13S_FAGTA
ID 13S_FAGTA Reviewed; 515 AA.
AC A9NJG2; Q8LGR7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=13S globulin seed storage protein {ECO:0000303|PubMed:18980324};
DE AltName: Full=13S globulin {ECO:0000303|PubMed:18980324};
DE AltName: Full=Legumin-like protein {ECO:0000303|PubMed:16717422, ECO:0000303|PubMed:22449541};
DE AltName: Full=Major allergen Fag t 1 {ECO:0000303|PubMed:22449541};
DE AltName: Full=TBt {ECO:0000303|PubMed:18980324, ECO:0000303|PubMed:21571740};
DE AltName: Allergen=Fag t 1 {ECO:0000305};
DE Contains:
DE RecName: Full=13S globulin seed storage protein acidic chain {ECO:0000305};
DE AltName: Full=13S globulin TBb chain {ECO:0000305};
DE AltName: Full=34 kDa allergenic protein {ECO:0000303|PubMed:21571740};
DE AltName: Full=Allergen b {ECO:0000305};
DE AltName: Full=N-terminal subunit TBb {ECO:0000303|PubMed:21571740};
DE AltName: Full=TBb {ECO:0000303|PubMed:18980324, ECO:0000303|PubMed:21571740};
DE Contains:
DE RecName: Full=13S globulin seed storage protein basic chain {ECO:0000305};
DE AltName: Full=13S globulin TBa chain {ECO:0000305};
DE AltName: Full=Allergen a {ECO:0000303|PubMed:16717422};
DE AltName: Full=C-terminal subunit TBa {ECO:0000303|PubMed:21571740};
DE AltName: Full=FTAP {ECO:0000312|EMBL:AAK97787.1};
DE AltName: Full=Major 24 kDa allergenic protein {ECO:0000303|PubMed:15277744, ECO:0000303|PubMed:16717422};
DE AltName: Full=TBa {ECO:0000303|PubMed:16717422, ECO:0000303|PubMed:18980324, ECO:0000303|PubMed:20431913, ECO:0000303|PubMed:21571740};
DE Flags: Precursor;
OS Fagopyrum tataricum (Tartarian buckwheat) (Polygonum tataricum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum.
OX NCBI_TaxID=62330 {ECO:0000312|EMBL:ABI32184.1};
RN [1] {ECO:0000312|EMBL:ABI32184.1}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, ALLERGEN, AND PHYLOGENETIC
RP ANALYSIS.
RC TISSUE=Immature seed {ECO:0000303|PubMed:18980324};
RX PubMed=18980324; DOI=10.1021/jf801855a;
RA Zhang X., Yuan J.M., Cui X.D., Wang Z.H.;
RT "Molecular cloning, recombinant expression, and immunological
RT characterization of a novel allergen from tartary buckwheat.";
RL J. Agric. Food Chem. 56:10947-10953(2008).
RN [2] {ECO:0000312|EMBL:AAK97787.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 321-515, DEVELOPMENTAL STAGE, AND ALLERGEN.
RC TISSUE=Radicle {ECO:0000303|PubMed:16717422};
RX PubMed=16717422; DOI=10.1271/bbb.70.1195;
RA Wang Z., Wang L., Chang W., Li Y., Zhang Z., Wieslander G., Norback D.;
RT "Cloning, expression, and identification of immunological activity of an
RT allergenic protein in tartary buckwheat.";
RL Biosci. Biotechnol. Biochem. 70:1195-1199(2006).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=15277744; DOI=10.1271/bbb.68.1409;
RA Wang Z., Zhang Z., Zhao Z., Wieslander G., Norbaeck D., Kreft I.;
RT "Purification and characterization of a 24 kDa protein from tartary
RT buckwheat seeds.";
RL Biosci. Biotechnol. Biochem. 68:1409-1413(2004).
RN [4]
RP ALLERGEN, BIOTECHNOLOGY, REGIONS, AND MUTAGENESIS OF LEU-359; LEU-362;
RP LEU-367; VAL-372 AND LEU-374.
RX PubMed=20431913; DOI=10.1007/s10529-010-0281-1;
RA Ren X., Zhang X., Li Y., Wang Z.;
RT "Epitope mapping and immunological characterization of a major allergen TBa
RT in tartary buckwheat.";
RL Biotechnol. Lett. 32:1317-1324(2010).
