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_4328 |
| Peptide Name | CALR_PRUAR |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Prunus armeniaca |
| Plant Source (Common Name) | Apricot |
| Plant Family | Rosaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein; Lectin; Metal-binding; Repeat; Signal; Zinc | Calreticulin precursor.Endoplasmic reticulum lumen (By similarity). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | AILNYNNTNNLIKKDVPCETDQLTHVYTFIIRPDATYSILIDNLEKQTGSDNPEFKDDPELYVYPNLKYVGIELWQVKSGTLFDNILITDEPEYAKQLAEESKPDSTEESAETEAEKHDELETWGKQKDAEKAAFEELEKKLQEEESKEDPVDSDAEDDDNEAEDGEESDSLAGEWNYTSGKWNGDPNDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFLYSDWDLLPAKKIKDPEAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDMAFRVPNSSLLSLILLSLLAIASAKVFFEERFEDGWDKRWVTSEWKKDENPDAKKPEDWDDEEDGEWTAPTIPNPEYKGEWKPKKIKNPNFKGKWKAPLISVKHEQKLDCGGGYIKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVH |
| Sequence Length | 421 |
| Validation | Experimental evidence at transcript level |
| Average Molecular Weight (Da) | 48416.3 |
| Monoisotopic Molecular Weight (Da) | 48386.46 |
| Isoelectric Point (pI) | 4.4 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q9XF98 |
| NCBI | --NA-- |
| EMBL | AF134733 |
| Link to Source Databases | SPdb28925 |
|---|
| Addtional Information | FUNCTION:Molecular calcium binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).DOMAIN:Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).DOMAIN:The interaction with glycans occurs through a binding site in the globular lectin domain (By similarity).DOMAIN:The zinc binding sites are localized to the N-domain (By similarity).SIMILARITY:Belongs to the calreticulin family. |
