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P52401 (E132_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. 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, basic isoform 2

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
Gene names
Name:GLUB2
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Is thought to be an important plant defense-related product against fungal pathogens.

Catalytic activity

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

Subcellular location

Vacuole By similarity.

Tissue specificity

High levels in leaves. Appreciable amounts in stems, roots, and sepals. Tubers, root tips, and all other flower organs contain very low levels of enzyme.

Developmental stage

Highest levels in old segments of leaves, stems and roots.

Induction

In leaves, in response to infection, elicitor, ethylene, or wounding.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentVacuole
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
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 – 2525 Potential
Chain26 – 340315Glucan endo-1,3-beta-glucosidase, basic isoform 2
PRO_0000011862
Propeptide341 – 36323Removed in mature form By similarity
PRO_0000011863

Sites

Active site2651Nucleophile By similarity
Active site3211Proton donor By similarity

Amino acid modifications

Modified residue261Pyrrolidone carboxylic acid Probable
Glycosylation3531N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P52401 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 201A1A6A50C30DCC

FASTA36339,759
        10         20         30         40         50         60 
MATSQIAVIV LLGLLVATNI HITEAQLGVC YGMMGNNLPS HSEVIQLYKS RNIGRLRLYD 

        70         80         90        100        110        120 
PNQGALNALR GSNIEVILGL PNVDVKHIAS GMEHARWWVQ KNVKDFWPDV KIKYIAVGNE 

       130        140        150        160        170        180 
ISPVTGTSSL TSFQVPALVN IYKAVGEAGL GNDIKVSTSV DMTLIGNSYP PSQGSFRNDV 

       190        200        210        220        230        240 
RWFTDPIVGF LRDTRAPLLV NIYPYFSYSG NPGQISLPYA LFTAPNVVVQ DGSRQYRNLF 

       250        260        270        280        290        300 
DAMLDSVYAA MERTGGGSVG IVVSECGWPS AGAFGATQDN AATYLRNLIQ HAKEGSPRKP 

       310        320        330        340        350        360 
GPIETYIFAM FDENNKNPEL EKHFGLFSPN KQPKYNLNFG VSERVWDISA ETNSTASSLI 


SEM 

« Hide

References

[1]"Primary structure and expression of mRNAs encoding basic chitinase and 1,3-beta-glucanase in potato."
Beerhues L., Kombrink E.
Plant Mol. Biol. 24:353-367(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Datura.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01901 mRNA. Translation: AAA18928.1.
PIRS43318.
RefSeqNP_001274869.1. NM_001287940.1.
UniGeneStu.256.

3D structure databases

ProteinModelPortalP52401.
SMRP52401. Positions 27-339.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome2551. Sola t Glucanase.
CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102577444.
KEGGsot:102577444.

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 nameE132_SOLTU
AccessionPrimary (citable) accession number: P52401
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 69 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