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_4489
Peptide NamePER34_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 DescriptionCalcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole | Peroxidase 34 precursor (EC 1.11.1.7) (Atperox P34) (ATPCb).Secreted (Probable). Vacuole (Probable).
Activity Against--NA--
IC50 value--NA--
SequenceANSARGFPVIDRMKAAVERACPRTVSCADMLTIAAQQSVTLAGGPSWRVPFDLRTPTVFDNKYYVNLKERKGLIQSDQELFSSPNATDTIPLVRAYADGTLGRRDSLQAFLELANANLPAPFFTLPQLKASFRNVGLDRPSDLVALSGGHMHFSSSSTSSTWTILITLGCLMLHASLSAAQLTPTFYDRSCPNVTNIVREQTFFNAFVEAMNRMGNITPTTGTQGQIRLNCRVVNSNSLLHDVVDIVDFVSSMTFGKNQCQFILDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNRSALVDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGN
Sequence Length353
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)38832.12
Monoisotopic Molecular Weight (Da)38807.53
Isoelectric Point (pI)7.73
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_4489


External links (Uniprot, PDB and Source Information Database)
UniprotQ9SMU8
NCBI--NA--
EMBLX71794
Link to Source DatabasesSPdb187768
Addtional InformationFUNCTION:Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.FUNCTION:May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway.Exhibits a Ca(2)-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.CATALYTIC ACTIVITY:Donor H(2)O(2) = oxidized donor 2 H(2)O.COFACTOR:Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).COFACTOR:Binds 2 calcium ions per subunit (By similarity).Note=Carboxy-terminal extension appears to target the protein to vacuoles.TISSUE SPECIFICITY:Preferentially expressed in roots, but also detected in flowers, leaves and stems.DEVELOPMENTAL STAGE:Up-regulated during leaf development.INDUCTION:Late-induced by Al treatment. Expression increased over 48 hours of Al treatment. Induced by oxidative stress. Up- regulated during a continuous drought stress. Early induced by benzothiadiazol, a chemical analog of salicylic acid. Enhanced expression following both compatible or incompatible pathogen attacks.MISCELLANEOUS:There are 73 peroxidase genes in A.thaliana.SIMILARITY:Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.SEQUENCE CAUTION:Sequence=AAG40051.2; Type=Frameshift; Positions=176;