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Protein

Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform

Gene

HGN1

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei276 – 2761NucleophileBy similarity
Active sitei333 – 3331Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. defense response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 4 chains:
Gene namesi
Name:HGN1
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Subcellular locationi

Vacuole Curated

GO - Cellular componenti

  1. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei3313. Hev b 2.0101.
386. Hev b 2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence AnalysisAdd
BLAST
Chaini37 – 356320Glucan endo-1,3-beta-glucosidase minor form 3PRO_0000011843Add
BLAST
Chaini37 – 355319Glucan endo-1,3-beta-glucosidase minor form 2PRO_0000011844Add
BLAST
Chaini37 – 354318Glucan endo-1,3-beta-glucosidase minor form 1PRO_0000011845Add
BLAST
Chaini37 – 352316Glucan endo-1,3-beta-glucosidase major formPRO_0000011846Add
BLAST
Propeptidei357 – 37418Removed in mature formSequence AnalysisPRO_0000011847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Pyrrolidone carboxylic acidCurated
Glycosylationi63 – 631N-linked (GlcNAc...)1 Publication
Glycosylationi350 – 3501N-linked (GlcNAc...)1 Publication
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.1 Publication
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 354.1 Publication

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP52407.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP52407.
SMRiP52407. Positions 38-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52407-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISSSTSGT SSSFPSRTTV MLLLFFFAAS VGITDAQVGV CYGMQGNNLP
60 70 80 90 100
PVSEVIALYK KSNITRMRIY DPNRAVLEAL RGSNIELILG VPNSDLQSLT
110 120 130 140 150
NPSNAKSWVQ KNVRGFWSSV LFRYIAVGNE ISPVNRGTAW LAQFVLPAMR
160 170 180 190 200
NIHDAIRSAG LQDQIKVSTA IDLTLVGNSY PPSAGAFRDD VRSYLDPIIG
210 220 230 240 250
FLSSIRSPLL ANIYPYFTYA YNPRDISLPY ALFTSPSVVV WDGQRGYKNL
260 270 280 290 300
FDATLDALYS ALERASGGSL EVVVSESGWP SAGAFAATFD NGRTYLSNLI
310 320 330 340 350
QHVKGGTPKR PNRAIETYLF AMFDENKKQP EVEKHFGLFF PNKWQKYNLN
360 370
FSAEKNWDIS TEHNATILFL KSDM
Length:374
Mass (Da):41,396
Last modified:February 29, 2004 - v2
Checksum:i7468888769FE3A9D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti344 – 3452WQ → RP (PubMed:7579190).Curated

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti342 – 3421N → D in strain: cv. PR 261 and cv. RRIM 600. 1 Publication
Natural varianti352 – 3521S → G in strain: cv. PR 261 and cv. RRIM 600. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22147 mRNA. Translation: AAA87456.1.
PIRiS65077.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22147 mRNA. Translation: AAA87456.1.
PIRiS65077.

3D structure databases

ProteinModelPortaliP52407.
SMRiP52407. Positions 38-351.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3313. Hev b 2.0101.
386. Hev b 2.
CAZyiGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEiP52407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1994) [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(1995) [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(2000)
    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(1994)
    Cited for: SUBUNIT.
    Strain: cv. RRIM 600.

Entry informationi

Entry nameiE13B_HEVBR
AccessioniPrimary (citable) accession number: P52407
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: February 29, 2004
Last modified: January 6, 2015
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.