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_5108
Peptide NameITRA_SOYBN
PMID(s)--NA--
Plant Source (Scientific Name)Glycine max
Plant Source (Common Name)Soybean
Plant FamilyFabaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function Description3D-structure; Direct protein sequencing; Protease inhibitor; Serine protease inhibitor; Signal | Trypsin inhibitor A precursor (Kunitz-type trypsin inhibitor A).
Activity Against--NA--
IC50 value--NA--
SequenceDKESLAKKNHGLSRSEEFNNYKLVFCPQQAEDDKCGDIGISIDHDDGTRRLVVSKNKPLVVQFQKLFDSFAVIMLCVGIPTEWSVVEDLPEGPAVKIGENKDAMDGWFRLERVSDDGGIRAAPTGNERCPLTVVQSRNELDKGIGTIISSPYRIRFIAEGHPLSLKMKSTIFFLFLFCAFTTSYLPSAIADFVLDNEGNPLENGGTYYILSDITAF
Sequence Length216
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)24005.29
Monoisotopic Molecular Weight (Da)23990.09
Isoelectric Point (pI)4.95
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_5108


External links (Uniprot, PDB and Source Information Database)
UniprotP01070
NCBI--NA--
EMBLS45092
Link to Source DatabasesSPdb128579
Addtional InformationFUNCTION:Inhibition of trypsin.MISCELLANEOUS:The sequence of variant A is shown.MISCELLANEOUS:Electrophoresis identifies three genetically distinct variants, A, B, and C, that are inherited as codominant alleles.SIMILARITY:Belongs to the protease inhibitor I3 (leguminous Kunitz-type inhibitor) family.CAUTION:Ref.4 sequence was originally thought to be rat caltrin.A number of peptide fragments were derived from a trypsin digest of caltrin and soybean trypsin inhibitor was used to stop the digestion. It appears that some of the inhibitor was also digested and sequenced.