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_5594 |
| Peptide Name | NLTP1_HORVU |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Hordeum vulgare |
| Plant Source (Common Name) | Barley |
| Plant Family | Poaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Direct protein sequencing; Lipid-binding; Lipoprotein; Signal; Transport | Non-specific lipid-transfer protein 1 precursor (LTP 1) (Probable,amylase/protease inhibitor). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | GECCNGVRDLHNQAQSSGDRQTVCNCLKGIARGIHNLNLNNAASIPSKCNMARAQVLLMAAALVLMLTAAPRAAVALNCGQVDSKMKPCLTYVQGGPGPSVNVPYTISPDIDCSRIY |
| Sequence Length | 117 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 12301.24 |
| Monoisotopic Molecular Weight (Da) | 12293.07 |
| Isoelectric Point (pI) | 8.71 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P07597 |
| NCBI | --NA-- |
| EMBL | M15207 |
| Link to Source Databases | SPdb170369 |
|---|
| Addtional Information | FUNCTION:Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.TISSUE SPECIFICITY:Aleurone layer of developing and germinating seeds.BIOTECHNOLOGY:During brewing process, structural and chemical modifications of the protein occur. Both unfolding of the structure and glycation should increased the amphiphilicity of the protein, leading to foam-promoting forms that concentrate in beer foams.SIMILARITY:Belongs to the plant LTP family.CAUTION:Was originally thought to be an inhibitor of alpha- amylase or of a protease and was known asPAPI:probable alpha- amylase/protease inhibitor.SEQUENCE CAUTION:Sequence=CAA42832.1; Type=Erroneous gene model prediction;WEB RESOURCE:Name=Protein Spotlight; Note=One beer please - Issue 48 of July 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt048.shtml"; |
