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_4688 |
| Peptide Name | CYSEP_RICCO |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Ricinus communis |
| Plant Source (Common Name) | Castor bean |
| Plant Family | Euphorbiaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease | Vignain precursor (EC 3.4.22.-) (Cysteine endopeptidase).Note=The pro-endopeptidase accumulates in the ricinosomes. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | AVANQPVSVAIDAGGSDFQFYSEGVFTGSCGTELDHGVAIVGYGTTIDGTGIKSSPKDELIKQRGGITTEANYPYEAYDGTCDVSKENAPAVSIDGHENVPENDENALLKKVKHHRMFRGGPRGNGTFMYEKVDTVPASVDWRKKGAVTSVKDQGQCGSCKYWTVKNSWGPEWGEKGYIRMERGISDKEGLCGIAMEASYPIKKSSNNPSLHEKQKRFNVFKHNAMHVHNANKMDKPYKLKLNKFADMTNHEFRNTYSGSMQKFILLALSLALVLAITESFDFHEKELESEESLWGLYERWRSHHTVSRSWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDTDQNQGCNGGLMDYAFEF |
| Sequence Length | 360 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 40110.92 |
| Monoisotopic Molecular Weight (Da) | 40085.52 |
| Isoelectric Point (pI) | 5.98 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | O65039 |
| NCBI | --NA-- |
| EMBL | AF050756 |
| Link to Source Databases | SPdb55632 |
|---|
| Addtional Information | FUNCTION:Involved in programmed cell death.CATALYTIC ACTIVITY:Pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions.ENZYME REGULATION:Low pH triggers activation of the protease and removal of the propeptide and the KDEL motif.DEVELOPMENTAL STAGE:Released during the final stage of cellular desintegration in the senescing endosperm of germinating bean.PTM:The potential N-glycosylation site at Asn-115 is not glycosylated.MISCELLANEOUS:The pro-endopeptidase goes directly from the ER lumen to the ricinosome, and the secretory pathway via the Golgi apparatus is not involved in the ricinosome biogenesis.SIMILARITY:Belongs to the peptidase C1 family. |
