DRAMP_ID Sequence Sequence_Length Name Swiss_Prot_Entry Family Gene Source Activity Protein_existence Structure Structure_Description PDB_ID Comments Target_Organism Hemolytic_activity Linear/Cyclic/Branched N-terminal_Modification C-terminal_Modification Other_Modifications Stereochemistry Cytotoxicity Binding_Traget Pubmed_ID Reference Author Title DRAMP03217 FRGLAKLLKIGLKSFARVLKKVLPKAAKAGKALAKSMADENAIRQQNQ 48 "M-oxotoxin-Ot1a (Oxyopinin-1, Oxki1; spiders, Arthropods, animals)" P83247 Not found Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Protein level Alpha helix Not found None "Function: Disrupts cell membranes, particularly those rich in phosphocholine, through formation of pores. Has antimicrobial activity against Gram-negative bacterium E. coli, Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep erythrocytes. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides." "[Ref.11976325]Gram-negative bacterium: Escherichia coli (MIC=1.6 ?M);##Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus (MIC=6.2 ?M)." [Ref.11976325]100% hemolytic activity at 50 ?M against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11976325##15328050 J Biol Chem. 2002 Jun 28;277(26):23627-23637.##Biochim Biophys Acta. 2004 Aug 30;1664(2):182-188. "Corzo G, Villegas E, G¨®mez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T.##Belokoneva OS, Satake H, Mal'tseva EL, Pal'mina NP, Villegas E, Nakajima T, Corzo G." "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins.##Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size." DRAMP03222 GFGALFKFLAKKVAKTVAKQAAKQGAKYVVNKQME 35 "M-ctenitoxin-Cs1a (M-CNTX-Cs1a; Cupiennin-1a; spiders, Arthropods, animals)" P83619 Belongs to the cupiennin family Not found Cupiennius salei (Wandering spider) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Protein level Alpha helix (3 helices; 11 residues) "The peptide adopts a helix-hinge-helix structure in a membrane mimicking solvent. The hinge may play a role in allowing the amphipathic N-terminal helix and polar C-terminal helix to orient independently upon membrane binding, in order to achieve maximal antibacterial efficacy.(Ref.2)" 2K38 resolved by NMR. "Function: Has antimicrobial activity. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane Function: with its amphipathic structure. Synergistically increases the insecticidal activity of CSTX-1, CSTX-9, and CSTX-13 by up to 65%. Also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. LD50 is 5.9 pmol/mg on Drosophila. " "[Ref.11792701]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.31-0.63 ?M), Pseudomonas aeruginosa ATCC 27853 (MIC=0.31-0.63 ?M);##Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=0.31-0.63 ?M), Enterococcus faecalis ATCC 29212 (MIC=2.50-5.00 ?M)." [Ref.11792701]EC50=24.4 ¦ÌM against human red blood cells. Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet calcium calmodulin 11792701##17319697 J Biol Chem. 2002 Mar 29;277(13):11208-11216.##Biochemistry. 2007 Mar 20;46(11):3576-3585. "Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W.##Pukala TL, Boland MP, Gehman JD, Kuhn-Nentwig L, Separovic F, Bowie JH." "Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae).##Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers." DRAMP03236 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 "M-zodatoxin-Lt8a (M-ZDTX-Lt8a; Cytoinsectotoxin-1a, CIT-1a; spiders, Arthropods, animals)" "P85253, B3W6H9" Belongs to the cytoinsectotoxin family cit 1-1 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Protein level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S. carnaria, and against the cockroach N. cinerea. CIT 1a Has hemolytic activity against human erythrocytes, and cytolytic activity against insect Sf9 cells in the same concentration range. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland. Toxic dose: LD50 is 5 ?g/g for adult and 20 ?g/g for larvae of flesh fly S. carnaria. LD50 is 500 ?g/g for cockroach N. cinerea." "[Ref.18215128]Gram-positive bacteria: Arthrobacter globiformis VKM Ac-1112 (MIC=0.5 ?M), Bacillus subtilis VKM B-501 (MIC=0.9 ?M), Micrococcus luteus (MIC>30 ?M), Staphylococcus aureus (MIC>30 ?M);##Gram-negative bacteria: Escherichia coli C600 (MIC=0.5 ?M), E. coli DH5alpha (MIC=0.9 ?M), E. coli MH1 (MIC=0.5 ?M), Pseudomonas aeruginosa PAO1 (MIC=1.9 ?M), Pseudomonas fluorescens VKM B-894 (MIC=3.8 ?M)." [Ref.18215128]EC50=6 ¦ÌM against human erythrocytes Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP00322 SEPQXGRDAGGAL 13 Insecticidal protein LA-a (Latex abundant protein a; Plant defensin) P86799 Not found Not found Morus alba (White mulberry) Insecticidal Protein level Not found Not found None "Function: Has insecticidal activity when consumed by D. melanogaster larvae. Has low chitinase and chitosanase activity. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan. PTM: Glycosylated; contains galactose." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Chitin-binding 20109180 BMC Biochem. 2010 Jan 28;11:6. "Kitajima S, Kamei K, Taketani S, Yamaguchi M, Kawai F, Komatsu A, Inukai Y." Two chitinase-like proteins abundantly accumulated in latex of mulberry show insecticidal activity. DRAMP00323 SEQQXGRDVGGAL 13 Insecticidal protein LA-b (Latex abundant protein b; Plant defensin) P86800 Not found Not found Morus alba (White mulberry) Insecticidal Protein level Not found Not found None "Function: Has insecticidal activity when consumed by D.melanogaster larvae. Has low chitinase and chitosanase activity. Catalytic activity: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan. PTM: Glycosylated; contains galactose." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20109180 BMC Biochem. 2010 Jan 28;11:6. "Kitajima S, Kamei K, Taketani S, Yamaguchi M, Kawai F, Komatsu A, Inukai Y." Two chitinase-like proteins abundantly accumulated in latex of mulberry show insecticidal activity. DRAMP00804 GIPCAESCVYIPCTVTALLGCSCSNRVCYN 30 Cycloviolacin-O1 (Plant defensin) P82230 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Combine helix and strand structure Not found 1NBJ resolved by NMR. "Function: Probably participates in a plant defense mechanism. It shows haemolytic activity. PTM: This is a cyclic peptide which contains three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L [Ref.20575512] Cytotoxicity on the human lymphoma cell line U-937 GTB(IC50 around 1 ?M). Not found 16872274##10600388##12482868 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336.