ID   LEGK_PEA                Reviewed;         350 AA.
AC   P05693;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Legumin K;
DE   Contains:
DE     RecName: Full=Legumin K alpha chain;
DE     AltName: Full=Legumin K acidic chain;
DE   Contains:
DE     RecName: Full=Legumin K beta chain;
DE     AltName: Full=Legumin K basic chain;
DE   Flags: Fragment;
GN   Name=LEGK;
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 [GENOMIC DNA].
RC   STRAIN=cv. Dark skinned Perfection;
RX   PubMed=3355508; DOI=10.1042/bj2500015;
RA   Gatehouse J.A., Bown D., Gilroy J., Levasseur M., Castleton J.,
RA   Ellis T.H.N.;
RT   "Two genes encoding 'minor' legumin polypeptides in pea (Pisum sativum L.).
RT   Characterization and complete sequence of the LegJ gene.";
RL   Biochem. J. 250:15-24(1988).
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; X07015; CAA30068.1; -; Genomic_DNA.
DR   PIR; S00337; S00337.
DR   AlphaFoldDB; P05693; -.
DR   SMR; P05693; -.
DR   PRIDE; P05693; -.
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..169
FT                   /note="Legumin K alpha chain"
FT                   /id="PRO_0000032074"
FT   CHAIN           170..350
FT                   /note="Legumin K beta chain"
FT                   /id="PRO_0000032075"
FT   DOMAIN          182..329
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   REGION          37..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        ?..176
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   350 AA;  39800 MW;  A2A5EF901C688732 CRC64;
     IPYWTYNHGD EPLVAISLLD TSNIANQLDS TPRVFYLGGN PETEFPETQE EQQGRHRQKH
     SYPVGRRSGH HQQEEESEEQ NEGNSVLSGV SSEFLAQTFN TEEDTAKRLR SPRDERSQIV
     RVEGGLRIIN PKGKEEEEEK EQSHSHSHRE EEEEEEEDEE KQRSEERKNG LEETICSAKI
     RENIADAAGA DLYNPRAGRI RTANSLTLPV LRYLRLSAEY VRLYRNGIYA PHWNINANSL
     LYVIRGEGRV RIVNFQGDAV FDNKVRKGQL VVVPQNFVVA EQAGEEEGLE YVVFKTNDRA
     AVSHVQQVLR ATPAEVLANA FGLRQRQVTE LKLSGNRGPL VHPQSQSQSH