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_5087
Peptide NameXIP1_WHEAT
PMID(s)--NA--
Plant Source (Scientific Name)Triticum aestivum
Plant Source (Common Name)Wheat
Plant FamilyPoaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function Description3D-structure; Direct protein sequencing; Glycoprotein; Plant defense; Secreted; Signal | Xylanase inhibitor protein 1 precursor (XIP-1) (XIP-I) (Class III,chitinase homolog).Secreted (Potential).
Activity Against--NA--
IC50 value--NA--
SequenceDGVDLFLEHGTPADRYDVLALELAKHNIRGGPGKPLHLTATVRCGYPPAAHVGRALATGIFERVHVRTYESDKWCNQNLGWEGSWDKWTAAYPATRFYVGKYYALREACDSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSSVGADIKHCQSKGLTADDKSHQWVHPKNVYYGVAPVAQKKDNYGGIMLWDRYFDKQTNYSSLIMAPLAARRPACLLALLSVAAALFLTPTALAAGGKTGQVTVFWGRNKAEGSVPVSLSIGGYGTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWL
Sequence Length304
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)33274.73
Monoisotopic Molecular Weight (Da)33253.61
Isoelectric Point (pI)8.67
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_5087


External links (Uniprot, PDB and Source Information Database)
UniprotQ8L5C6
NCBI--NA--
EMBLAJ422119
Link to Source DatabasesSPdb320525
Addtional InformationFUNCTION:Fungal xylanase inhibitor. Possesses competitive inhibiting activity against fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10) and family 11 (GH11). Possesses also inhibitory activity towards barley alpha- amylases. Binding to xylanases or amylases is necessary for inhibition activity. May function in plant defense against secreted fungal pathogen xylanases. Is similar to class III chitinases, but does not exhibit chitinase activity.SUBUNIT:Binds to fungal GH10 and GH11 xylanases. Forms also a ternary complex with barley alpha-amylase 1 (AMY1) and insoluble starch.DEVELOPMENTAL STAGE:Expressed in immature embryos 3 weeks after pollination, in roots and shoots of 3 day and 5 day old seedlings, and in roots of 10 day old seedlings.INDUCTION:By wounding, methyl jasmonate, and by E.graminis infection in leaves.SIMILARITY:Belongs to the glycosyl hydrolase 18 family. Xylanase inhibitor subfamily.