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_5918 |
| Peptide Name | FKB15_VICFA |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Vicia faba |
| Plant Source (Common Name) | Broad bean |
| Plant Family | Fabaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Direct protein sequencing; Endoplasmic reticulum; Isomerase; Rotamase; Signal; Stress response | FK506-binding protein 2 precursor (EC 5.2.1.8) (Peptidyl-prolyl cis-,trans isomerase) (PPIase) (Rotamase) (15 kDa FKBP) (FKBP-15).Endoplasmic reticulum lumen (Potential). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | KRKLKIPAKLGYGEQGSPPTIPGGATLIFDTELVGVNDKSLSEEKSTSSEKVKVHYRGKLTDGTVFDSSFERNSPIDFELGGGQVIKGWDQGLLGMCLGELMKLFSIFLIFTIFIIASALVAAKSAADVTELQIGVKYKPASCEVQAHKGD |
| Sequence Length | 151 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 16223.71 |
| Monoisotopic Molecular Weight (Da) | 16213.51 |
| Isoelectric Point (pI) | 6.93 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q41649 |
| NCBI | --NA-- |
| EMBL | U52045 |
| Link to Source Databases | SPdb83520 |
|---|
| Addtional Information | FUNCTION:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.CATALYTIC ACTIVITY:Peptidylproline (omega=180) = peptidylproline (omega=0).ENZYME REGULATION:Inhibited by both FK506 and rapamycin.TISSUE SPECIFICITY:Ubiquitously expressed.INDUCTION:By heat shock.SIMILARITY:Belongs to the FKBP-type PPIase family. FKBP2 subfamily.SIMILARITY:Contains 1 PPIase FKBP-type domain. |