##J Biol Chem. 2003 Mar 7;278(10):8606-8616. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C.##Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##Twists, knots, and rings in proteins. Structural definition of the cyclotide framework." DRAMP00805 GIPCGESCVWIPCISSAIGCSCKSKVCYRN 30 Cycloviolacin-O2 (Plant defensin) "P58434, P85526" Belongs to the cyclotide family Not found Viola biflora (Yellow wood violet) & Viola odorata (Sweet violet) Insecticidal Protein level Combine helix and strand structure Not found "2KCG, 2KNM, 2KNN resolved by NMR." "Function: Probably participates in a plant defense mechanism. Has strong cytotoxic activity against a variety of drug-resistant and drug-sensitive human tumor cell lines, and against primary chronic lymphocytic leukemia and ovarian carcinoma cells. Has weaker cytotoxic activity against normal lymphocytes. Has hemolytic activity. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." "[Ref.16872274]Human tumor cell lines: RPMI-8226/s (IC50=0.12 ?M), RPMI-8226/Dox40 (IC50=0.12 ?M), RPMI-8226/LR-5 (IC50=0.12 ?M), U-937GTB (IC50=0.26 ?M), U-937Vcr (IC50=0.20 ?M), ACHN (IC50=0.22 ?M), CCRF-CEM (IC50=0.11 ?M), CCRF-CEM/VM-1 (IC50=0.14 ?M), NCI-H69 (IC50=0.12 ?M), NCI-H69AR (IC50=0.26 ?M)." [Ref:16872274] It has 35% hemolytic activity at 1.0 ¦ÌM and 60% hemolytic activity at 1.5 ¦ÌM against human type A red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L "[Ref.20580652] Cytotoxicity: U251(IC50=17.05¦Ìg/mL), MDA-MB-231(IC50=4.81¦Ìg/mL), A549(IC50=5.99¦Ìg/mL), DU145(IC50=5.08¦Ìg/mL), BEL-7402(IC5=6.07¦Ìg/mL)." Not found 16872274##10600388##16872274 "Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Biochem J . 2006 Nov 15;400(1):1-12. " "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C.##David C Ireland 1, Michelle L Colgrave, David J Craik" "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability" DRAMP00806 GIPCGESCVWIPCLTSAIGCSCKSKVCYRN 30 Cycloviolacin-O3 (Plant defensin) P58435 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00807 GIPCGESCVWIPCISSAIGCSCKNKVCYRN 30 Cycloviolacin-O4 (Plant defensin) P58436 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00808 GTPCGESCVWIPCISSAVGCSCKNKVCYKN 30 Cycloviolacin-O5 (Plant defensin) P58437 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00809 GTLPCGESCVWIPCISAVGCSCKSKVCYKN 30 Cycloviolacin-O6 (Plant defensin) P58438 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00810 SIPCGESCVWIPCTITALAGCKCKSKVCYN 30 Cycloviolacin-O7 (Plant defensin) P58439 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00811 GTLPCESCVWIPCISSVVGCSCKSKVCYKN 30 Cycloviolacin-O8 (Cyclotide c1; Plant defensin) "P58440, Q5USN9" Belongs to the cyclotide family Voc1 Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L "[Ref.29734037] Cytotoxicity against three cancer cell lines: MDA-MB-231 breast (IC50=1.15?¦ÌM), PC-3 prostate (IC50=1.05?¦ÌM), and OVCAR-3 ovarian (IC50=0.80?¦ÌM). Cytotoxicity against non-cancerous human dermal fibroblast cells was determined to be ?3¡Á less (3.13?¦ÌM) than cancer cell lines " Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00812 GIPCGESCVWIPCLTSAVGCSCKSKVCYRN 30 Cycloviolacin-O9 (Vbc5; Plant defensin) "P58441, B1NRR2" Belongs to the cyclotide family Not found Viola odorata (Sweet violet) & Viola biflora (Yellow wood violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388##18191970 Biochem J. 2006 Nov 15;400(1):1-12.##J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Phytochemistry. 2008 Feb;69(4):939-952. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C.##Herrmann A, Burman R, Mylne JS, Karlsson G, Gullbo J, Craik DJ, Clark RJ, G?ransson U." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity." DRAMP00813 GIPCGESCVYIPCLTSAVGCSCKSKVCYRN 30 Cycloviolacin-O10 (Plant defensin) P58442 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00814 GTLPCGESCVWIPCISAVVGCSCKSKVCYKN 31 Cycloviolacin-O11 (Cyclotide c2; Plant defensin) "P58443, Q5USP0" Belongs to the cyclotide family Voc2 Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 16872274##10600388 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ.##Craik DJ, Daly NL, Bond T, Waine C." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability..##Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif." DRAMP00816 GIPCGESCVWIPCISAAIGCSCKSKVCYRN 30 Cycloviolacin-O13 (Cyclotide c3; Plant defensin) Q5USN8 Belongs to the cyclotide family Voc3 Viola odorata (Sweet violet) "Antiviral,Insecticidal " Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=320 nM). [Ref:16872274] It has 50% hemolytic activity at 1.0 ¦ÌM and 75% hemolytic activity at 1.5 ¦ÌM against human type A red blood cells Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=6400 nM. Not found 16872274##18008336 Biochem J. 2006 Nov 15;400(1):1-12.##Biopolymers. 2008;90(1):51-60. "Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. " "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability.##Cyclotides as natural anti-HIV agents." DRAMP00817 GSIPACGESCFKGKCYTPGCSCSKYPLCAKN 31 Cycloviolacin-O14 (Plant defensin) P85177 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) "Antiviral,Insecticidal " Protein level Combine helix and strand structure Cycloviolacin O14 is shown to contain the CCK motif. 2GJ0 resolved by NMR. "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 6-20; 10-22; 15-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=440 nM). [Ref:16872274] It has 3% hemolytic activity at 1.0 ¦ÌM and 13% hemolytic activity at 1.5 ¦ÌM against human type A red blood cells Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys6 and Cys20; Cys10 and Cys22; Cys15 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=4800 nM. Not found 16872274##18008336 Biochem J. 2006 Nov 15;400(1):1-12.##Biopolymers. 2008;90(1):51-60. "Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. " "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability.##Cyclotides as natural anti-HIV agents." DRAMP00818 GLVPCGETCFTGKCYTPGCSCSYPICKKN 29 Cycloviolacin-O15 (Plant defensin) P85178 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database [Ref:16872274] It has 6% hemolytic activity at 1.0 ¦ÌM and 26% hemolytic activity at 1.5 ¦ÌM against human type A red blood cells Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00819 GLPCGETTCFTGKCYTPGCSCSYPICKKIN 30 Cycloviolacin-O16 (Plant defensin) P85179 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-18; 8-20; 13-25." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys18; Cys8 and Cys20; Cys13 and Cys25. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00820 GIPCGESCVWIPGISAAIGCSCKNKVCYRN 30 Cycloviolacin-O17 (Plant defensin) P85180 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which contains three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00821 GIPCGESCVYIIPCTVTALAQCKCKSKVCYN 31 Cycloviolacin-O18 (Plant defensin) P85181 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-21; 8-23; 13-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys21; Cys8 and Cys23; Cys13 and Cys28. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00822 GTLPCGESCVWIPCISSVVGCSCKSKVCYKD 31 Cycloviolacin-O19 (Plant defensin) P85182 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-21; 9-23; 14-28." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys21; Cys9 and Cys23; Cys14 and Cys28. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00823 GIPCGESCVWIPCLTSAIGCSCKSKVCYKD 30 Cycloviolacin-O20 (Plant defensin) P85183 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 4-20; 8-22; 13-27." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys4 and Cys20; Cys8 and Cys22; Cys13 and Cys27. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00824 GLPVCGETCVTGSCYTPGCTCSWPVCTRN 29 Cycloviolacin-O21 (Plant defensin) P85184 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00825 GLPICGETCVGGTCNTPGCTCSWPVCTRN 29 Cycloviolacin-O22 (Plant defensin) P85185 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00826 GLPTCGETCFGGTCNTPGCTCDSSWPICTHN 31 Cycloviolacin-O23 (Plant defensin) P85186 Belongs to the cyclotide family Not found Viola odorata (Sweet violet) Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-26." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys26. L No cytotoxicity information found Not found 16872274 Biochem J. 2006 Nov 15;400(1):1-12. "Ireland DC, Colgrave ML, Craik DJ." "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability." DRAMP00857 GLPVCGETCFGGTCNTPGCSCTWPICTRD 29 Kalata-B2 (Plant defensin) P58454 Belongs to the cyclotide family OAK4 Oldenlandia affinis Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. Inhibitory effect on the growth and development of Helicoverpa armigera larvae suggests a role for the cyclotides in plant defense. Has hemolytic activity. PTM: Kalata-B2 is a cyclic peptide which contains three disulfide bonds 5-19; 9-21; 14-26." [Ref.17534989]Insects: Helicoverpa armigera [Ref.20564013] HD50=3.3¡À1.9 ¦ÌM against Human red blood cells . Cyclic No specific N-terminal No specific C-terminal "Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys26." L No cytotoxicity information found Not found 10600388##15654741##17534989##20564013 "J Mol Biol. 1999 Dec 17;294(5):1327-1336.##Biochemistry. 2005 Jan 25;44(3):851-860.##Chembiochem. 2007 Jun 18;8(9):1001-1011.##Biopolymers . 2010;94(5):647-58." "Craik DJ, Daly NL, Bond T, Waine C.##Jennings CV, Rosengren KJ, Daly NL, Plan M, Stevens J, Scanlon MJ, Waine C, Norman DG, Anderson MA, Craik DJ.##Plan MR, G?ransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.##Manuel R Plan, K Johan Rosengren, Lillian Sando, Norelle L Daly, David J Craik" "Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.##Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: do M?bius strips exist in nature?##The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.##Structural and biochemical characteristics of the cyclotide kalata B5 from Oldenlandia affinis" DRAMP00858 GLPTCGETCFGGTCNTPGCTCDPWPICTRD 30 Kalata-B3 (Plant defensin) P58455 Belongs to the cyclotide family OAK2 Oldenlandia affinis Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: Kalata-B3 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database [Ref:11535828] It has hemolytic activity Cyclic No specific N-terminal No specific C-terminal Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys27. L No cytotoxicity information found Not found 11535828 Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10614-9. "Jennings C, West J, Waine C, Craik D, Anderson M." Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. DRAMP00861 GLPVCGETCFGGTCNTPGCSCSSWPICTRN 30 Kalata-B6 (Plant defensin) P58455 Belongs to the cyclotide family OAK2 Oldenlandia affinis Insecticidal Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: Kalata-B6 are cyclic peptides which may contain three disulfide bonds 5-19; 9-21; 14-27." No MICs found in DRAMP database [Ref.20564013] HD50=7.7¡À1.3 ¦ÌM against Human red blood cells. Cyclic No specific N-terminal No specific C-terminal "Disulfide bonds between Cys5 and Cys19,Cys9 and Cys21,Cys14 and Cys27." L No cytotoxicity information found cell membrabce 17534989 Chembiochem. 2007 Jun 18;8(9):1001-1011. "Plan MR, G?ransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ." "The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides." DRAMP02762 WLGSALKIGAKLLPSVVGLFKKKKQ 25 "Ponericin-W1 (ants, insects, animals)" P82423 Belongs to the ponericin-W family Not found Pachycondyla goeldii (Ponerine ant) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal" Protein level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." "[Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 10mm), B. megaterium ATCC 9885b(Inhibition zone = 12.5mm), B. stearothermophilus CIP 675(Inhibition zone = 17mm), B. subtilis ATCC 6623(Inhibition zone = 12mm), Enterococcus faecalis CIP 636(Inhibition zone = 6mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 15mm), Streptococcus pyogenes CIP 561(Inhibition zone = 10mm), S. sanguinis CIP 55128(Inhibition zone = 7.5mm), Listeria ivanovii LMA 94d(Inhibition zone = 11.5mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 9.5mm), Micrococcus luteus CIP 5345(Inhibition zone = 11.5mm), Staphylococcus aureus CIP 677(Inhibition zone = 10mm), Staphylococcus aureus LMA(Inhibition zone = 13.5mm), S. epidermidis CIP 53134(Inhibition zone = 13.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 8mm), Enterobacter cloacae CIP 6085(Inhibition zone = 3mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 6.5mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(Inhibition zone = 3mm), Serratia marcescens LMA TP(no detected), Flavobacterium meningosepticum CIP 6057(Inhibition zone = 6mm), Pseudomonas aeruginosa CIP A22(Inhibition zone = 16mm)." [Ref.11279030]2mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 ¦Ìl of the peptide solution and placed overnight at 4¡æ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. "Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J." "Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii." DRAMP02763 WLGSALKIGAKLLPSVVGLFQKKKK 25 "Ponericin-W2 (ants, insects, animals)" P82424 Belongs to the ponericin-W family Not found Pachycondyla goeldii (Ponerine ant) "Antibacterial, Antifungal, Insecticidal, Antimicrobial" Protein level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria. Has insecticidal activities. