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_5353 |
| Peptide Name | ASPR_HORVU |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Hordeum vulgare |
| Plant Source (Common Name) | Barley |
| Plant Family | Poaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Aspartyl protease; Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Signal; Vacuole; Zymogen | Phytepsin precursor (EC 3.4.23.40) (Aspartic proteinase) [Contains:,Phytepsin 32 kDa subunit; Phytepsin 29 kDa subunit; Phytepsin 16 kDa,subunit; Phytepsin 11 kDa subunit].Vacuole. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | EHTYVPVTQKGYWQFDMGDVLVGGKSTGFCAGGCAAIADSGTSLLAGPTAEYILKVGEGAAAQCISGFTAMDIPPPRGPLWILGDVFMGPYHTVFDYGKLFDTGSSNLWVPSAKCYFSIACYLHSRYKAGASSTYKKNGKPAAIQYGTGSIAGYFSEDSVTVGDLVVKDQEFIEATKEPGITFLVAKFDGILGLGFKEISIITEINEKIGAAGVVSQECKTIVSQYGQQILDLLLAETQPKKICSQVGLCMGTRGLALALLAAVLLLQTVLPAASEAEGLVRIALKKRPIDRNSRVATGLRIGFAKAASGGEEQPLLSGANPLRSEEEGDIVALKNYMNAQYFGEIGVGTPPQKFTVITFDGTRGVSAGIRSVVDDEPVKSNGLRADPMCSACEMAVVWMQNQLAQNKTQDLILDYVNQLCNRLPSPMGESAVDCGSLGSMPDIEFTIGGKKFALKPEVGKAVPVWYKMIEQGLVSDPVFSFWLNRHVDEGEGGEIIFGGMDPKHYVG |
| Sequence Length | 508 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 54226.21 |
| Monoisotopic Molecular Weight (Da) | 54191.4 |
| Isoelectric Point (pI) | 5.23 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P42210 |
| NCBI | --NA-- |
| EMBL | X56136 |
| Link to Source Databases | SPdb17108 |
|---|
| Addtional Information | CATALYTIC ACTIVITY:Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.SUBUNIT:Heterodimer of two subunits (29 kDa and 11 kDa) processed from the precursor molecule. A large enzyme (32 kDa and 16 kDa) is an intermediate precursor form.TISSUE SPECIFICITY:Embryo and leaf.SIMILARITY:Belongs to the peptidase A1 family.SIMILARITY:Contains 1 saposin B-type domain. |
