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_5376 |
| Peptide Name | CP20A_ARATH |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Arabidopsis thaliana |
| Plant Source (Common Name) | Mouse-ear cress |
| Plant Family | Brassicaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Chaperone; Complete proteome; Cyclosporin; Endoplasmic reticulum; Isomerase; Rotamase; Secreted; Signal | Peptidyl-prolyl cis-trans isomerase CYP20-1 precursor (EC 5.2.1.8),(PPIase CYP20-1) (Rotamase cyclophilin-7) (Cyclophilin of 20 kDa 1).Endoplasmic reticulum (By similarity). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | ELPLFITTVTTSWLDGRHVVFGKVVTGMDVVYKVEAEGNQSGTPKSKVVIVDSGIVMGLFGKTVPKTVENFRALCTGEKGIGKNGKALHYKGSSFHRIIPSFMLMASSVTLLLWSLLLLGTLSAIQAKKSKENLKEITHKVYFDVEIDGKAAGRQGGDFTHGNGMGGESIYGEKFADENFKLKHTGPGFLSMANAGQDTNGSQF |
| Sequence Length | 204 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 21961.25 |
| Monoisotopic Molecular Weight (Da) | 21947.34 |
| Isoelectric Point (pI) | 9.08 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q9SP02 |
| NCBI | --NA-- |
| EMBL | AF192490 |
| Link to Source Databases | SPdb47005 |
|---|
| Addtional Information | FUNCTION:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Seems to be involved in root development.CATALYTIC ACTIVITY:Peptidylproline (omega=180) = peptidylproline (omega=0).ENZYME REGULATION:Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase (By similarity).SUBUNIT:Interacts with the PP2A A subunit PP2AA1/RCN1.Secreted (By similarity).TISSUE SPECIFICITY:Ubiquitous, mostly in aerial organs. Higher levels in leaf and buds, and lower levels in seedlings.SIMILARITY:Belongs to the cyclophilin-type PPIase family.SIMILARITY:Contains 1 PPIase cyclophilin-type domain. |
