ID   7SBG2_SOYBN             Reviewed;         433 AA.
AC   Q8RVH5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Basic 7S globulin 2;
DE   AltName: Full=SBg7S;
DE            Short=Bg;
DE   Contains:
DE     RecName: Full=Basic 7S globulin 2 high kDa subunit;
DE   Contains:
DE     RecName: Full=Basic 7S globulin 2 low kDa subunit;
DE   Flags: Precursor;
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RA   Ishizu Y., Sassa H., Hirano H.;
RT   "Sequence of a cDNA encoding soybean basic 7S globulin isoform.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-59 AND 283-311.
RX   PubMed=2064630;
RA   Barbashov S.F., Egorov T.S.A., Kochkina V.M.;
RT   "Isolation and characteristics of insulin-binding proteins from soybeans.";
RL   Bioorg. Khim. 17:421-423(1991).
CC   -!- FUNCTION: Seed storage protein. Has a protein kinase activity. Binds
CC       leginsulin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The mature protein consists of high- and low-kDa subunits
CC       linked by disulfide bonds.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB084260; BAB91077.1; -; mRNA.
DR   RefSeq; NP_001237167.1; NM_001250238.1.
DR   AlphaFoldDB; Q8RVH5; -.
DR   SMR; Q8RVH5; -.
DR   STRING; 3847.GLYMA19G42490.1; -.
DR   PRIDE; Q8RVH5; -.
DR   EnsemblPlants; KRG96855; KRG96855; GLYMA_19G236600.
DR   GeneID; 547485; -.
DR   Gramene; KRG96855; KRG96855; GLYMA_19G236600.
DR   KEGG; gmx:547485; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_032185_0_0_1; -.
DR   InParanoid; Q8RVH5; -.
DR   OrthoDB; 536577at2759; -.
DR   Proteomes; UP000008827; Chromosome 19.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Reference proteome;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:2064630"
FT   CHAIN           25..433
FT                   /note="Basic 7S globulin 2"
FT                   /id="PRO_0000032201"
FT   CHAIN           25..282
FT                   /note="Basic 7S globulin 2 high kDa subunit"
FT                   /id="PRO_0000032202"
FT   CHAIN           283..433
FT                   /note="Basic 7S globulin 2 low kDa subunit"
FT                   /id="PRO_0000032203"
FT   DOMAIN          54..413
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CONFLICT        31
FT                   /note="H -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="A -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="N -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="G -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290..291
FT                   /note="GG -> CC (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="F -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   433 AA;  47205 MW;  FA41B93D8BD3EA38 CRC64;
     MASILHYFLA LSLSFSFLFF LSDSVPIPQH HTNPTKPINL LVLPVQNDAS TGLHWANLQK
     RTPLMQVPVL VDLNGNHLWV NCEQHYSSKT YQAPFCHSTQ CSRANTHQCL SCPAASRPGC
     HKNTCGLMST NPITQQTGLG ELGQDVLAIH ATQGSTQQLG PLVTVPQFLF SCAPSFLLQK
     GLPRNIQGVA GLGHAPISLP NQLASHFGLQ HQFTTCLSRY PTSKGALIFG DAPNNMQQFH
     NQDIFHDLAF TPLTVTPQGE YNVRVSSIRI NQHSVFPPNK ISSTIVGSSG GTMISTSTPH
     MVLQQSLYQA FTQVFAQQLE KQAQVKSVAP FGLCFNSNKI NAYPSVDLVM DKPNGPVWRI
     SGEDLMVQAQ PGVTCLGVMN GGMQPRAEVT LGTRQLEEKL MVFDLARSRV GFSTSSLHSH
     GVKCGDLFNF ANA