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P52407 (E13B_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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, basic vacuolar isoform

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:HGN1
OrganismHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifier3981 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Protein attributes

Sequence length374 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.

Catalytic activity

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

Subunit structure

Monomer. Ref.4

Subcellular location

Vacuole Potential.

Tissue specificity

Expressed at highest levels in laticifer cells of the petiole. Ref.1

Post-translational modification

Glycosylated in cv. GT.1 and cv. RRIM 600 but not in cv. PR 261. Asn-350 is glycosylated only in cv. GT.1 due to the presence of Ser-352. In cv. PR 261 and cv. RRIM 600, Ser-352 is replaced by Gly so Asn-350 is not glycosylated. Ref.3

In cv. GT.1, four different forms of the enzyme have been detected with differently processed C-termini. In cv. PR 261 and cv. RRIM 600, only 2 forms are detected, a major form which is processed at residue 352 and a minor form which is processed at residue 354.

Polymorphism

The enzyme from cv. GT.1 displays a 3-5 fold lower specific activity than the enzyme from cv. PR 261.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5-5.0. The enzyme from cv. GT.1 displays a second optimum pH at 6.7.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentVacuole
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Pyrrolidone carboxylic acid
   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_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 – 3636 Potential
Chain37 – 356320Glucan endo-1,3-beta-glucosidase minor form 3
PRO_0000011843
Chain37 – 355319Glucan endo-1,3-beta-glucosidase minor form 2
PRO_0000011844
Chain37 – 354318Glucan endo-1,3-beta-glucosidase minor form 1
PRO_0000011845
Chain37 – 352316Glucan endo-1,3-beta-glucosidase major form
PRO_0000011846
Propeptide357 – 37418Removed in mature form Potential
PRO_0000011847

Sites

Active site2761Nucleophile By similarity
Active site3331Proton donor By similarity

Amino acid modifications

Modified residue371Pyrrolidone carboxylic acid Probable
Glycosylation631N-linked (GlcNAc...)
Glycosylation3501N-linked (GlcNAc...)
Glycosylation3641N-linked (GlcNAc...) Potential

Natural variations

Natural variant3421N → D in strain: cv. PR 261 and cv. RRIM 600. Ref.3
Natural variant3521S → G in strain: cv. PR 261 and cv. RRIM 600. Ref.3

Experimental info

Sequence conflict344 – 3452WQ → RP Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52407 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 7468888769FE3A9D

FASTA37441,396
        10         20         30         40         50         60 
MAISSSTSGT SSSFPSRTTV MLLLFFFAAS VGITDAQVGV CYGMQGNNLP PVSEVIALYK 

        70         80         90        100        110        120 
KSNITRMRIY DPNRAVLEAL RGSNIELILG VPNSDLQSLT NPSNAKSWVQ KNVRGFWSSV 

       130        140        150        160        170        180 
LFRYIAVGNE ISPVNRGTAW LAQFVLPAMR NIHDAIRSAG LQDQIKVSTA IDLTLVGNSY 

       190        200        210        220        230        240 
PPSAGAFRDD VRSYLDPIIG FLSSIRSPLL ANIYPYFTYA YNPRDISLPY ALFTSPSVVV 

       250        260        270        280        290        300 
WDGQRGYKNL FDATLDALYS ALERASGGSL EVVVSESGWP SAGAFAATFD NGRTYLSNLI 

       310        320        330        340        350        360 
QHVKGGTPKR PNRAIETYLF AMFDENKKQP EVEKHFGLFF PNKWQKYNLN FSAEKNWDIS 

       370 
TEHNATILFL KSDM 

« Hide

References

[1]"Beta-1,3-glucanase is highly-expressed in laticifers of Hevea brasiliensis."
Chye M.-L., Cheung K.-Y.
Plant Mol. Biol. 29:397-402(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. RRIM 600.
Tissue: Latex.
[2]"Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea latex."
Subroto T., van Koningsveld G.A., Schreuder H.A., Soedjanaatmadja U.M.S., Beintema J.J.
Phytochemistry 43:29-37(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-64 AND 323-352.
Strain: cv. RRIM 600.
Tissue: Latex.
[3]"Enzymic and structural studies on processed proteins from the vacuolar (lutoid-body) fraction of latex of Hevea brasiliensis."
Subroto T., de Vries H., Schuringa J.J., Soedjanaatmadja U.M.S., Hofsteenge J., Jekel P.A., Beintema J.J.
Plant Physiol. Biochem. 39:1047-1055(2001)
Cited for: PROTEIN SEQUENCE OF 323-356, GLYCOSYLATION, PROTEOLYTIC PROCESSING OF C-TERMINUS, VARIANTS ASP-342 AND GLY-352.
Strain: cv. GT.1, cv. PR 261 and cv. RRIM 600.
[4]"Beta-1,3-glucanase isozymes from the latex of Hevea brasiliensis."
Churngchow N., Suntaro A., Wititsuwannnakul R.
Phytochemistry 39:505-509(1995)
Cited for: SUBUNIT.
Strain: cv. RRIM 600.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22147 mRNA. Translation: AAA87456.1.
PIRS65077.

3D structure databases

ProteinModelPortalP52407.
SMRP52407. Positions 38-351.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3313. Hev b 2.0101.
386. Hev b 2.
CAZyGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEP52407.

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 nameE13B_HEVBR
AccessionPrimary (citable) accession number: P52407
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 1, 2004
Last modified: February 19, 2014
This is version 79 of the entry and version 2 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