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. "Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J." "Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii." DRAMP02764 GIWGTLAKIGIKAVPRVISMLKKKKQ 26 "Ponericin-W3 (ants, insects, animals)" P82425 Not found Not found Pachycondyla goeldii (Ponerine ant) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal" Protein level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." "[Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 10mm), B. megaterium ATCC 9885b(Inhibition zone = 13.5mm), B. stearothermophilus CIP 675(Inhibition zone = 17mm), B. subtilis ATCC 6623(Inhibition zone = 13mm), Enterococcus faecalis CIP 636(Inhibition zone = 8mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 17.5mm), Streptococcus pyogenes CIP 561(Inhibition zone = 11.5mm), S. sanguinis CIP 55128(Inhibition zone = 10mm), Listeria ivanovii LMA 94d(Inhibition zone = 14mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 11mm), Micrococcus luteus CIP 5345(Inhibition zone = 11mm), Staphylococcus aureus CIP 677(Inhibition zone = 13mm), Staphylococcus aureus LMA(Inhibition zone = 18mm), S. epidermidis CIP 53134(Inhibition zone = 15mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 10mm), Enterobacter cloacae CIP 6085(Inhibition zone = 4mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 7.5mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(Inhibition zone = 4mm), Serratia marcescens LMA TP(Inhibition zone = 11mm), Flavobacterium meningosepticum CIP 6057(no detected), Pseudomonas aeruginosa CIP A22(Inhibition zone = 18.5mm)." [Ref.11279030]1mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 ¦Ìl of the peptide solution and placed overnight at 4¡æ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. "Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J." "Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii." DRAMP02765 GIWGTALKWGVKLLPKLVGMAQTKKQ 26 "Ponericin-W4 (ants, insects, animals)" P82426 Not found Not found Pachycondyla goeldii (Ponerine ant) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal" Protein level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." "[Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 8.5mm), B. megaterium ATCC 9885b(Inhibition zone = 13.5mm), B. stearothermophilus CIP 675(Inhibition zone = 18mm), B. subtilis ATCC 6623(Inhibition zone = 13mm), Enterococcus faecalis CIP 636(Inhibition zone = 3mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 14mm), Streptococcus pyogenes CIP 561(Inhibition zone = 8mm), S. sanguinis CIP 55128(Inhibition zone = 7mm), Listeria ivanovii LMA 94d(Inhibition zone = 10mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 10mm), Micrococcus luteus CIP 5345(Inhibition zone = 12.5mm), Staphylococcus aureus CIP 677(Inhibition zone = 11.5mm), Staphylococcus aureus LMA(Inhibition zone = 13.5mm), S. epidermidis CIP 53134(Inhibition zone = 11.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 8.5mm), Enterobacter cloacae CIP 6085(Inhibition zone = 16.5mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 9mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(no detected), Serratia marcescens LMA TP(Inhibition zone = 13mm), Flavobacterium meningosepticum CIP 6057(no detected), Pseudomonas aeruginosa CIP A22(Inhibition zone = 17mm)." [Ref.11279030]2mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 ¦Ìl of the peptide solution and placed overnight at 4¡æ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. "Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J." "Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii." DRAMP02766 FWGALIKGAAKLIPSVVGLFKKKQ 24 "Ponericin-W5 (ants, insects, animals)" P82427 Belongs to the ponericin-W family Not found Pachycondyla goeldii (Ponerine ant) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal, Antifungal" Protein level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. Tissue specificity: Expressed by the venom gland." "[Ref.11279030]Gram-positive bacteria: Bacillus cereus CIP 6624a(Inhibition zone = 7mm), B. megaterium ATCC 9885b(Inhibition zone = 12mm), B. stearothermophilus CIP 675(Inhibition zone = 17mm), B. subtilis ATCC 6623(Inhibition zone = 13mm), Enterococcus faecalis CIP 636(Inhibition zone = 3mm), Lactococcus lactis ssp. cremoris I116(Inhibition zone = 11mm), Streptococcus pyogenes CIP 561(Inhibition zone = 6.5mm), S. sanguinis CIP 55128(Inhibition zone = 4.5mm), Listeria ivanovii LMA 94d(Inhibition zone = 8mm), Listeria monocytogenes ATCC 15313(Inhibition zone = 6.5mm), Micrococcus luteus CIP 5345(Inhibition zone = 11mm), Staphylococcus aureus CIP 677(Inhibition zone = 7.5mm), Staphylococcus aureus LMA(Inhibition zone = 9mm), S. epidermidis CIP 53134(Inhibition zone = 7.5mm);##Gram-negative bacteria: Escherichia coli(Inhibition zone = 3mm), Enterobacter cloacae CIP 6085(Inhibition zone = 11mm), Klebsiella pneumoniae CIP 8291(Inhibition zone = 6.5mm), Proteus mirabilis LMA TP(no detected), Salmonella enterica CIP 813(no detected), Serratia marcescens LMA TP(Inhibition zone = 11mm), Flavobacterium meningosepticum CIP 6057(Inhibition zone = 5mm), Pseudomonas aeruginosa CIP A22(Inhibition zone = 14mm)." [Ref.11279030]4mm in test condition against horse erythrocytes (A 12-ml sample of blood agar medium was supplemented with 1 ml of sheep or horse erythrocytes. Wells 5 mm in diameter were filled with 20 ¦Ìl of the peptide solution and placed overnight at 4¡æ to allow the diffusion of the hemolytic agent) Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11279030 J. Biol. Chem. 2001; 276: 17823-17829. "Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J." "Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii." DRAMP03163 ATCDLFSFRSKWVTPNHAACAAHCLLRGNRGGRCKGTICHCRK 43 "R. prolixus defensin A (RprDefA; insect defensin; Insects, animals)" No entry found Not found Not found Rhodnius prolixus "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Not found Combine helix and strand structure Not found None Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. "Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C." "Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease." DRAMP03164 ATCDLLSFRSKWVTPNHAGCAAHCLLRGNRGGHCKGTICHCRK 43 "R. prolixus defensin B (RprDefB; insect defensin; Insects, animals)" No entry found Not found Not found Rhodnius prolixus "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Not found Combine helix and strand structure Not found None Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. "Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C." "Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease." DRAMP03165 ATCDLFSFRSKWVTPNHAGCAAHCIFLGNRGGRCVGTVCHCRK 43 "R. prolixus defensin C (RprDefC; insect defensin; Insects, animals)" No entry found Not found Not found Rhodnius prolixus "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Not found Combine helix and strand structure Not found None Comment: No comments found on DRAMP database Gram-negative bacterium: Escherichia coli;##Gram-positive bacterium: Micrococcus luteus. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12650692 Insect Biochem Mol Biol. 2003 Apr;33(4):439-447. "Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C." "Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease." DRAMP03218 GKFSVFGKILRSIAKVFKGVGKVRKQFKTASDLDKNQ 37 "M-oxotoxin-Ot2a (Oxyopinin-2a, Oxki2a; spiders, Arthropods, animals)" P83248 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) "Antimicrobial, Antibacterial, Insecticidal" Protein level Alpha helix Not found None "Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides." No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 ?M against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. "Corzo G, Villegas E, G¨®mez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. " "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins." DRAMP03219 GKFSGFAKILKSIAKFFKGVGKVRKQFKEASDLDKNQ 37 "M-oxotoxin-OtIIb (Oxyopinin-IIb, OxkiIIb; spiders, Arthropods, animals)" P83249 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) "Antimicrobial, Antibacterial, Insecticidal" Protein level Not found Not found None "Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides." No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 ?M against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. "Corzo G, Villegas E, G¨®mez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. " "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins." DRAMP03220 GKLSGISKVLRAIAKFFKGVGKARKQFKEASDLDKNQ 37 "M-oxotoxin-Ot2c (Oxyopinin-2c, Oxki2c; spiders, Arthropods, animals)" P83250 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) "Antimicrobial, Antibacterial, Insecticidal" Protein level Alpha helix Not found None "Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides." No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 ?M against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Cell membrane 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. "Corzo G, Villegas E, G¨®mez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. " "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins." DRAMP03221 GKFSVFSKILRSIAKVFKGVGKVRKQFKTASDLDKNQ 37 "M-oxotoxin-Ot2d (Oxyopinin-2d, Oxki2d; spiders, Arthropods, animals)" P83251 Belongs to the oxyopinin-2 family Not found Oxyopes takobius (Lynx spider) "Antimicrobial, Antibacterial, Insecticidal" Protein level Not found Not found None "Function: Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides." No MICs found in DRAMP database [Ref.11976325]10% hemolytic activity at 50 ?M against sheep red blood cells Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11976325 J Biol Chem. 2002 Jun 28;277(26):23627-23637. "Corzo G, Villegas E, G¨®mez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. " "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins." DRAMP03223 GFGSLFKFLAKKVAKTVAKQAAKQGAKYIANKQME 35 "M-ctenitoxin-Cs1b (M-CNTX-Cs1b; Cupiennin-1b; spiders, Arthropods, animals)" P83620 Belongs to the cupiennin family Not found Cupiennius salei (Wandering spider) "Antimicrobial, Antibacterial, Insecticidal" Protein level Not found Not found None "Function: Has antimicrobial activity. Has insecticidal activity. Probably acts by disturbing membrane Function: with its amphipathic structure. Synergistically increases the insecticidal activity of CSTX-1, CSTX-9, and CSTX-13 by up to 65%. Also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. LD50 is 5.9 pmol/mg on Drosophila. " No MICs found in DRAMP database [Ref.11792701]Not determined Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11792701 J Biol Chem. 2002 Mar 29;277(13):11208-11216. "Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W." "Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae)." DRAMP03238 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKYYGKKALQKASEKL 69 "M-zodatoxin-Lt8c (M-ZDTX-Lt8c; Cytoinsectotoxin-1c, CIT-1c; spiders, Arthropods, animals)" "P85255, B3W6I1" Belongs to the cytoinsectotoxin family cit 1-3 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal" Protein level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis(By similarity). Tissue specificity: Expressed by the venom gland." "Gram-positive bacteria: Micrococcus luteus VKM Ac-2230, Staphylococcus aureus 209P, Arthrobacter globiformis VKM Ac-1112, Bacillus subtilis VKM B-501;##Gram-negative bacteria: Escherichia coli C600, E. coli DH5?¡À, E. coli MH1, Pseudomonas aeruginosa PAO1, Pseudomonas fluorescens VKM B-894, Serratia marcescens VKM B-1248." No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03239 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGITKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 "M-zodatoxin-Lt8d (M-ZDTX-Lt8d; Cytoinsectotoxin-1d, CIT-1d; spiders, Arthropods, animals)" "P85256, B3W6I2" Belongs to the cytoinsectotoxin family cit 1-4 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Protein level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03240 GFFGNTWKKIKGKSDKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 "M-zodatoxin-Lt8e (M-ZDTX-Lt8e; Cytoinsectotoxin-1e, CIT-1e; spiders, Arthropods, animals)" "P85256, B3W6I3" Belongs to the cytoinsectotoxin family cit 1-5 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Protein level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03241 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKALQKASEKL 69 "M-zodatoxin-Lt8f (M-ZDTX-Lt8f; Cytoinsectotoxin-1f, CIT-1f; spiders, Arthropods, animals)" "P85258, B3W6I4" Belongs to the cytoinsectotoxin family cit 1-7 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Anti-Gram-, Insecticidal" Protein level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S. carnaria. Has antibacterial activity against the Gram-negative bacteria E.coli. