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 IDPPepDB_5063
Peptide NameCP19D_ARATH
PMID(s)--NA--
Plant Source (Scientific Name)Arabidopsis thaliana
Plant Source (Common Name)Mouse-ear cress
Plant FamilyBrassicaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function DescriptionChaperone; Complete proteome; Cyclosporin; Cytoplasm; Endoplasmic reticulum; Isomerase; Membrane; Rotamase; Signal | Peptidyl-prolyl cis-trans isomerase CYP19-4 precursor (EC 5.2.1.8),(PPIase CYP19-4) (Rotamase CYP19-4) (Cyclophilin of 19 kDa 4),(Cyclophilin-5).Cytoplasm. Membrane. Endoplasmic reticulum.
Activity Against--NA--
IC50 value--NA--
SequenceDFTHGNGMGGESIYGQKFADENFKLKHTGPGVLSMANSGEDTNGSQFFITGLFGKAVPKTAENFRALCTGEKGVGKSGKPLHYKGSKFHRIIPSFMIQGGLMAKASFILLGTLFLFGAIASIQAKEDLKEVTHKVYFDVEIDGKSAGRVVITVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVVIADSGELP
Sequence Length201
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)21533.73
Monoisotopic Molecular Weight (Da)21520.13
Isoelectric Point (pI)9.06
Method / Extraction--NA--


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_5063


External links (Uniprot, PDB and Source Information Database)
UniprotQ8LDP4
NCBI--NA--
EMBLAF020433
Link to Source DatabasesSPdb46957
Addtional InformationFUNCTION:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved during embryogenesis and organ development by regulating the folding of EMB30/GNOM, and thus, by modulating its activity.CATALYTIC ACTIVITY:Peptidylproline (omega=180) = peptidylproline (omega=0).ENZYME REGULATION:Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.SUBUNIT:Interacts with EMB30/GNOM.Note=Mostly cytoplasmic, also membrane-associated. Present in endoplasmic reticulum and barely secreted.TISSUE SPECIFICITY:Ubiquitous, mostly in aerial organs (at protein level).DEVELOPMENTAL STAGE:Mostly expressed in both apical and basal regions in peduncles and stems (including upper roots) before the bolting stage. Later restricted in the apical region. During embryogenesis, accumulates in all cells during globular stage.From the heart stage, more expressed in inner cells than in epidermal cells (at protein level).INDUCTION:Slightly induced by cold and salt stresses.SIMILARITY:Belongs to the cyclophilin-type PPIase family.SIMILARITY:Contains 1 PPIase cyclophilin-type domain.