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_4469 |
| Peptide Name | SCP8_ARATH |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Arabidopsis thaliana |
| Plant Source (Common Name) | Mouse-ear cress |
| Plant Family | Brassicaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Acyltransferase; Alternative splicing; Carboxypeptidase; Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Signal; Transferase; Vacuole | Serine carboxypeptidase-like 8 precursor (EC 3.4.16.-),(Sinapoylglucose--malate O-sinapoyltransferase) (EC 2.3.1.92) (SMT),(Protein SINAPOYLGLUCOSE ACCUMULATOR 1).Vacuole. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | ANDESVREALHIEKGSKGKWARCNRTIPYNHDIVSSIPYHMNNSISGYRSFLQKWLSRHPQYFSNPLYVVGDSYSGMIVPALVQEISQGNYICCEPPINLLIYSGDHDIAVPFLATQAWIRSLNYSPIHNWRPWMINNQIAGYTRAYSNKMSLKIKFLLLLVLYHHVDSASIVKFLPGFEGPLPFELETGYIGIGEDENVMTFATIKGGGHTAEYRPNETFIMFQRWISGQPLQFFYYFIKSENNPKEDPLLIWLNGGPGCSCLGGIIFENGPVGLKFEVFNGQGYMLGNPVTYMDFEQNFRIPYAYGMGLISDEIYEPMKRICNGNYYNVDPSAPSLFSTTYSWTKMANIIFLDQPVGSGFSYSKTPIDKTGDISEVKRTHESNTQCLKLTEEYHKCTAKINIHHILTPDCDVTNVTSPDCYYYPYHLIECW |
| Sequence Length | 433 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 49439.27 |
| Monoisotopic Molecular Weight (Da) | 49407.21 |
| Isoelectric Point (pI) | 5.97 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q8RUW5 |
| NCBI | --NA-- |
| EMBL | AF275313 |
| Link to Source Databases | SPdb266530 |
|---|
| Addtional Information | FUNCTION:Involved in plants secondary metabolism. Functions as acyltransferase to form the sinapate ester sinapoylmalate. May rather catalyze a transesterification reaction rather than a hydrolysis. May also have carboxypeptidase activity.CATALYTIC ACTIVITY:1-O-sinapoyl-beta-D-glucose (S)-malate = D- glucose sinapoyl-(S)-malate.ENZYME REGULATION:Slightly inhibited by phenylmethylsulphonylfluoride (PMSF).ALTERNATIVE PRODUCTS:Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8RUW5-1; Sequence=Displayed; Name=2; IsoId=Q8RUW5-2; Sequence=VSP_027464; Note=Derived from EST data. May be due to a competing donor splice site. No experimental confirmation available;TISSUE SPECIFICITY:Highly expressed in seedlings. Expressed in leaves, stems, flowers and siliques, and at low levels in roots.PTM:N-glycosylated.MISCELLANEOUS:Plants lacking SCPL8 do not contain sinapoylmalate and accumulate its biosynthetic precursor, sinapoylglucose.SIMILARITY:Belongs to the peptidase S10 family.SEQUENCE CAUTION:Sequence=AAC17816.2; Type=Erroneous gene model prediction; Sequence=AAK32769.1; Type=Frameshift; Positions=260; Sequence=AAM15006.1; Type=Erroneous gene model prediction; |
