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_4348 |
| Peptide Name | PATB2_SOLTU |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Solanum tuberosum |
| Plant Source (Common Name) | Potato |
| Plant Family | Solanaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Plant defense; Signal; Storage protein; Vacuole | Patatin-B2 precursor (EC 3.1.1.-).Vacuole (By similarity). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | AISSFDIKTNKPVIFTKSNLAKSPELDAKMYDICYSTAAAPIYFPPHHFVDIVPFYFEHGPHIFNYSGSILGPMYDGKYLLQVLQEKLGETRVHQALTEVKKPVSKDSPETYEEALKRFAKLLSDRKKLRANKASHKQMLLLSLGTGTNSEFDKTYTAEEAAKWGPLRWMLAIQQMTNAASSYMTDLEGQLQEVDNNKDARLADYFDVIGGTSTGGLLTAMITTPNENNRPFAAAKMATTKSFLILFFMILATTSSTCAKLEEMVTVLSIDGGGIKGIIPAIILEFTHTSNGARYEFNLVDGAVATVGDPALLSLSVATRLAQEDPAFSSIKSLDYYYISTVFQARHSQNNYLRVQENALNGTTTEMDDASEANMELLVQVGETLL |
| Sequence Length | 386 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 42612.54 |
| Monoisotopic Molecular Weight (Da) | 42585.57 |
| Isoelectric Point (pI) | 5.46 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P15477 |
| NCBI | --NA-- |
| EMBL | X13178 |
| Link to Source Databases | SPdb184187 |
|---|
| Addtional Information | FUNCTION:Lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens. Can use p-nitrophenyl esters as substrats with highest activity on p- nitrophenyl caprate (C10). Also active on mono- acylglycolphosphocholines and diacylphospholipids, with highest specific activities observed were obtained with the synthetic phospholipids diC8PCho and diC9PCho. Mono-olein and myverol can also be hydrolyzed.ENZYME REGULATION:Inhibited by methyl-p-nitrophenyl- octylphosphonate.BIOPHYSICOCHEMICAL PROPERTIES:Kinetic parameters: Note=At pH 8.0, the highest specific activity is observed with phospholipids such as diC8PCho and diC9PCho and with p- nitrophenyl esters such as p-nitrophenyl caprate;DOMAIN:The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.MISCELLANEOUS:Patatin have a dual role as a somatic storage protein and as an enzyme involved in host resistance. This tuber protein represents approximately 40% of the total protein in mature tubers.SIMILARITY:Belongs to the patatin family.SIMILARITY:Contains 1 patatin domain. |
