Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P52407

- E13B_HEVBR

UniProt

P52407 - E13B_HEVBR

Protein

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

Gene

HGN1

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    MAISSSTSGT SSSFPSRTTV MLLLFFFAAS VGITDAQVGV CYGMQGNNLP    50
    PVSEVIALYK KSNITRMRIY DPNRAVLEAL RGSNIELILG VPNSDLQSLT 100
    NPSNAKSWVQ KNVRGFWSSV LFRYIAVGNE ISPVNRGTAW LAQFVLPAMR 150
    NIHDAIRSAG LQDQIKVSTA IDLTLVGNSY PPSAGAFRDD VRSYLDPIIG 200
    FLSSIRSPLL ANIYPYFTYA YNPRDISLPY ALFTSPSVVV WDGQRGYKNL 250
    FDATLDALYS ALERASGGSL EVVVSESGWP SAGAFAATFD NGRTYLSNLI 300
    QHVKGGTPKR PNRAIETYLF AMFDENKKQP EVEKHFGLFF PNKWQKYNLN 350
    FSAEKNWDIS TEHNATILFL KSDM 374
    Length:374
    Mass (Da):41,396
    Last modified:March 1, 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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22147 mRNA. Translation: AAA87456.1.
    PIRiS65077.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22147 mRNA. Translation: AAA87456.1 .
    PIRi S65077.

    3D structure databases

    ProteinModelPortali P52407.
    SMRi P52407. Positions 38-351.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 3313. Hev b 2.0101.
    386. Hev b 2.
    CAZyi GH17. Glycoside Hydrolase Family 17.

    Proteomic databases

    PRIDEi P52407.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00332. Glyco_hydro_17. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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(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.

    Entry informationi

    Entry nameiE13B_HEVBR
    AccessioniPrimary (citable) accession number: P52407
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 80 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