ID 13S3_FAGES Reviewed; 538 AA. AC Q9XFM4; Q9M641; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 02-SEP-2026, entry version 86. DE RecName: Full=13S globulin seed storage protein 3; DE AltName: Full=Legumin-like protein 3; DE AltName: Allergen=Fag e 1; DE Contains: DE RecName: Full=13S globulin seed storage protein 3 acidic chain; DE Contains: DE RecName: Full=13S globulin seed storage protein 3 basic chain; DE Flags: Precursor; GN Name=FAGAG1; OS Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Miyazaki zairai; RA Nair A., Ohmoto T., Woo S.H., Adachi T.; RT "A molecular-genetic approach for hypoallergenic buckwheat."; RL Fagopyrum 16:29-36(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 348-538. RX PubMed=12806007; DOI=10.1100/tsw.2002.157; RA Nair A., Adachi T.; RT "Screening and selection of hypoallergenic buckwheat species."; RL ScientificWorldJournal 2:818-826(2002). CC -!- FUNCTION: Seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic CC chain derived from a single precursor and linked by a disulfide bond. CC {ECO:0000250}. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; AF152003; AAD32713.1; -; mRNA. DR EMBL; AF216801; AAF34635.1; -; Genomic_DNA. DR AlphaFoldDB; Q9XFM4; -. DR SMR; Q9XFM4; -. DR Allergome; 698; Fag e 1. DR GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro. DR CDD; cd02243; cupin_11S_legumin_C; 1. DR CDD; cd02242; cupin_11S_legumin_N; 1. DR FunFam; 2.60.120.10:FF:000073; Glycinin G1; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 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 InterPro; IPR050253; Seed_Storage-Functional. DR PANTHER; PTHR31189:SF76; 11S GLOBULIN SUBUNIT BETA-LIKE; 1. DR PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR SMART; SM00835; Cupin_1; 2. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 1: Evidence at protein level; KW Allergen; Disulfide bond; Seed storage protein; Signal; Storage protein. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..347 FT /note="13S globulin seed storage protein 3 acidic chain" FT /evidence="ECO:0000250" FT /id="PRO_0000032007" FT CHAIN 348..538 FT /note="13S globulin seed storage protein 3 basic chain" FT /evidence="ECO:0000250" FT /id="PRO_0000032008" FT DOMAIN 49..301 FT /note="Cupin type-1 1" FT /evidence="ECO:0000255" FT DOMAIN 360..509 FT /note="Cupin type-1 2" FT /evidence="ECO:0000255" FT REGION 125..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 241..272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 326..346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..194 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..268 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..340 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 44..77 FT /evidence="ECO:0000250" FT DISULFID 120..354 FT /note="Interchain (between acidic and basic chains)" FT /evidence="ECO:0000255" SQ SEQUENCE 538 AA; 61164 MW; 41D6BA55220CFDAC CRC64; MSTKLILSFS LCLMVLSCSA QLLPWQKGQR SRPHHGHQQF QHQCDIQRLT ASEPSRRVRS EAGVTEIWDH DTPEFRCAGF VAVRVVIQPG GLLLPSYSNA PYITFVEQGR GVQGVVVPGC PETFQSGSEF EYPRSQRDQR SRQSESGESS RGDQRSRQSE SEESSRGDQR SRQSESEEFS RGDQHQKIFR IRDGDVIPSP AGVVQWTHNN GDNDLISITL YDANSFQNQL DENVRNFFLA GQSKQSREDR RSQRQTREEG SDRQSRESQD DEALLEANIL SGFEDEILQE IFRNVDQETI SKLRGENDQR GFIVQARDLK LRVPEEYEEE LQRERGDRKR GGSGRSNGLE QAFCNLKFRQ NVNRPSRADV FNPRAGRINT VDSNNLPILE FIQLSAQHVV LYKNAILGPR WNLNAHSALY VTRGEGRVQV VGDEGRSVFD DNVQRGQILV VPQGFAVVLK AGREGLEWVE LKNDDNAITS PIAGKTSVLR AIPVEVLANS YDISTKEAFR LKNGRQEVEV FRPFQSRDEK ERERFSIV //