Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
|---|
| PPepDB ID | PPepDB_5454 |
| Peptide Name | E13B_HEVBR |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Hevea brasiliensis |
| Plant Source (Common Name) | Para rubber tree |
| Plant Family | Euphorbiaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Polymorphism; Pyrrolidone carboxylic acid; Signal; Vacuole | Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform precursor,(EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase) ((1->3)-beta-,glucanase) (Beta-1,3-endoglucanase) [Contains: Glucan endo-1,3-beta-,glucosidase minor form 3; Glucan endo-1,3-beta-glucosidase minor form,2; Glucan endo-1,3-beta-glucosidase minor form 1; Glucan endo-1,3-,beta-glucosidase major form].Vacuole (Potential). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | FDATLDALYSALERASGGSLEVVVSESGWPSAGAFAATFDNGRTYLSNLIFLSSIRSPLLANIYPYFTYAYNPRDISLPYALFTSPSVVVWDGQRGYKNLFSAEKNWDISTEHNATILFLKSDMMAISSSTSGTSSSFPSRTTVMLLLFFFAASVGITDAQVGVCYGMQGNNLPNIHDAIRSAGLQDQIKVSTAIDLTLVGNSYPPSAGAFRDDVRSYLDPIIGNPSNAKSWVQKNVRGFWSSVLFRYIAVGNEISPVNRGTAWLAQFVLPAMRPVSEVIALYKKSNITRMRIYDPNRAVLEALRGSNIELILGVPNSDLQSLTQHVKGGTPKRPNRAIETYLFAMFDENKKQPEVEKHFGLFFPNKWQKYNLN |
| Sequence Length | 374 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 41396.04 |
| Monoisotopic Molecular Weight (Da) | 41370.12 |
| Isoelectric Point (pI) | 8.95 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P52407 |
| NCBI | --NA-- |
| EMBL | U22147 |
| Link to Source Databases | SPdb69273 |
|---|
| Addtional Information | 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.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;SUBUNIT:Monomer.TISSUE SPECIFICITY:Expressed at highest levels in laticifer cells of the petiole.PTM: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.PTM: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.SIMILARITY:Belongs to the glycosyl hydrolase 17 family. |