RN [5]
RP ALLERGEN, BIOTECHNOLOGY, REGIONS, SITE, MUTAGENESIS OF ARG-161; ARG-163 AND
RP ASP-166, AND 3D-STRUCTURE MODELING.
RX PubMed=21571740; DOI=10.1093/abbs/gmr036;
RA Li P., Cui X., Li Y., Wang Z.;
RT "Epitope mapping and identification on a 3D model built for the tartary
RT buckwheat allergic protein TBb.";
RL Acta Biochim. Biophys. Sin. 43:441-447(2011).
RN [6]
RP ALLERGEN, BIOTECHNOLOGY, 3D-STRUCTURE MODELING, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=22449541; DOI=10.1016/j.fct.2012.03.039;
RA Yang Z., Li Y., Li C., Wang Z.;
RT "Synthesis of hypoallergenic derivatives of the major allergen Fag t 1 from
RT tartary buckwheat via sequence restructuring.";
RL Food Chem. Toxicol. 50:2675-2680(2012).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. Loss of stability only after incubation for 1
CC hour at 100 degrees Celsius. {ECO:0000269|PubMed:15277744};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:A0A1L6K371}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level).
CC {ECO:0000269|PubMed:15277744}.
CC -!- DEVELOPMENTAL STAGE: Expressed in immature seeds at 20 days after
CC flowering (PubMed:18980324). Expressed in radicles (PubMed:16717422).
CC {ECO:0000269|PubMed:16717422, ECO:0000269|PubMed:18980324}.
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 {ECO:0000250|UniProtKB:A0A1L6K371}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:18980324,
CC PubMed:16717422, PubMed:15277744, PubMed:20431913, PubMed:21571740,
CC PubMed:22449541). Natural protein binds to IgE in all 5 buckwheat-
CC allergic patients tested. Natural protein is susceptible to digestion
CC with pepsin, but resistant to digestion with trypsin. Recombinant
CC protein binds to IgG of buckwheat-allergic patients (PubMed:22449541).
CC Recombinant full-length protein (rTBt) binds to IgE of patients
CC allergic to buckwheat (PubMed:18980324, PubMed:22449541). Recombinant
CC N-terminal subunit (rTBb) binds to IgE of patients allergic to
CC buckwheat (PubMed:21571740). Recombinant C-terminal subunit (rTBa)
CC binds to IgE of patients allergic to buckwheat (PubMed:18980324,
CC PubMed:16717422, PubMed:20431913). Natural 24 kDa protein binds to IgE
CC of patients allergic to buckwheat (PubMed:15277744). Both the
CC recombinant rTBb and rTBa have higher IgE-binding activity than rTBt
CC (PubMed:18980324). {ECO:0000269|PubMed:15277744,
CC ECO:0000269|PubMed:16717422, ECO:0000269|PubMed:18980324,
CC ECO:0000269|PubMed:20431913, ECO:0000269|PubMed:21571740,
CC ECO:0000269|PubMed:22449541}.
CC -!- BIOTECHNOLOGY: This protein, when mutated, can potentially be
CC applicable to the development of transgenic hypoallergenic crops of
CC tartarian buckwheat and specific immunotherapy to treat tartarian
CC buckwheat allergy (PubMed:20431913, PubMed:21571740). Destructing the
CC native conformation of this protein significantly reduces its
CC allergenicity and it may be a candidate for the development of vaccine
CC that builds immunotolerance in individuals with buckwheat allergy.
CC Production of mosaic molecules which are reassembled derivatives of the
CC protein may have advantages compared to production of modified
CC fragments. The treatment can be achieved with a single molecule that is
CC more stable and easier to produce and purify. The production is also
CC more cost-effective than with chemically modified allergens
CC (PubMed:22449541). {ECO:0000269|PubMed:20431913,
CC ECO:0000269|PubMed:21571740, ECO:0000269|PubMed:22449541}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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DR EMBL; DQ849083; ABI32184.1; -; mRNA.
DR EMBL; AY044918; AAK97787.1; -; mRNA.
DR SMR; A9NJG2; -.
DR Allergome; 1534; Fag t 1.
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; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
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.
