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_5322 |
| Peptide Name | CYSEP_VIGMU |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Vigna mungo |
| Plant Source (Common Name) | Rice bean, Black gram |
| Plant Family | Fabaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease; Vacuole; Zymogen | Vignain precursor (EC 3.4.22.-) (Bean endopeptidase) (Cysteine,proteinase) (Sulfhydryl-endopeptidase) (SH-EP) [Contains: Vignain-1;,Vignain-2].Endoplasmic reticulum lumen. Vacuole, aleurone grain. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | EFIKQKGGITTESNYPYTAQEGTCDESKVNDLAVSIDGHENVPVNDENALGSKVNHHKMFRGSQHGSGTFMYEKVGSVPASVDWRKKGAVTDVKDQGQCGGTNYWIVRNSWGPEWGEQGYIRMQRNISKKEGLCGIAMMASYPIKNSSDNLKAVANQPVSVAIDAGGSDFQFYSEGVFTGDCNTDLNHGVAIVGYGTTVDMAMKKLLWVVLSLSLVLGVANSFDFHEKDLESEESLWDLYERWRSHHTVSPTGSLSSPKDELRSLGEKHKRFNVFKANVMHVHNTNKMDKPYKLKLNKFADMTNHEFRSTYASCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDKEENQGCNGGLMESAF |
| Sequence Length | 362 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 40222.05 |
| Monoisotopic Molecular Weight (Da) | 40196.49 |
| Isoelectric Point (pI) | 5.87 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
| Uniprot | P12412 |
| NCBI | --NA-- |
| EMBL | X15732 |
| Link to Source Databases | SPdb55633 |
| Addtional Information | FUNCTION:Thought to be involved in the hydrolysis of stored seed proteins.CATALYTIC ACTIVITY:Hydrolysis of proteins, such as azocasein.Preferential cleavage: Asn-|-Xaa in small molecule substrates such as Boc-Asn-|-OPHNO(2).PTM:The mature protein is not glycosylated.PTM:The precursor stored in the endoplasmic reticulum lumen is processed during the transport to proteins bodies to two dominant mature forms that differ by a single amino acid residue at the N- terminus.SIMILARITY:Belongs to the peptidase C1 family. |