ID   LEGB2_VICFA             Reviewed;         335 AA.
AC   P16078;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Legumin type B;
DE   Contains:
DE     RecName: Full=Legumin type B alpha chain;
DE     AltName: Full=Legumin type B acidic chain;
DE   Contains:
DE     RecName: Full=Legumin type B beta chain;
DE     AltName: Full=Legumin type B basic chain;
DE   Flags: Fragment;
GN   Name=LEB2;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Fribo; TISSUE=Leaf;
RX   PubMed=2491681; DOI=10.1007/bf00016020;
RA   Heim U., Schubert R., Baeumlein H., Wobus U.;
RT   "The legumin gene family: structure and evolutionary implications of Vicia
RT   faba B-type genes and pseudogenes.";
RL   Plant Mol. Biol. 13:653-663(1989).
CC   -!- FUNCTION: This protein found in the seeds of many leguminous and non-
CC       leguminous plants is the source of sulfur-containing amino acids in
CC       seed meals.
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   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000305}.
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DR   EMBL; X14237; CAA32454.1; -; Genomic_DNA.
DR   PIR; S07576; S07576.
DR   AlphaFoldDB; P16078; -.
DR   SMR; P16078; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
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; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Seed storage protein; Storage protein.
FT   CHAIN           <1..154
FT                   /note="Legumin type B alpha chain"
FT                   /id="PRO_0000032076"
FT   CHAIN           155..335
FT                   /note="Legumin type B beta chain"
FT                   /id="PRO_0000032077"
FT   DOMAIN          167..314
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   REGION          47..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        ?..161
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   335 AA;  37820 MW;  2853CF90F6C30C27 CRC64;
     GIPYWTYNNG DEPLVAISLL DTSNIANQLD STPRVFYLGG NPEVEFPETQ EEQQERHQQK
     HSLPVGRRGG QHQQEEESEE QKDGNSVLSG FSSEFLAQTF NTEEDTAKRL RSPRDKRNQI
     VRVEGGLRII NPEGQQEEEE EEEEEKQRSE QGRNGLEETI CSLKIRENIA QPARADLYNP
     RAGSISTANS LTLPILRYLR LSAEYVRLYR NGIYAPHWNI NANSLLYVIR GEGRVRIVNS
     QGNAVFDNKV RKGQLVVVPQ NFVVAEQAGE EEGLEYLVFK TNDRAAVSHV QQVFRATPAD
     VLANAFGLRQ RQVTELKLSG NRGPLVHPQS QSQSN