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03242 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKALQKASEKL 69 "M-zodatoxin-Lt8g (M-ZDTX-Lt8g; Cytoinsectotoxin-1g, CIT-1g; spiders, Arthropods, animals)" "P85259, B3W6I5" Belongs to the cytoinsectotoxin family cit 1-8 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Anti-Gram-, Insecticidal" Protein level Not found Not found None "Function: Has insecticidal activity against the flesh fly S. carnaria. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03243 GFFGNAWKKIKGKAEKFFRKKAAKIIAKKEGITKEEAEAKVDTMSKKQIKVYLLKHYGKKALQKASEKL 69 "M-zodatoxin-Lt8h (M-ZDTX-Lt8h; Cytoinsectotoxin-1h, CIT-1h; spiders, Arthropods, animals)" "P85247, B3W6I6" Belongs to the cytoinsectotoxin family cit 1-11 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Anti-Gram-, Insecticidal" Protein level Not found Not found None "Function: Has insecticidal activity against the flesh fly S. carnaria. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." Gram-negative bacterium: Escherichia coli. No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03244 GFFGNTWKKIKGKTDKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKALQKASEKL 69 "M-zodatoxin-Lt8j (M-ZDTX-Lt8j; Cytoinsectotoxin 1-9; spiders, Arthropods, animals)" P0CAZ3 Belongs to the cytoinsectotoxin family cit 1-9 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis " No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski AA, Kozlov SA, Samsonova OV, Egorova NS, Karpunin DV, Pluzhnikov KA, Feofanov AV, Grishin EV." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03245 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKALQKVSEKL 69 "M-zodatoxin-Lt8k (M-ZDTX-Lt8k; Cytoinsectotoxin 1-10; spiders, Arthropods, animals)" P0CAZ4 Belongs to the cytoinsectotoxin family cit 1-10 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03246 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGIFKEEAQAKVDAMSKKQIRLYLLKYYGKKALQKASEKL 69 "M-zodatoxin-Lt8i (M-ZDTX-Lt8i; Cytoinsectotoxin 1-6; spiders, Arthropods, animals)" P0CAZ2 Belongs to the cytoinsectotoxin family cit 1-6 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski AA, Kozlov SA, Samsonova OV, Egorova NS, Karpunin DV, Pluzhnikov KA, Feofanov AV, Grishin EV." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03247 GFFGNAWKKIKGKAEKFFRKKAAKIIAKKEGITKEEAEAKVDPMSKKQIKVYLLKHYGKKALQKASEKL 69 "M-zodatoxin-Lt8l (M-ZDTX-Lt8l; Cytoinsectotoxin 1-12; spiders, Arthropods, animals)" P0CAZ5 Belongs to the cytoinsectotoxin family cit 1-12 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03248 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKLFKKRPKNCDQ 71 "M-zodatoxin-Lt8m (M-ZDTX-Lt8m; Cytoinsectotoxin 1-13; spiders, Arthropods, animals)" P0CAZ6 Belongs to the cytoinsectotoxin family cit 1-13 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03249 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKLFKKRPKNCDQ 71 "M-zodatoxin-Lt8o (M-ZDTX-Lt8o; Cytoinsectotoxin 1-14; spiders, Arthropods, animals)" P0CAZ7 Belongs to the cytoinsectotoxin family cit 1-14 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03250 GFFGNTWKKIKGKADKIMLKKAVKLMVKKEGISKEEAQAKVDAMSKKQIRLYLLKYYGKKSSSKSVRKIVISKSF 75 "M-zodatoxin-Lt8p (M-ZDTX-Lt8p; Cytoinsectotoxin 1-15; spiders, Arthropods, animals)" P0CAZ8 Belongs to the cytoinsectotoxin family cit 1-15 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03251 GFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKSSSKSFRKIVISKSF 75 "M-zodatoxin-Lt8q (M-ZDTX-Lt8q; Cytoinsectotoxin 1-16; spiders, Arthropods, animals)" P0CAZ9 Belongs to the cytoinsectotoxin family cit 1-16 Lachesana tarabaevi (Spider) "Antimicrobial, Antibacterial, Insecticidal" Transcript level Not found Not found None "Function: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. Tissue specificity: Expressed by the venom gland." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 18215128 Biochem J. 2008 May 1;411(3):687-696. "Vassilevski A.A, Kozlov S.A, Samsonova O.V, Egorova N.S, Karpunin D.V, Pluzhnikov K.A, Feofanov A.V, Grishin E.V." "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides from spider venom." DRAMP03259 RTCMIKKEGWGKCLIDTTCAHSCKNRGYIGGDCKGMTRTCYCLVNC 46 VrCRP (Cyst-rich; Plant defensin) No entry found Not found Not found V. radiata (a bruchid-resistant mungbean) Insecticidal Not found Not found Not found None Function: VrCRP exhibits insecticidal activity in vitro against C. chinensis. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 12452641 J Agric Food Chem. 2002 Dec 4;50(25):7258-7263. "Chen KC, Lin CY, Kuan CC, Sung HY, Chen CS." A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid. DRAMP03741 IFGSLFSLGSKLLPSVFKLFSRKKQ 25 "Ponericin-W-like 32.1 (Arthropods, animals)" P0CI91 Belongs to the ponericin-W family Not found Lychas mucronatus (Chinese swimming scorpion) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Insecticidal" Transcript level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities (By similarity). Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P0CI91]Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae [Swiss_Prot Entry P0CI91]has hemolytic activities Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20663230 BMC Genomics. 2010 Jul 28;11:452. "Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L." Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP03742 IFGSLFSLGSKLLPTVFKLFSRKKQ 25 "Ponericin-W-like 32.2 (Arthropods, animals)" P0CI92 Belongs to the ponericin-W family Not found Lychas mucronatus (Chinese swimming scorpion) "Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Insecticidal" Transcript level Not found Not found None "Function: Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities (By similarity). Tissue specificity: Expressed by the venom gland." [Swiss_Prot Entry P0CI92]Broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae [Swiss_Prot Entry P0CI92]has hemolytic activities Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 20663230 BMC Genomics. 2010 Jul 28;11:452. "Ruiming Z, Yibao M, Yawen H, Zhiyong D, Yingliang W, Zhijian C, Wenxin L." Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. DRAMP04526 SCVFIPCITSLAGCSCKNKVCYYDGGSVPCGE 32 Parigidin-br1 (Cyclotides; Plants) No entry found Not found Not found Palicourea rigida (Rubiaceae) Insecticidal Not found Not found Not found None "Function: Parigidin-br1 showes potent insecticidal activity against neonate larvae of Lepidoptera (Diatraea saccharalis), causing 60% mortality at a concentration of 1 ?m but had no detectable antibacterial effects." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 22074926 J Biol Chem. 2012 Jan 2;287(1):134-147. "Pinto MF, Fensterseifer IC, Migliolo L, Sousa DA, de Capdville G, Arboleda-Valencia JW, Colgrave ML, Craik DJ, Magalh?es BS, Dias SC, Franco OL." Identification and structural characterization of novel cyclotide with activity against an insect pest of sugar cane. DRAMP18097 MPFHYFPKLNPITWIPGWIPGLGKDRCLLPKVTGPCKASLTRYYYDKDTKACVEFIYGGCRGNRNNFKRKDECEKACTDH 80 Kunitz-type serine protease inhibitor U1-aranetoxin-Av1a (U1-AATX-Av1a; Toxin 1; AvTox-1) Q8T3S7 Belongs to the venom Kunitz-type family Not found Araneus ventricosus (Orbweaver spider) (Epeira ventricosa) Insecticidal Transcript level Not found Not found None "Function: Putative insecticidal toxin that may inhibit trypsin.##Miscellaneous: Since this peptide has no sequence signal, its secretion is unsure." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Ind. Entomol. 4:43-49 (2002) "Jung E.H., Lee K.S. , Han J.H., Je Y.H., Chang J.H., Roh J.Y., Sohn H.D., Jin B.R." "Molecular cloning of two cDNAs encoding an insecticidal toxin fromthe spider, Araneus ventricosus, and construction of a recombinantbaculovirus expressing a spider toxin." DRAMP18098 MALALLGLTIKPEHVPEGTGKAVADVEALACDPAQCMRSCPFNPFLNQYGGICKNGQCVCVKPS 64 U2-aranetoxin-Av1a (U2-AATX-Av1a; Toxin 2; AvTox-2) Q8T3S6 Not found Not found Araneus ventricosus (Orbweaver spider) (Epeira ventricosa) Insecticidal Transcript level Not found Not found None "Function: Putative insecticidal toxin.##Miscellaneous: Since this peptide has no sequence signal, its secretion is unsure." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Int. J. Ind. Entomol. 4:43-49 (2002). "Jung E.H., Lee K.S. , Han J.H., Je Y.H., Chang J.H., Roh J.Y., Sohn H.D., Jin B.R." "Molecular cloning of two cDNAs encoding an insecticidal toxin fromthe spider, Araneus ventricosus, and construction of a recombinantbaculovirus expressing a spider toxin." DRAMP18099 ECAAKNKRCADWAGPWCCEGLYCSCRSYPGCMCRPNS 37 Beta/delta-agatoxin-7 (Mu-2Aga_01; U3-agatoxin-Ao1a; U3-AGTX-Ao1a) Q5Y4V8 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18100 GCVGENQQCADWAGPHCCSGYYCTCRYFPKCICRKDS 37 Beta/delta-agatoxin-3 (Mu-2Aga_04; U3-agatoxin-Ao1c; U3-AGTX-Ao1c) Q5Y4V6 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18101 GDCVGESQQCADWSGPYCCKGYYCTCRYFPKCICVNDN 38 Beta/delta-agatoxin-1 (Mu-2Aga_07; U3-agatoxin-Ao1f; U3-AGTX-Ao1f) Q5Y4V3 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." Fly larvae (LD50=7 ??g/g). No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18102 GGCVGESQQCADWSGPYCCKGYYCTCRYFPKCICVNDN 38 Beta/delta-agatoxin-2 (Mu-2Aga_08; U3-agatoxin-Ao1g; U3-AGTX-Ao1g) Q5Y4V2 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18103 GCVGENQQCADWAGLHCCSGYYCTCRYFPKCICRKDS 37 Beta/delta-agatoxin-4 (Mu-2Aaga_12; U3-agatoxin-Ao1k; U3-AGTX-Ao1k) Q5Y4U8 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18104 DCVGENGRCRDWYNDCCDGFYCSCRQPPYCICRNNN 36 Beta/delta-agatoxin-5 (Mu-2Aaga_13; U3-agatoxin-Ao1l; U3-AGTX-Ao1l) Q5Y4U7 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18105 ECVGENGHCRSWYNDCCDGYYCSCMQPPNCICRNNN 36 Beta/delta-agatoxin-6 (Mu-2Aaga_14; U3-agatoxin-Ao1m; U3-AGTX-Ao1m) Q5Y4U6 Belongs to the beta/delta-agatoxin family Not found Agelena orientalis (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that modulates the insect Nav channel (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation and inactivation processes being affected. The voltage dependence of activation is shifted toward more hyperpolarized potentials (analogous to site 4 toxins) and a non- inactivating persistent sodium current is induced (site 3-like action). Interestingly, both effects take place in a voltage- dependent manner, producing a bell-shaped curve between -80 and 0 mV. Compared to beta/delta-agatoxin-1 to -3, this toxin appears to affect the insect sodium channel only weakly.##Miscellaneous: Does not affect mammalian sodium channels (Nav) (By similarity)." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15688451##20385552 Proteins 59:131-140 (2005).##J. Biol. CheM. 285:18545-18554 (2010). "Kozlov S. A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R., Grishin E.V.##Billen B., Vassilevski A., Nikolsky A., Debaveye S. , Tytgat J., Grishin E." A novel strategy for the identification of toxinlike structures inspider venoM. ##Unique bell-shaped voltage-dependent modulation of Na+ channel gatingby novel insect-selective toxins from the spider Agelena orientaliS. DRAMP18106 IFECVFSCDIKKEGKPCKPKGEKKCTGGWRCKIKLCLKI 39 U1-theraphotoxin-Ba1b (U1-TRTX-Ba1b; Venom peptide 2) P85504 Belongs to the huwentoxin-2 family Not found Brachypelma ruhnaui (Mexican golden redrump tarantula) (Brachypelmaalbiceps) Insecticidal Protein level Beta sheet (3 strands; 10 residues) "The three-dimensional conformation (Fig. 3B) of Ba2 consists in a three-stranded (residues 15?€¡°17, 29?€¡°32 and 35?€¡°38) anti-parallel beta-sheet. The first strand is connected with the second one by a large loop made of residues 19?€¡°28, whereas the second and third strands are connected by a ??-turn." 2KGH resolved by NMR Function: Has insecticidal activity. Insect LD50=9.2 ?¡À 0.9 ??g/g No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 19374957 BiochiM. BiophyS. Acta 1794:1190-1196 (2009). "Corzo G., Bernard C. , Clement H., Villegas E., Bosmans F., Tytgat J., Possani L.D., Darbon H., Alagon A." Insecticidal peptides from the theraposid spider Brachypelmaalbiceps: an NMR-based model of Ba2. DRAMP18107 ILECVFSCDIKKEGKPCKPKGEKKCTGGWRCKIKLCLKI 39 U1-theraphotoxin-Ba1a (U1-TRTX-Ba1a; Venom peptide 1) P85497 Belongs to the huwentoxin-2 family Not found Brachypelma ruhnaui (Mexican golden redrump tarantula) (Brachypelmaalbiceps) Insecticidal Protein level Not found Not found None Function: Has insecticidal activity. