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LEGA2_PEA
ID   LEGA2_PEA               Reviewed;         520 AA.
AC   P15838;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Legumin A2;
DE   Contains:
DE     RecName: Full=Legumin A2 alpha chain;
DE     AltName: Full=Legumin A2 acidic chain;
DE   Contains:
DE     RecName: Full=Legumin A2 beta chain;
DE     AltName: Full=Legumin A2 basic chain;
DE   Flags: Precursor;
GN   Name=LEGA2;
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. Greenfeast;
RX   PubMed=2308850; DOI=10.1093/nar/18.3.655;
RA   Rerie W.G., Whitecross M.I., Higgins T.J.V.;
RT   "Nucleotide sequence of an A-type legumin gene from pea.";
RL   Nucleic Acids Res. 18:655-655(1990).
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; X17193; CAA35056.1; -; Genomic_DNA.
DR   PIR; S08237; S08237.
DR   AlphaFoldDB; P15838; -.
DR   SMR; P15838; -.
DR   PRIDE; P15838; -.
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; 2.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..335
FT                   /note="Legumin A2 alpha chain"
FT                   /id="PRO_0000032068"
FT   CHAIN           336..520
FT                   /note="Legumin A2 beta chain"
FT                   /id="PRO_0000032069"
FT   DOMAIN          37..233
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          348..497
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          250..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        32..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..342
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   520 AA;  59270 MW;  CDB8B5E350C760C6 CRC64;
     MATKLLALSL SFCFLLLGGC FALREQPEQN ECQLERLNAL EPDNRIESEG GLIETWNPNN
     KQFRCAGVAL SRATLQHNAL RRPYYSNAPQ EIFIQQGNGY FGMVFPGCPE TFEEPQESEQ
     GEGRRYRDRH QKVNRFREGD IIAVPTGIVF WMYNDQDTPV IAVSLTDIRS SNNQLDQMPR
     RFYLAGNHEQ EFLRYQHQQG GKQEQENEGN NIFSGFKRDF LEDAFNVNRH IVDRLQGRNE
     DEEKGAIVKV KGGLSIISPP EKQARHQRGS RQEEDEDEDE ERQPRHQRGS RQEEEEDEDE
     ERQPRHQRRR GEEEEEDKKE RRGSQKGKSR RQGDNGLEET VCTAKLRLNI GPSSSPDIYN
     PEAGRIKTVT SLDLPVLRWL KLSAEHGSLH KNAMFVPHYN LNANSIIYAL KGRARLQVVN
     CNGNTVFDGE LEAGRALTVP QNYAVAAKSL SDRFSYVAFK TNDRAGIARL AGTSSVINNL
     PLDVVAATFN LQRNEARQLK SNNPFKFLVP ARQSENRASA
 
 
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