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Q03773 (E13A_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-beta-glucosidase

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
OrganismGlycine max (Soybean) (Glycine hispida) [Reference proteome]
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is thought to be an important plant defense-related product against fungal pathogens. Is capable of releasing soluble and highly active elicitor molecules from fungus cell walls.

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Subcellular location

Vacuole By similarity. Note: In intact tissues By similarity.

Induction

By ethylene.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentVacuole
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 347315Glucan endo-1,3-beta-glucosidase
PRO_0000011866

Sites

Active site2701Nucleophile By similarity
Active site3271Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03773 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0FB1B814FDF78753

FASTA34738,112
        10         20         30         40         50         60 
MAKYHSSGKS SSMTAIAFLF ILLITYTGTT DAQSGVCYGR LGNNLPTPQE VVALYNQANI 

        70         80         90        100        110        120 
RRMRIYGPSP EVLEALRGSN IELLLDIPND NLRNLASSQD NANKWVQDNI KNYANNVRFR 

       130        140        150        160        170        180 
YVSVGNEVKP EHSFAQFLVP ALENIQRAIS NAGLGNQVKV STAIDTGALA ESFPPSKGSF 

       190        200        210        220        230        240 
KSDYRGAYLD GVIRFLVNNN APLMVNVYSY FAYTANPKDI SLDYALFRSP SVVVQDGSLG 

       250        260        270        280        290        300 
YRNLFDASVD AVYAALEKAG GGSLNIVVSE SGWPSSGGTA TSLDNARTYN TNLVRNVKQG 

       310        320        330        340 
TPKRPGAPLE TYVFAMFDEN QKQPEFEKFW GLFSPITKQP KYSINFN 

« Hide

References

[1]"Molecular cloning and ethylene induction of mRNA encoding a phytoalexin elicitor-releasing factor, beta-1,3-endoglucanase, in soybean."
Takeuchi Y., Yoshikawa M., Takeba G., Tanaka K., Shibata D., Horino O.
Plant Physiol. 93:673-682(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 186-194 AND 219-224.
Strain: cv. Harosoy 63.
Tissue: Cotyledon.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37753 mRNA. Translation: AAA33946.1.
PIRT07108.
RefSeqNP_001238474.1. NM_001251545.1.
UniGeneGma.31973.

3D structure databases

ProteinModelPortalQ03773.
SMRQ03773. Positions 35-346.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEQ03773.
ProMEXQ03773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsGLYMA03G28850.1; GLYMA03G28850.1; GLYMA03G28850.
GeneID547822.
KEGGgmx:547822.

Phylogenomic databases

OMAARTYVNN.

Gene expression databases

GenevestigatorQ03773.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE13A_SOYBN
AccessionPrimary (citable) accession number: Q03773
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries