ID   GLCB1_SOYBN             Reviewed;         439 AA.
AC   P25974; I1NGF4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 2.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Beta-conglycinin beta subunit 1 {ECO:0000305};
DE            Short=CG-beta-1 {ECO:0000305};
DE   AltName: Full=Beta-conglycinin beta subunit {ECO:0000303|PubMed:2562562};
DE   AltName: Allergen=Gly m 5 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=CG-4 {ECO:0000303|PubMed:2562562};
GN   ORFNames=GLYMA_20G146200 {ECO:0000312|EMBL:KRG91303.1};
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 [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Dare, and cv. Forrest;
RX   PubMed=2562562; DOI=10.1105/tpc.1.4.415;
RA   Harada J.J., Barker S.J., Goldberg R.B.;
RT   "Soybean beta-conglycinin genes are clustered in several DNA regions and
RT   are regulated by transcriptional and posttranscriptional processes.";
RL   Plant Cell 1:415-425(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82;
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-38.
RX   PubMed=16663129; DOI=10.1104/pp.72.4.1114;
RA   Staswick P.E., Broue P., Nielsen N.C.;
RT   "Glycinin composition of several perennial species related to soybean.";
RL   Plant Physiol. 72:1114-1118(1983).
RN   [4]
RP   PROTEIN SEQUENCE OF 24-50.
RC   STRAIN=cv. Raiden;
RX   DOI=10.1016/S0031-9422(00)81477-6;
RA   Hirano H., Kagawa H., Kamata Y., Yamauchi F.;
RT   "Structural homology among the major 7s globulin subunits of soybean seed
RT   storage proteins.";
RL   Phytochemistry 26:41-45(1987).
RN   [5]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=15447650; DOI=10.1111/j.1365-313x.2004.02204.x;
RA   Mori T., Maruyama N., Nishizawa K., Higasa T., Yagasaki K., Ishimoto M.,
RA   Utsumi S.;
RT   "The composition of newly synthesized proteins in the endoplasmic reticulum
RT   determines the transport pathways of soybean seed storage proteins.";
RL   Plant J. 40:238-249(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   DOI=10.1016/j.plantsci.2004.06.004;
RA   Nishizawa K., Maruyama N., Satoh R., Higasa T., Utsumi S.;
RT   "A vacuolar sorting determinant of soybean beta-conglycinin beta subunit
RT   resides in a C-terminal sequence.";
RL   Plant Sci. 167:937-947(2004).
RN   [7]
RP   ALLERGEN.
RX   PubMed=18996574; DOI=10.1016/j.jaci.2008.09.034;
RA   Holzhauser T., Wackermann O., Ballmer-Weber B.K., Bindslev-Jensen C.,
RA   Scibilia J., Perono-Garoffo L., Utsumi S., Poulsen L.K., Vieths S.;
RT   "Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and
RT   Gly m 6 (glycinin) are potential diagnostic markers for severe allergic
RT   reactions to soy.";
RL   J. Allergy Clin. Immunol. 123:452-458(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-439 OF WILD-TYPE PROTEIN, AND
RP   GLYCOSYLATION AT ASN-351.
RX   PubMed=11422391; DOI=10.1046/j.1432-1327.2001.02268.x;
RA   Maruyama N., Adachi M., Takahashi K., Yagasaki K., Kohno M., Takenaka Y.,
RA   Okuda E., Nakagawa S., Mikami B., Utsumi S.;
RT   "Crystal structures of recombinant and native soybean beta-conglycinin beta
RT   homotrimers.";
RL   Eur. J. Biochem. 268:3595-3604(2001).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 24-439 OF MUTANT PROTEIN, AND
RP   MUTAGENESIS OF ILE-145 AND LYS-147.
RX   PubMed=12758152; DOI=10.1016/s1570-9639(03)00113-4;
RA   Maruyama N., Maruyama Y., Tsuruki T., Okuda E., Yoshikawa M., Utsumi S.;
RT   "Creation of soybean beta-conglycinin beta with strong phagocytosis-
RT   stimulating activity.";
RL   Biochim. Biophys. Acta 1648:99-104(2003).
CC   -!- FUNCTION: Seed storage protein. Accumulates during seed development and
CC       is hydrolyzed after germination to provide a carbon and nitrogen source
CC       for the developing seedling. {ECO:0000305|PubMed:2562562}.
CC   -!- SUBUNIT: The alpha-, alpha'-, and beta-subunits associate in various
CC       combinations to form trimeric proteins. {ECO:0000305|PubMed:15447650}.
CC   -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000305}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:15447650}. Protein storage
CC       vacuole {ECO:0000269|PubMed:15447650, ECO:0000269|Ref.6}.
CC       Note=Localizes in protein storage vacuoles in cotyledons of developing
CC       and mature beans (PubMed:15447650, Ref.6). Synthesized and assembled
CC       into trimers in the endoplasmic reticulum, and transported to the
CC       protein storage vacuoles by the dense vesicles (PubMed:15447650).
CC       {ECO:0000269|PubMed:15447650, ECO:0000269|Ref.6}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds. Not detected in cotyledons or
CC       in mature plants. {ECO:0000305|PubMed:2562562}.
CC   -!- DEVELOPMENTAL STAGE: Expressed early in embryogenesis, with a high
CC       transcription rate at midmaturation and then decreases prior to seed
CC       dormancy. {ECO:0000269|PubMed:2562562}.
CC   -!- PTM: The N-linked glycans are not essential for the folding and
CC       assembly into trimers. {ECO:0000269|PubMed:11422391}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:18996574). Binds
CC       to IgE of patients with severe allergic reactions (anaphylaxis) to
CC       soybean (PubMed:18996574). {ECO:0000269|PubMed:18996574}.
