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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
Proteomesi
  • UP000008827 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)DescriptionActionsGraphical viewLength
Mutagenesisi145I → 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 Publication1
Mutagenesisi147K → T, F or W: Little or no effect on the secondary structure and strong phagocytosis-stimulating activity; when associated with M-145. 1 Publication1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000003219124 – 439Beta-conglycinin, beta chain2 PublicationsAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi351N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP25974.

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

1439
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 30Combined sources3
Helixi38 – 40Combined sources3
Beta strandi41 – 47Combined sources7
Beta strandi49 – 56Combined sources8
Helixi59 – 62Combined sources4
Helixi64 – 69Combined sources6
Beta strandi73 – 79Combined sources7
Beta strandi83 – 101Combined sources19
Beta strandi103 – 108Combined sources6
Beta strandi113 – 118Combined sources6
Beta strandi122 – 126Combined sources5
Beta strandi131 – 136Combined sources6
Beta strandi143 – 154Combined sources12
Beta strandi160 – 164Combined sources5
Beta strandi166 – 168Combined sources3
Helixi172 – 175Combined sources4
Helixi178 – 185Combined sources8
Helixi189 – 196Combined sources8
Helixi202 – 204Combined sources3
Beta strandi205 – 212Combined sources8
Helixi215 – 221Combined sources7
Helixi230 – 234Combined sources5
Beta strandi236 – 238Combined sources3
Helixi242 – 244Combined sources3
Beta strandi248 – 250Combined sources3
Beta strandi252 – 259Combined sources8
Turni261 – 263Combined sources3
Helixi265 – 270Combined sources6
Beta strandi272 – 279Combined sources8
Beta strandi283 – 292Combined sources10
Beta strandi294 – 311Combined sources18
Beta strandi327 – 335Combined sources9
Beta strandi339 – 342Combined sources4
Beta strandi348 – 363Combined sources16
Beta strandi370 – 376Combined sources7
Helixi381 – 383Combined sources3
Helixi386 – 392Combined sources7
Beta strandi393 – 395Combined sources3
Helixi397 – 403Combined sources7
Beta strandi411 – 414Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25974.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi199 – 202Poly-GluSequence analysis4

Sequence similaritiesi

Belongs to the 7S seed storage protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410INE4. Eukaryota.
ENOG410YEDB. LUCA.
InParanoidiP25974.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR006045. Cupin_1.
IPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 1 hit.
PF07883. Cupin_2. 1 hit.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti36F → L AA sequence (Ref. 3) Curated1
Sequence conflicti36F → L AA sequence (PubMed:16663129).Curated1
Sequence conflicti39S → V AA sequence (Ref. 3) Curated1
Sequence conflicti44T → G AA sequence (Ref. 3) Curated1
Sequence conflicti50N → D AA sequence (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S44893 Genomic DNA. Translation: AAB23463.1.
PIRiJQ0969. FWSYCB.
UniGeneiGma.26853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S44893 Genomic DNA. Translation: AAB23463.1.
PIRiJQ0969. FWSYCB.
UniGeneiGma.26853.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.

Proteomic databases

PRIDEiP25974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410INE4. Eukaryota.
ENOG410YEDB. LUCA.
InParanoidiP25974.

Miscellaneous databases

EvolutionaryTraceiP25974.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR006045. Cupin_1.
IPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 1 hit.
PF07883. Cupin_2. 1 hit.
[Graphical view]
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 90 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

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 one 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.