ID   13SB_FAGES              Reviewed;         194 AA.
AC   P83004;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=13S globulin basic chain;
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 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. BDS-1354; TISSUE=Endosperm;
RX   PubMed=12657290; DOI=10.1016/s0031-9422(02)00755-0;
RA   Bharali S., Chrungoo N.K.;
RT   "Amino acid sequence of the 26 kDa subunit of legumin-type seed storage
RT   protein of common buckwheat (Fagopyrum esculentum Moench): molecular
RT   characterization and phylogenetic analysis.";
RL   Phytochemistry 63:1-5(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-17.
RX   PubMed=9214774; DOI=10.1016/s0031-9422(97)00051-4;
RA   Rout M.K., Chrungoo N.K., Rao K.S.;
RT   "Amino acid sequence of the basic subunit of 13S globulin of buckwheat.";
RL   Phytochemistry 45:865-867(1997).
CC   -!- FUNCTION: Seed storage protein with a relatively high level of Lys and
CC       Met. {ECO:0000269|PubMed:12657290}.
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   -!- TISSUE SPECIFICITY: Cotyledons and endosperm protein bodies.
CC       {ECO:0000269|PubMed:12657290}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83004; -.
DR   SMR; P83004; -.
DR   Allergome; 698; Fag e 1.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
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; 1.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Seed storage protein;
KW   Storage protein.
FT   CHAIN           1..194
FT                   /note="13S globulin basic chain"
FT                   /id="PRO_0000152877"
FT   DOMAIN          13..162
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   DISULFID        7..?
FT                   /note="Interchain (between basic and acidic chains)"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   194 AA;  21847 MW;  65A6FC49AFC1E9D0 CRC64;
     GIDENVCTMK LRENIKSPQE ADFYNPKAGR ITTANSQKLP ALRSLQMSAE RGFLYSNGIY
     APHWNINAHS ALYVTRGNAK VQVVGDEGNK VFDDEVKQGQ LIIVPQYFAV IKKAGNQGFE
     YVAFKTNDNA MINPLVGRLS AFRAIPEEVL RSSFQISSEE AEELKYGRQE ALLLSEQSQQ
     GKREVADEKE RERF