P25974 · GLCB1_SOYBN

Function

function

Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.

Miscellaneous

Mutagenesis of Ile-145 and Lys-147 allow the creation of a beta-conglycinin beta chain containing a phagocytosis-stimulating peptide, soymetide, found normally only in the alpha' chain. The three mutants created exhibit phagocytosis activities after digestion by trypsin and the order is wild type < I145M/K147T < I145M/K147F < I145M/K147W.

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentaleurone grain
Cellular Componentendoplasmic reticulum
Cellular Componentprotein storage vacuole
Molecular Functionnutrient reservoir activity

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Beta-conglycinin beta subunit 1
  • Short names
    CG-beta-1
  • Alternative names
    • Beta-conglycinin beta subunit
  • Allergen name
    Gly m 5

Gene names

    • Name
      CG-4
    • ORF names
      GLYMA_20G146200

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Dare
    • cv. Forrest
    • cv. Williams 82
    • cv. Raiden
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja

Accessions

  • Primary accession
    P25974
  • Secondary accessions
    • I1NGF4

Proteomes

Genome annotation databases

Subcellular Location

Endoplasmic reticulum
Note: Localizes in protein storage vacuoles in cotyledons of developing and mature beans (PubMed:15447650, Ref.6). Synthesized and assembled into trimers in the endoplasmic reticulum, and transported to the protein storage vacuoles by the dense vesicles (PubMed:15447650).

Keywords

Phenotypes & Variants

Allergenic properties

Causes an allergic reaction in human (PubMed:18996574).
Binds to IgE of patients with severe allergic reactions (anaphylaxis) to soybean (PubMed:18996574).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis145Little or no effect on the secondary structure and strong phagocytosis-stimulating activity; when associated with T-147; F-147 or W-147.
Mutagenesis147Little or no effect on the secondary structure and strong phagocytosis-stimulating activity; when associated with M-145.

Keywords

Protein family/group databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000003219124-439Beta-conglycinin beta subunit 1
Glycosylation351N-linked (GlcNAc...) asparagine

Post-translational modification

The N-linked glycans are not essential for the folding and assembly into trimers.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in seeds. Not detected in cotyledons or in mature plants.

Developmental stage

Expressed early in embryogenesis, with a high transcription rate at midmaturation and then decreases prior to seed dormancy.

Interaction

Subunit

The alpha-, alpha'-, and beta-subunits associate in various combinations to form trimeric proteins.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain34-193Cupin type-1 1
Domain240-401Cupin type-1 2
Region411-439Disordered
Region430-439Necessary for sorting to protein storage vacuole

Sequence similarities

Belongs to the 7S seed storage protein family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    439
  • Mass (Da)
    50,476
  • Last updated
    2019-01-16 v2
  • Checksum
    86D20314FC21D9E7
MMRVRFPLLVLLGTVFLASVCVSLKVREDENNPFYLRSSNSFQTLFENQNGRIRLLQRFNKRSPQLENLRDYRIVQFQSKPNTILLPHHADADFLLFVLSGRAILTLVNNDDRDSYNLHPGDAQRIPAGTTYYLVNPHDHQNLKIIKLAIPVNKPGRYDDFFLSSTQAQQSYLQGFSHNILETSFHSEFEEINRVLFGEEEEQRQQEGVIVELSKEQIRQLSRRAKSSSRKTISSEDEPFNLRSRNPIYSNNFGKFFEITPEKNPQLRDLDIFLSSVDINEGALLLPHFNSKAIVILVINEGDANIELVGIKEQQQKQKQEEEPLEVQRYRAELSEDDVFVIPAAYPFVVNATSNLNFLAFGINAENNQRNFLAGEKDNVVRQIERQVQELAFPGSAQDVERLLKKQRESYFVDAQPQQKEEGSKGRKGPFPSILGALY

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict36in Ref. 1; AAB23463
Sequence conflict39in Ref. 4; AA sequence
Sequence conflict44in Ref. 4; AA sequence
Sequence conflict50in Ref. 4; AA sequence
Sequence conflict51in Ref. 1; AAB23463

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
S44893
EMBL· GenBank· DDBJ
AAB23463.1
EMBL· GenBank· DDBJ
Genomic DNA
CM000853
EMBL· GenBank· DDBJ
KRG91303.1
EMBL· GenBank· DDBJ
Genomic DNA
ACUP02012674
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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