to cashew nuts (PubMed:14555856, PubMed:18558706,
CC PubMed:20362336, PubMed:24926808, PubMed:25766831, PubMed:26769082,
CC PubMed:27513566). Recombinant protein binds to IgE in 62% of the 21
CC patients tested (PubMed:14555856). Reduced IgE-binding following 50 mM
CC sodium sulfite treatment at 100 degrees Celsius or by 5 mM
CC dithiothreitol (DTT) (PubMed:24926808). IgE-binding is reduced by 35%
CC with 5 mM sodium oleate treatment at 70 degrees Celsius for 60 min only
CC if followed by an additional overnight incubation at 37 degrees Celsius
CC (PubMed:25766831). Allergenicity is removed from the cashew apple juice
CC concentrate by 5 kDa filtration (PubMed:18558706). Retains
CC immunoreactivity for mouse monoclonal antibodies (mAbs) 4C3 and 4H9
CC after a variety of processing treatments including autoclaving,
CC blanching, microwave heating, dry roasting, gamma-irradiation and pH
CC (PubMed:18795784). Significantly reduced immunoreactivity for mouse mAb
CC 4C3 by 2.5 mM sodium dodecyl sulfate (SDS) or 2% v/v reducing agent
CC beta-mercaptoethanol (beta-ME) with heat (100 degrees Celsius for 10
CC min) treatments (PubMed:21138244). Exposure to extreme pH (1 or 13) and
CC extreme heat treatments (autoclaving for 30 min or roasting at 200
CC degrees Celsius for 15 min) results in almost complete loss of binding
CC to mouse mAb 4C3 (PubMed:18795784). Mouse mAb 2B5 recognizes a
CC conformational epitope on the acidic chain of this protein, the
CC recognition of which requires the association of the basic chain, but
CC is independent of their post-translational cleavage. The antibody
CC competes with patient IgE for binding to the epitope. The epitope is
CC destroyed by physical (boiling) and chemical (0.5 M beta-ME, 10% SDS
CC and 6 M urea) denturation (PubMed:20362336). Cashew allergic patients
CC elicit responses to this protein by CD4(+) T cells with T-helper 2
CC (Th2) and Th2/T-helper 17 (Th17) phenotypes (PubMed:27129138).
CC {ECO:0000269|PubMed:14555856, ECO:0000269|PubMed:18558706,
CC ECO:0000269|PubMed:18795784, ECO:0000269|PubMed:20362336,
CC ECO:0000269|PubMed:21138244, ECO:0000269|PubMed:24926808,
CC ECO:0000269|PubMed:25766831, ECO:0000269|PubMed:26769082,
CC ECO:0000269|PubMed:27129138, ECO:0000269|PubMed:27513566}.
CC -!- BIOTECHNOLOGY: Can be used as part of the diagnostics for predicting
CC the risk for positive double-blind, placebo-controlled food challenge
CC test (DBPCFC) in cashew-allergic children. The risk increases with
CC higher specific IgE levels to this protein.
CC {ECO:0000269|PubMed:27513566}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000255|RuleBase:RU003681, ECO:0000305}.
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DR EMBL; AF453947; AAN76862.1; -; mRNA.
DR AlphaFoldDB; Q8GZP6; -.
DR SMR; Q8GZP6; -.
DR Allergome; 3077; Ana o 2.0101.
DR Allergome; 976; Ana o 2.
DR PRIDE; Q8GZP6; -.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR022379; 11S_seedstore_CS.
DR InterPro; IPR006044; 11S_seedstore_pln.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR PRINTS; PR00439; 11SGLOBULIN.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; IgE-binding protein;
KW IgG-binding protein; Seed storage protein; Signal; Storage protein.
