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_5400 |
| Peptide Name | AGI_URTDI |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Urtica dioica |
| Plant Source (Common Name) | Stinging nettle |
| Plant Family | Urticaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Antimicrobial; Carbohydrate metabolism; Chitin degradation; Chitin-binding; Direct protein sequencing; Fungicide; Glycoprotein; Glycosidase; Hydrolase; Lectin; Metal-binding; Plant defense; Polysaccharide degradation; Pyrrolidone carboxylic acid; Repeat; Signal; Zinc | Lectin/endochitinase 1 precursor (EC 3.2.1.14) (Agglutinin) (UDA),(chia5.1.1) [Contains: Lectin 1]. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | EPYCGRTCENKCWSGERSDHRCGAAVGNPPCGQDRCCSVHGWCGGGNDYCGLAGQAIGEDLIQNPDLVEKDPIISFKTALWFWMSQHDNKPSCHDIVLNALKYWFDNTPSSEFQRIQMRVAAMMMRFLSAVVIMSSAMAVGLVSAQRCGSQGGGGTCPALWCCSIWGWCGDSNSAANRIPNKGVIGNIISRAFGHDDFAVRSSSIGFYKRYCDMLGVSYGHDSGSKCQYRCSSSVRGPRVALSGNSTANSIGNVVVTEPLFDQMFSHRKDCPSQGFYSYHSFLVAAESFPAFGTIGDVATRKREVAAFLAHISQATSGERSDVENPHAWGLCHINTTTVTENDFCTSSDWPCAAGKKYSPRGPIQLTHNFNY |
| Sequence Length | 372 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 40541.54 |
| Monoisotopic Molecular Weight (Da) | 40514.89 |
| Isoelectric Point (pI) | 7.23 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P11218 |
| NCBI | --NA-- |
| EMBL | M87302 |
| Link to Source Databases | SPdb6426 |
|---|
| Addtional Information | FUNCTION:Functions both as a chitinase and as a N-acetyl-D- glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties.CATALYTIC ACTIVITY:Random hydrolysis of N-acetyl-beta-D- glucosaminide 1,4-beta-linkages in chitin and chitodextrins.SUBUNIT:Monomer and homodimer. Zinc favors dimerization. Active in the monomeric form but probably inactive in the dimeric form.The interaction with glycans on the mammalian TCR and MHC molecules of the T cell and antigen-presenting cell, respectively, is inhibited by oligomers of GlcNAc.TISSUE SPECIFICITY:Rhizomes and inflorescence with immature seeds.PTM:Proteolytically processed to yield a very small protein (8.5 kDa, 86 AA) containing only the two chitin-binding domains.MASS SPECTROMETRY:Mass=9380; Method=MALDI; Range=24-372; Source=PubMed:10080699;MASS SPECTROMETRY:Mass=9380.7; Mass_error=0.4; Method=Electrospray; Range=24-372; Source=PubMed:10080699;SIMILARITY:Contains 2 chitin-binding type-1 domains. |
