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P52397 (E13J_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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, acidic isoform PR-O

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
PR-37
Gene names
Name:PR0
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Protein attributes

Sequence length160 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in the defense of plants against pathogens.

Catalytic activity

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

Subcellular location

Secretedextracellular space.

Induction

Not found in healthy tissues, but accumulates to high levels in the extracellular compartment of leaves in response to pathogen infection or treatment with salicylic acid.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

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

Chain‹1 – 160›160Glucan endo-1,3-beta-glucosidase, acidic isoform PR-O
PRO_0000205278

Sites

Active site811Nucleophile By similarity
Active site1411Proton donor By similarity

Experimental info

Sequence conflict1281A → N AA sequence Ref.2
Sequence conflict1351K → Q AA sequence Ref.2
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P52397 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 98C270F390764B7F

FASTA16017,980
        10         20         30         40         50         60 
NSFINPIIQF LARNNLPLLA NVYPYFGHIY NTADVPLSYA LFTQQEANPA GYQNLFDALL 

        70         80         90        100        110        120 
DSMYFAVEKA GGPNVEIIVS ESGWPSEGNS AATIENAQTY YRNLIDHVKR GAGTPKKPGK 

       130        140        150        160 
TIETYLFAMF DENDKKGEIT EKHFGLFSPD QRAKYQLNFN 

« Hide

References

[1]"Differential regulation of beta-1,3-glucanase messenger RNAs in response to pathogen infection."
Ward E.R., Payne G.B., Moyer M.B., Williams S.C., Dincher S.S., Sharkey K.C., Beck J.J., Taylor H.T., Ahl-Goy P., Meins F., Ryals J.A.
Plant Physiol. 96:390-397(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Xanthi NC.
Tissue: Leaf.
[2]"Characterization of vacuolar and extracellular beta(1,3)-glucanases of tobacco: evidence for a strictly compartmentalized plant defense system."
van den Bulcke M., Bauw G., Castresana C., van Montagu M., Vandekerckhove J.
Proc. Natl. Acad. Sci. U.S.A. 86:2673-2677(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 70-93; 126-136; 143-152 AND 155-160.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60461 mRNA. Translation: AAA34102.1.

3D structure databases

ProteinModelPortalP52397.
SMRP52397. Positions 2-159.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEP52397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameE13J_TOBAC
AccessionPrimary (citable) accession number: P52397
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 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