ID   LEGB_PEA                Reviewed;         338 AA.
AC   P14594;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Legumin B;
DE   Contains:
DE     RecName: Full=Legumin B alpha chain;
DE     AltName: Full=Legumin B acidic chain;
DE   Contains:
DE     RecName: Full=Legumin B beta chain;
DE     AltName: Full=Legumin B basic chain;
DE   Flags: Fragment;
GN   Name=LEGB;
OS   Pisum sativum (Garden pea).
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; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   AGRICOLA=IND87019921; DOI=10.1007/BF00020330;
RA   Domoney C., Barker D., Casey R.;
RT   "The complete deduced amino acid sequences of legumin beta-polypeptides
RT   from different genetic loci in Pisum.";
RL   Plant Mol. Biol. 7:467-474(1986).
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; M16890; AAA33678.1; -; mRNA.
DR   PIR; S04321; S04321.
DR   AlphaFoldDB; P14594; -.
DR   SMR; P14594; -.
DR   PRIDE; P14594; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 3.
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; 1.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Seed storage protein; Storage protein.
FT   CHAIN           <1..161
FT                   /note="Legumin B alpha chain"
FT                   /id="PRO_0000032070"
FT   CHAIN           162..338
FT                   /note="Legumin B beta chain"
FT                   /id="PRO_0000032071"
FT   DOMAIN          174..321
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   REGION          16..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        ?..168
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   338 AA;  38990 MW;  752CFC3D336B6AE0 CRC64;
     GNSVLSGFNV EFLAHSLNTK EDTAKRLRSP QDERGQIVKV EDGLHIISPE LQEEEEQSHS
     QRKEEEEEEQ EQRHRKHSKK EDEDEDEEEE EEREQRHRKH SEKEEEDEDE PRSYETRRKW
     KKHTAEKKRE SHGQGEEEEE LEKEEEEEEE IQRQHSKGRK NGLEETICSA KIRENIARPS
     RGDLYNSGAG RISTVNSLTL PILRNLRLSA EYVLLYRNGI YAPHWNINAN SLLYVIRGEG
     RVRIVNSEGN KVFDDKVSLG QLVVVPQNFV VAQQAGNEEG FEYVVFKTND RAAVSHVNQV
     FRATPGEVLA NAFGLRHSQV AQIKSNGNRG PLVQPQSQ