FT SIGNAL <1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..271
FT /note="11S globulin seed storage protein Ana o 2.0101
FT acidic chain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:14555856,
FT ECO:0000305|PubMed:20362336"
FT /id="PRO_0000448659"
FT CHAIN 272..457
FT /note="11S globulin seed storage protein Ana o 2.0101 basic
FT chain"
FT /evidence="ECO:0000305|PubMed:14555856,
FT ECO:0000305|PubMed:20362336"
FT /id="PRO_0000448660"
FT DOMAIN 30..220
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 284..433
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 15..29
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:14555856"
FT REGION 29..37
FT /note="Conformational epitope; mouse monoclonal antibody
FT (mAb) 2B5-binding"
FT /evidence="ECO:0000269|PubMed:21861454"
FT REGION 31..48
FT /note="Conformational epitope; mouse monoclonal antibody
FT (mAb) 2B5-binding"
FT /evidence="ECO:0000269|PubMed:21861454"
FT REGION 32..45
FT /note="Binds goat polyclonal antibodies (pAbs)"
FT /evidence="ECO:0000269|PubMed:23681851"
FT REGION 34..57
FT /note="Mouse monoclonal antibody (mAb) 2B5-binding"
FT /evidence="ECO:0000269|PubMed:20362338"
FT REGION 41..55
FT /note="Mouse monoclonal antibody (mAb) 4H9-binding"
FT /evidence="ECO:0000269|PubMed:18795784"
FT REGION 55..86
FT /note="Binds goat polyclonal antibodies (pAbs)"
FT /evidence="ECO:0000269|PubMed:23681851"
FT REGION 105..119
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:14555856"
FT REGION 215..239
FT /note="Binds goat polyclonal antibodies (pAbs)"
FT /evidence="ECO:0000269|PubMed:23681851"
FT REGION 233..252
FT /note="CD4(+) T cell-reactive epitope"
FT /evidence="ECO:0000269|PubMed:27129138"
FT REGION 243..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..289
FT /note="Linear epitope; mouse monoclonal antibody (mAb) 1F5-
FT binding"
FT /evidence="ECO:0000269|PubMed:21861454"
FT REGION 289..308
FT /note="CD4(+) T cell-reactive epitope"
FT /evidence="ECO:0000269|PubMed:27129138"
FT REGION 297..316
FT /note="CD4(+) T cell-reactive epitope"
FT /evidence="ECO:0000269|PubMed:27129138"
FT REGION 321..340
FT /note="CD4(+) T cell-reactive epitope"
FT /evidence="ECO:0000269|PubMed:27129138"
FT REGION 329..348
FT /note="CD4(+) T cell-reactive epitope"
FT /evidence="ECO:0000269|PubMed:27129138"
FT REGION 377..396
FT /note="CD4(+) T cell-reactive epitope"
FT /evidence="ECO:0000269|PubMed:27129138"
FT REGION 395..416
FT /note="Binds goat polyclonal antibodies (pAbs), but buried
FT in the 3D-structure model"
FT /evidence="ECO:0000269|PubMed:23681851"
FT MOTIF 271..276
FT /note="NGXEET; peptidase recognition motif"
FT /evidence="ECO:0000250|UniProtKB:Q2TPW5"
FT SITE 34
FT /note="Critical for epitope recognition by the mouse
FT monoclonal antibody (mAb) 2B5"
FT /evidence="ECO:0000269|PubMed:20362338"
FT DISULFID 25..58
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT DISULFID 101..278
FT /note="Interchain (between acidic and basic chains)"
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT MUTAGEN 34
FT /note="E->A: Significantly reduced binding to mouse
FT monoclonal antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 36
FT /note="D->A: Loss of binding to mouse monoclonal antibody
FT (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 38
FT /note="R->A: Loss of binding to mouse monoclonal antibody
FT (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 39
FT /note="V->A: Significantly reduced binding to mouse
FT monoclonal antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 40
FT /note="E->A: Significantly reduced binding to mouse
FT monoclonal antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 42
FT /note="E->A: Significantly reduced binding to mouse
FT monoclonal antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 50
FT /note="D->A: Loss of binding to mouse monoclonal antibody
FT (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 52
FT /note="N->A: No effect in binding to mouse monoclonal
FT antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 53
FT /note="H->A: Significantly reduced binding to mouse
FT monoclonal antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 54
FT /note="E->A: No effect in binding to mouse monoclonal
FT antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT MUTAGEN 57
FT /note="R->A: Significantly reduced binding to mouse
FT monoclonal antibody (mAb) 2B5."
FT /evidence="ECO:0000269|PubMed:20362338"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAN76862.1"
SQ SEQUENCE 457 AA; 51996 MW; 91413A7A10E6419C CRC64;
LSVCFLILFH GCLASRQEWQ QQDECQIDRL DALEPDNRVE YEAGTVEAWD PNHEQFRCAG
VALVRHTIQP NGLLLPQYSN APQLIYVVQG EGMTGISYPG CPETYQAPQQ GRQQGQSGRF
QDRHQKIRRF RRGDIIAIPA GVAHWCYNEG NSPVVTVTLL DVSNSQNQLD RTPRKFHLAG
NPKDVFQQQQ QHQSRGRNLF SGFDTELLAE AFQVDERLIK QLKSEDNRGG IVKVKDDELR
VIRPSRSQSE RGSESEEESE DEKRRWGQRD NGIEETICTM RLKENINDPA RADIYTPEVG
RLTTLNSLNL PILKWLQLSV EKGVLYKNAL VLPHWNLNSH SIIYGCKGKG QVQVVDNFGN
RVFDGEVREG QMLVVPQNFA VVKRAREERF EWISFKTNDR AMTSPLAGRT SVLGGMPEEV
LANAFQISRE DARKIKFNNQ QTTLTSGESS HHMRDDA
