Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-conglycinin, beta chain

Gene

CG-4

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Seed storage protein, Storage protein

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-conglycinin, beta chain1 Publication
Gene namesi
Name:CG-41 Publication
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
ProteomesiUP000008827 Componenti: Unplaced

Subcellular locationi

  • Vacuolealeurone grain 1 Publication

  • Note: Embryo axis, and cotyledonary membrane-bound vacuolar protein bodies.1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451I → M: Little or no effect on the secondary structure and strong phagocytosis-stimulating activity; when associated with T-147; F-147 or W-147. 1 Publication
Mutagenesisi147 – 1471K → T, F or W: Little or no effect on the secondary structure and strong phagocytosis-stimulating activity; when associated with M-145. 1 Publication

Protein family/group databases

Allergomei5816. Gly m 5.
5819. Gly m 5.0301.
5820. Gly m 5.0302.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 439416Beta-conglycinin, beta chain2 PublicationsPRO_0000032191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi351 – 3511N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The N-linked glycans are not essential for the folding and assembly into trimers.1 Publication

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Expressed in seeds. Not detected in cotyledons or in mature plants.1 Publication

Developmental stagei

Expressed early in embryogenesis, with a high transcription rate at midmaturation and then decreases prior to seed dormancy.1 Publication

Interactioni

Subunit structurei

The alpha'-, alpha-, and beta-subunits associate in various combinations to form trimeric proteins.1 Publication

Protein-protein interaction databases

STRINGi3847.GLYMA20G28460.1.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Helixi38 – 403Combined sources
Beta strandi41 – 477Combined sources
Beta strandi49 – 568Combined sources
Helixi59 – 624Combined sources
Helixi64 – 696Combined sources
Beta strandi73 – 797Combined sources
Beta strandi83 – 10119Combined sources
Beta strandi103 – 1086Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi122 – 1265Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi143 – 15412Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi166 – 1683Combined sources
Helixi172 – 1754Combined sources
Helixi178 – 1858Combined sources
Helixi189 – 1968Combined sources
Helixi202 – 2043Combined sources
Beta strandi205 – 2128Combined sources
Helixi215 – 2217Combined sources
Helixi230 – 2345Combined sources
Beta strandi236 – 2383Combined sources
Helixi242 – 2443Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi252 – 2598Combined sources
Turni261 – 2633Combined sources
Helixi265 – 2706Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi283 – 29210Combined sources
Beta strandi294 – 31118Combined sources
Beta strandi327 – 3359Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi348 – 36316Combined sources
Beta strandi370 – 3767Combined sources
Helixi381 – 3833Combined sources
Helixi386 – 3927Combined sources
Beta strandi393 – 3953Combined sources
Helixi397 – 4037Combined sources
Beta strandi411 – 4144Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IPJX-ray2.70A/B/C24-439[»]
1IPKX-ray2.70A/B/C24-439[»]
1UIJX-ray2.50A/B/C/D/E/F24-439[»]
ProteinModelPortaliP25974.
SMRiP25974. Positions 26-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25974.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi199 – 2024Poly-GluSequence Analysis

Sequence similaritiesi

Belongs to the 7S seed storage protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP25974.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR006045. Cupin_1.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 2 hits.
[Graphical view]
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25974-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRVRFPLLV LLGTVFLASV CVSLKVREDE NNPFYFRSSN SFQTLFENQN
60 70 80 90 100
VRIRLLQRFN KRSPQLENLR DYRIVQFQSK PNTILLPHHA DADFLLFVLS
110 120 130 140 150
GRAILTLVNN DDRDSYNLHP GDAQRIPAGT TYYLVNPHDH QNLKIIKLAI
160 170 180 190 200
PVNKPGRYDD FFLSSTQAQQ SYLQGFSHNI LETSFHSEFE EINRVLFGEE
210 220 230 240 250
EEQRQQEGVI VELSKEQIRQ LSRRAKSSSR KTISSEDEPF NLRSRNPIYS
260 270 280 290 300
NNFGKFFEIT PEKNPQLRDL DIFLSSVDIN EGALLLPHFN SKAIVILVIN
310 320 330 340 350
EGDANIELVG IKEQQQKQKQ EEEPLEVQRY RAELSEDDVF VIPAAYPFVV
360 370 380 390 400
NATSNLNFLA FGINAENNQR NFLAGEKDNV VRQIERQVQE LAFPGSAQDV
410 420 430
ERLLKKQRES YFVDAQPQQK EEGSKGRKGP FPSILGALY
Length:439
Mass (Da):50,552
Last modified:May 1, 1992 - v1
Checksum:iDBD8AA2A0776088B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361F → L AA sequence (Ref. 3) Curated
Sequence conflicti36 – 361F → L AA sequence (PubMed:16663129).Curated
Sequence conflicti39 – 391S → V AA sequence (Ref. 3) Curated
Sequence conflicti44 – 441T → G AA sequence (Ref. 3) Curated
Sequence conflicti50 – 501N → D AA sequence (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S44893 Genomic DNA. Translation: AAB23463.1.
PIRiJQ0969. FWSYCB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S44893 Genomic DNA. Translation: AAB23463.1.
PIRiJQ0969. FWSYCB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IPJX-ray2.70A/B/C24-439[»]
1IPKX-ray2.70A/B/C24-439[»]
1UIJX-ray2.50A/B/C/D/E/F24-439[»]
ProteinModelPortaliP25974.
SMRiP25974. Positions 26-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3847.GLYMA20G28460.1.

Protein family/group databases

Allergomei5816. Gly m 5.
5819. Gly m 5.0301.
5820. Gly m 5.0302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiP25974.

Miscellaneous databases

EvolutionaryTraceiP25974.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR006045. Cupin_1.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 2 hits.
[Graphical view]
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Soybean beta-conglycinin genes are clustered in several DNA regions and are regulated by transcriptional and posttranscriptional processes."
    Harada J.J., Barker S.J., Goldberg R.B.
    Plant Cell 1:415-425(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
    Strain: cv. Dare and cv. Forrest.
  2. "Glycinin composition of several perennial species related to soybean."
    Staswick P.E., Broue P., Nielsen N.C.
    Plant Physiol. 72:1114-1118(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-38.
  3. "Structural homology among the major 7s globulin subunits of soybean seed storage proteins."
    Hirano H., Kagawa H., Kamata Y., Yamauchi F.
    Phytochemistry 26:41-45(1987)
    Cited for: PROTEIN SEQUENCE OF 24-50.
    Strain: cv. Raiden.
  4. "Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers."
    Maruyama N., Adachi M., Takahashi K., Yagasaki K., Kohno M., Takenaka Y., Okuda E., Nakagawa S., Mikami B., Utsumi S.
    Eur. J. Biochem. 268:3595-3604(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-439 OF WILD-TYPE PROTEIN, GLYCOSYLATION AT ASN-351.
  5. "Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity."
    Maruyama N., Maruyama Y., Tsuruki T., Okuda E., Yoshikawa M., Utsumi S.
    Biochim. Biophys. Acta 1648:99-104(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 24-439 OF MUTANT PROTEIN, MUTAGENESIS OF ILE-145 AND LYS-147.

Entry informationi

Entry nameiGLCB_SOYBN
AccessioniPrimary (citable) accession number: P25974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.