CC   -!- MISCELLANEOUS: Mutagenesis of Ile-145 and Lys-147 allow the creation of
CC       a beta-conglycinin beta chain containing a phagocytosis-stimulating
CC       peptide, soymetide, found normally only in the alpha' chain. The three
CC       mutants created exhibit phagocytosis activities after digestion by
CC       trypsin and the order is wild type < I145M/K147T < I145M/K147F <
CC       I145M/K147W. {ECO:0000269|PubMed:12758152}.
CC   -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC       {ECO:0000305}.
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DR   EMBL; S44893; AAB23463.1; -; Genomic_DNA.
DR   EMBL; CM000853; KRG91303.1; -; Genomic_DNA.
DR   EMBL; ACUP02012674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JQ0969; FWSYCB.
DR   PDB; 1IPJ; X-ray; 2.70 A; A/B/C=24-439.
DR   PDB; 1IPK; X-ray; 2.70 A; A/B/C=24-439.
DR   PDB; 1UIJ; X-ray; 2.50 A; A/B/C/D/E/F=24-439.
DR   PDBsum; 1IPJ; -.
DR   PDBsum; 1IPK; -.
DR   PDBsum; 1UIJ; -.
DR   AlphaFoldDB; P25974; -.
DR   SMR; P25974; -.
DR   STRING; 3847.P25974; -.
DR   Allergome; 5816; Gly m 5.
DR   Allergome; 5819; Gly m 5.0301.
DR   Allergome; 5820; Gly m 5.0302.
DR   GlyCosmos; P25974; 1 site, No reported glycans.
DR   iPTMnet; P25974; -.
DR   PaxDb; 3847-GLYMA20G28460-1; -.
DR   EnsemblPlants; KRG91303; KRG91303; GLYMA_20G146200.
DR   Gramene; KRG91303; KRG91303; GLYMA_20G146200.
DR   eggNOG; ENOG502QQEP; Eukaryota.
DR   HOGENOM; CLU_018703_0_1_1; -.
DR   InParanoid; P25974; -.
DR   OMA; ELTGDEC; -.
DR   OrthoDB; 936915at2759; -.
DR   EvolutionaryTrace; P25974; -.
DR   Proteomes; UP000008827; Chromosome 20.
DR   GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0000326; C:protein storage vacuole; IDA:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   CDD; cd02245; cupin_7S_vicilin-like_C; 1.
DR   CDD; cd02244; cupin_7S_vicilin-like_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR31189:SF41; VICILIN C72; 1.
DR   Pfam; PF00190; Cupin_1; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC-like cupins; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Reference proteome; Seed storage protein; Signal;
KW   Storage protein; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000305|Ref.4"
FT   CHAIN           24..439
FT                   /note="Beta-conglycinin beta subunit 1"
FT                   /evidence="ECO:0000269|PubMed:16663129, ECO:0000269|Ref.4"
FT                   /id="PRO_0000032191"
FT   DOMAIN          34..193
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          240..401
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          411..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..439
FT                   /note="Necessary for sorting to protein storage vacuole"
FT                   /evidence="ECO:0000269|Ref.6"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11422391"
FT   MUTAGEN         145
FT                   /note="I->M: Little or no effect on the secondary structure
FT                   and strong phagocytosis-stimulating activity; when
FT                   associated with T-147; F-147 or W-147."
FT                   /evidence="ECO:0000269|PubMed:12758152"
FT   MUTAGEN         147
FT                   /note="K->T,F,W: Little or no effect on the secondary
FT                   structure and strong phagocytosis-stimulating activity;
FT                   when associated with M-145."
FT                   /evidence="ECO:0000269|PubMed:12758152"
FT   CONFLICT        36
FT                   /note="L -> F (in Ref. 1; AAB23463)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="S -> V (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="T -> G (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="N -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="G -> V (in Ref. 1; AAB23463)"
FT                   /evidence="ECO:0000305"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1IPK"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           64..69
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          83..101
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          143..154
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           178..185
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           189..196
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          205..212
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           215..221
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           230..234
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:1IPK"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          252..259
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           265..270
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          272..279
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          283..292
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          294..311
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          327..335
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          339..342
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          348..363
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          370..376
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           386..392
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   HELIX           397..403
FT                   /evidence="ECO:0007829|PDB:1UIJ"
FT   STRAND          411..414
FT                   /evidence="ECO:0007829|PDB:1UIJ"
SQ   SEQUENCE   439 AA;  50476 MW;  86D20314FC21D9E7 CRC64;
     MMRVRFPLLV LLGTVFLASV CVSLKVREDE NNPFYLRSSN SFQTLFENQN GRIRLLQRFN
     KRSPQLENLR DYRIVQFQSK PNTILLPHHA DADFLLFVLS GRAILTLVNN DDRDSYNLHP
     GDAQRIPAGT TYYLVNPHDH QNLKIIKLAI PVNKPGRYDD FFLSSTQAQQ SYLQGFSHNI
     LETSFHSEFE EINRVLFGEE EEQRQQEGVI VELSKEQIRQ LSRRAKSSSR KTISSEDEPF
     NLRSRNPIYS NNFGKFFEIT PEKNPQLRDL DIFLSSVDIN EGALLLPHFN SKAIVILVIN
     EGDANIELVG IKEQQQKQKQ EEEPLEVQRY RAELSEDDVF VIPAAYPFVV NATSNLNFLA
     FGINAENNQR NFLAGEKDNV VRQIERQVQE LAFPGSAQDV ERLLKKQRES YFVDAQPQQK
     EEGSKGRKGP FPSILGALY
//