7SB1_SOYBN
ID 7SB1_SOYBN Reviewed; 427 AA.
AC P13917; Q39901; Q43464;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Basic 7S globulin;
DE AltName: Full=SBg7S;
DE Short=Bg;
DE Contains:
DE RecName: Full=Basic 7S globulin high kDa subunit;
DE Contains:
DE RecName: Full=Basic 7S globulin low kDa subunit;
DE Flags: Precursor;
GN Name=BG; Synonyms=G7S;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Miyagishirome; TISSUE=Seed;
RX PubMed=2587227; DOI=10.1093/nar/17.21.8868;
RA Kagawa H., Hirano H.;
RT "Sequence of a cDNA encoding soybean basic 7S globulin.";
RL Nucleic Acids Res. 17:8868-8868(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Miyagishirome; TISSUE=Etiolated leaf;
RX PubMed=8058830; DOI=10.1104/pp.105.3.1019;
RA Watanabe Y., Hirano H.;
RT "Nucleotide sequence of the basic 7S globulin gene from soybean.";
RL Plant Physiol. 105:1019-1020(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Shi-shi; TISSUE=Cotyledon;
RA Shu T.F., Hsieh K.L., Hsing Y.I., Chen Z.Y., Chow T.Y.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 25-57; 135-150; 276-311 AND 383-417.
RX PubMed=2226413; DOI=10.1002/elps.1150110708;
RA Hirano H., Watanabe T.;
RT "Microsequencing of proteins electrotransferred onto immobilizing matrices
RT from polyacrylamide gel electrophoresis: application to an insoluble
RT protein.";
RL Electrophoresis 11:573-580(1990).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RA Kagawa H., Yamauchi F., Hirano H.;
RT "Soybean basic 7S globulin represents a protein widely distributed in
RT legume species.";
RL FEBS Lett. 226:145-149(1987).
CC -!- FUNCTION: Seed storage protein. Has a protein kinase activity. Binds
CC leginsulin.
CC -!- SUBUNIT: The mature protein consists of high- and low-kDa subunits
CC linked by disulfide bonds.
CC -!- INTERACTION:
CC P13917; P13917: BG; NbExp=5; IntAct=EBI-8621895, EBI-8621895;
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; X16469; CAA34489.1; -; mRNA.
DR EMBL; U59425; AAB03390.1; -; mRNA.
DR EMBL; D16107; BAA03681.1; -; Genomic_DNA.
DR PIR; S06750; S06750.
DR RefSeq; XP_003521716.1; XM_003521668.3.
DR PDB; 3AUP; X-ray; 1.91 A; A/B/C/D=25-427.
DR PDBsum; 3AUP; -.
DR AlphaFoldDB; P13917; -.
DR SMR; P13917; -.
DR MINT; P13917; -.
DR STRING; 3847.GLYMA03G39940.1; -.
DR PRIDE; P13917; -.
DR EnsemblPlants; KRH68584; KRH68584; GLYMA_03G239700.
DR Gramene; KRH68584; KRH68584; GLYMA_03G239700.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_032185_0_0_1; -.
DR InParanoid; P13917; -.
DR OMA; RAPRCHS; -.
DR OrthoDB; 536577at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR Genevisible; P13917; GM.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2226413"
FT CHAIN 25..427
FT /note="Basic 7S globulin"
FT /id="PRO_0000032198"
FT CHAIN 25..275
FT /note="Basic 7S globulin high kDa subunit"
FT /id="PRO_0000032199"
FT CHAIN 276..427
FT /note="Basic 7S globulin low kDa subunit"
FT /id="PRO_0000032200"
FT DOMAIN 47..407
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CONFLICT 48
FT /note="W -> S (in Ref. 3; AAB03390)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="N -> T (in Ref. 1; CAA34489)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="F -> C (in Ref. 1; CAA34489)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="F -> C (in Ref. 1; CAA34489)"
FT /evidence="ECO:0000305"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3AUP"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3AUP"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3AUP"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 129..144
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 155..166
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:3AUP"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:3AUP"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:3AUP"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:3AUP"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:3AUP"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:3AUP"
SQ SEQUENCE 427 AA; 46393 MW; 66041BC0680BACCB CRC64;
MASILHYFLA LSLSCSFLFF LSDSVTPTKP INLVVLPVQN DGSTGLHWAN LQKRTPLMQV
PVLVDLNGNH LWVNCEQQYS SKTYQAPFCH STQCSRANTH QCLSCPAASR PGCHKNTCGL
MSTNPITQQT GLGELGEDVL AIHATQGSTQ QLGPLVTVPQ FLFSCAPSFL VQKGLPRNTQ
GVAGLGHAPI SLPNQLASHF GLQRQFTTCL SRYPTSKGAI IFGDAPNNMR QFQNQDIFHD
LAFTPLTITL QGEYNVRVNS IRINQHSVFP LNKISSTIVG STSGGTMIST STPHMVLQQS
VYQAFTQVFA QQLPKQAQVK SVAPFGLCFN SNKINAYPSV DLVMDKPNGP VWRISGEDLM
VQAQPGVTCL GVMNGGMQPR AEITLGARQL EENLVVFDLA RSRVGFSTSS LHSHGVKCAD
LFNFANA