PE 1: Evidence at protein level;
KW Allergen; Disulfide bond; IgE-binding protein; IgG-binding protein;
KW Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..515
FT /note="13S globulin seed storage protein"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18980324"
FT /id="PRO_5002741086"
FT CHAIN 23..320
FT /note="13S globulin seed storage protein acidic chain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18980324,
FT ECO:0000305|PubMed:21571740"
FT /id="PRO_0000455376"
FT CHAIN 321..515
FT /note="13S globulin seed storage protein basic chain"
FT /evidence="ECO:0000305|PubMed:16717422,
FT ECO:0000305|PubMed:18980324, ECO:0000305|PubMed:20431913"
FT /id="PRO_0000455377"
FT DOMAIN 52..272
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 333..482
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 23..96
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:21571740"
FT REGION 97..172
FT /note="IgE-binding epitope with a very strong IgE-binding
FT activity"
FT /evidence="ECO:0000269|PubMed:21571740"
FT REGION 123..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..248
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:21571740"
FT REGION 210..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..320
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:21571740"
FT REGION 295..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..387
FT /note="IgE-binding epitope with a strong IgE-binding
FT activity"
FT /evidence="ECO:0000269|PubMed:20431913"
FT REGION 407..457
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20431913"
FT REGION 440..476
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20431913"
FT REGION 475..511
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20431913"
FT COMPBIAS 137..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 163
FT /note="Critical for IgE-binding"
FT /evidence="ECO:0000269|PubMed:21571740"
FT DISULFID 47..80
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT DISULFID 123..327
FT /note="Interchain (between acidic and basic chains)"
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT MUTAGEN 161
FT /note="R->A: Decreased IgE-binding to the wild-type epitope
FT 97-L--A-172."
FT /evidence="ECO:0000269|PubMed:21571740"
FT MUTAGEN 163
FT /note="R->A: Significantly decreased IgE-binding to the
FT wild-type epitope 97-L--A-172."
FT /evidence="ECO:0000269|PubMed:21571740"
FT MUTAGEN 166
FT /note="D->A: Decreased IgE-binding to the wild-type epitope
FT 97-L--A-172."
FT /evidence="ECO:0000269|PubMed:21571740"
FT MUTAGEN 359
FT /note="L->R: Decreased IgE-binding to the wild-type epitope
FT 347-R--N-387."
FT /evidence="ECO:0000269|PubMed:20431913"
FT MUTAGEN 362
FT /note="L->R: Significantly decreased IgE-binding to the
FT wild-type epitope 347-R--N-387."
FT /evidence="ECO:0000269|PubMed:20431913"
FT MUTAGEN 367
FT /note="L->R: Significantly decreased IgE-binding to the
FT wild-type epitope 347-R--N-387."
FT /evidence="ECO:0000269|PubMed:20431913"
FT MUTAGEN 372
FT /note="V->R: Decreased IgE-binding to the wild-type epitope
FT 347-R--N-387."
FT /evidence="ECO:0000269|PubMed:20431913"
FT MUTAGEN 374
FT /note="L->R: Significantly decreased IgE-binding to the
FT wild-type epitope 347-R--N-387."
FT /evidence="ECO:0000269|PubMed:20431913"
SQ SEQUENCE 515 AA; 58356 MW; 430FF6864A17CB59 CRC64;
MSTKLILSFS LCLMVLSCSA QAAQLWPWRK GQDSRPHHGH QQFQQQCDIQ RLTASEPSRR
VRSEAGVTEI WDHNTPEFRC TGFVAVRYVI QPGGLLLPSY SNAPYITFVE QGRGVQGVVI
PGCPETFQSD SEYPQSQRGQ HSRESESQES SRGDQHQKIF RVREGDVIPS PAGVVQWTHN
DGDQDLISVT LLDANSFHNQ LDENVRSFFL AGQSQQGREE RRSQQQTREE GGDRQSRESD
DVEALIGANI LSGFQDEILH ELFRDVDRET ISKLRGENDQ RGFIVQAQDL KLRVPEDSEE
GYERQRGDRK RDERGSGRSN GLEQAFCNLK FRQNVNRPSH ADVFNPRAGR INTVNSNNLP
ILEFLQLSAQ HVVLYKNAII GPRWNLNAHS ALYVTRGEGR VQVVGDEGKS VFDDNVQRGQ
ILVVPQGFAV VVKAGRQGLE WVELKNNDNA ITSPIAGRTS VLRAIPVEVL ANSYDISTEE
AYKLKNGRQE VEVFRPFQSR YEKEEEKERE RFSIV