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found PubMed ID is not available Submitted (FEB-2008) to UniProtK "Corzo G., Clement H., Alagon A." Primary structure of two insecticidal peptides from the theraposid Brachypelma ruhnaui. DRAMP18109 SDCTLRNHDCTDDRHSCCRSKMFKDVCTCFYPSQAKKELCTCQQPKHLKYIEKGLQKAKDYAT 63 U2-ctenitoxin-Cs1a (U1-CNTX-Cs2a; Neurotoxic enhancer CSTX-13; U1-ctenitoxin-Cs2a; Fragments) "P83919, P83920" Belongs to the spider toxin CSTX superfamily Not found Cupiennius salei (Wandering spider) Insecticidal Protein level Not found Not found None "Function: This toxin alone has very weak insecticidal activity, with an unknown molecular target. Acts as a neurotoxic enhancer, synergistically enhancing the neurotoxic action of omega-CNTX-Cs1a (CSTX-1) (AC P81694)." Fly (LD50=16.3 pmol/mg) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 15272079##15914655 ProC. Natl. Acad. Sci. U.S. A. 101:11251-11256 (2004).##J. Exp. Biol. 208:2115-2121 (2005). "Wullschleger B., Kuhn-Nentwig L., Tromp J., Kaempfer U., Schaller J., Schuerch S. , Nentwig W.##Wullschleger B., Nentwig W., Kuhn-Nentwig L." "CSTX-13, a highly synergistically acting two-chain neurotoxicenhancer in the venom of the spider Cupiennius salei (Ctenidae).##Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei." DRAMP18110 SSVCIPSGQPCPYNEHCCSGSCTYKENENGNTVQRCD 37 Omega-hexatoxin-Ar1a (Omega-HXTX-Ar1a; Omega-atracotoxin-Ar1a; Omega-AcTx-Ar1a) "P83580, A5A3H0" Belongs to the omega-atracotoxin type 1 family Not found Atrax robustus (Sydney funnel-web spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal toxin that reversibly and voltage- independently blocks both mid-low- (M-LVA) and high-voltage- activated (HVA) calcium channels (Cav) in cockroach DUM neuronS. Also causes a modest block of insect sodium channel currents (Nav). Induces potent excitatory symptoms, followed by flaccid paralysis leading to death in house cricketS. Miscellaneous: This toxin comes from a female specimen. It is observed that propeptide sequences coming from female specimen have only limited homology with the male paralogs, but the reason is unknown.Does not inhibit potassium channel currentS. Has no activity in vertebrate smooth and skeletal nerve-muscle preparations (PubMed: 17610847)." House crickets (LD50=236?¡À28 pmol/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 17610847 BiocheM. Pharmacol. 74:623-638 (2007). "Chong Y., Hayes J.L., Sollod B., Wen S. , Wilson D.T., Hains P.G., Hodgson W.C. , Broady K.W., King G.F., Nicholson G.M. " The omega-atracotoxins: selective blockers of insect M-LVA and HVAcalcium channelS. DRAMP18111 GGCIKWNHSCQTTTLKCCGKCVVCYCHTPWGTNCRCDRTRLFCTED 46 Mu-hexatoxin-Mg2a (Mu-HXTX-Mg2a; Neurotoxin magi-3) P83559 Not found Not found Macrothele gigas (Spider) Insecticidal Protein level Not found Not found None Function: Competes for binding at site 3 of the insect voltage- gated sodium channel (Nav). Insecticidal neurotoxin. Causes temporary paralysis to lepidopteran larvae when injected at 10.3 nmol/g. Is not toxic to mice when injected intracranially at 20 pmol/g.##PTM: Contains 5 disulfide bondS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet site 3 of the insect voltage- gated sodium channel (Nav) 12860384 FEBS Lett. 547:43-50 (2003). "Corzo G., Gilles N., Satake H., Villegas E., Dai L., Nakajima T., Haupt J." Distinct primary structures of the major peptide toxins from thevenom of the spider Macrothele gigas that bind to sites 3 and 4 in thesodium channel. DRAMP18112 CMGYDIHCTDRLPCCFGLECVKTSGYWWYKKTYCRRKS 38 Mu-hexatoxin-Mg1b (Mu-HXTX-Mg1b; Neurotoxin magi-1) P83557 Belongs to the magi-1 family Not found Macrothele gigas (Spider) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin. Shows competition for site 3 of insect voltage-gated sodium channels (Nav). Has no effect on lepidopteran larvae when injected at 20 pmol/g, or on mice when injected intracranially at 32.8 nmol/g." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet site 4 of the insect voltage- gated sodium channel (Nav) 12860384 FEBS Lett. 547:43-50 (2003). "Corzo G., Gilles N., Satake H., Villegas E., Dai L., Nakajima T., Haupt J." Distinct primary structures of the major peptide toxins from thevenom of the spider Macrothele gigas that bind to sites 3 and 4 in thesodium channel. DRAMP18113 ACVGDGQRCASWSGPYCCDGYYCSCRSMPYCRCRNNS 37 Delta-amaurobitoxin-Pl1b (Delta-AMATX-Pl1b; Delta-palutoxin IT2; Delta-paluIT2) P83257 Belongs to the beta/delta-agatoxin family Not found Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus) Insecticidal Protein level beta sheet (5 strands; 10 residues) "The three-dimensional structure of ??-paluIT2 consists of a compact disulfide-bonded core, from which four loops emerge.In ??-paluIT2, the corresponding loops encompass residues 3?€¡°6 (loop I), 10?€¡°15 (loop II), 18?€¡°20 (loop III), and 25?€¡°31 (loop IV), and residues 7?€¡°9 are involved in an extended structure. The ??-sheet structure is therefore made of three anti-parallel ??-strands (Q7?€¡°R8, Y21?€¡°S24, and R32?€¡°N35 )." 1V91 resolved by NMR Function: Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation. Insect LD50=24.7 ?¡À 11.8 mg/g No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 10971590##15683238##15726637 Eur. J. BiocheM. 267:5783-5795 (2000).##Biochemistry 44:1542-1549 (2005).##Proteins 59:368-379 (2005). "Corzo G., Escoubas P., Stankiewicz M. , Pelhate M. , Kristensen C. P., Nakajima T.##Corzo G., Escoubas P., Villegas E., Karbat I., Gordon D., Gurevitz M. , Nakajima T., Gilles N.##Ferrat G., Bosmans F., Tytgat J., Pimentel C. , Chagot B., Gilles N., Nakajima T., Darbon H., Corzo G." "Isolation, synthesis and pharmacological characterization of delta-palutoxins IT, novel insecticidal toxins from the spider Paracoelotesluctuosus (Amaurobiidae).##A spider toxin that induces a typical effect of scorpion alpha-toxinsbut competes with beta-toxins on binding to insect sodium channelS. ##Solution structure of two insect-specific spider toxins and their pharmacological interaction with the insect voltage-gated Na+channel." DRAMP18116 QDFMKHLDKKTQTPKL 16 U2-segestritoxin-Sf1b (U2-SGTX-Sf1b; F5.7; Toxin SFI 2) P61096 Belongs to the spider toxin SFI family Not found Segestria florentina (Tube-web spider) (Segestria gracilis) Insecticidal Protein level Not found Not found None Function: Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.25 mg/kg body weight. Heliothis virescens (LD50=7 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689233 Toxicon 40:125-130 (2002). "Lipkin A., Kozlov S. , Nosyreva E., Blake A., Windass J.D., Grishin E." Novel insecticidal toxins from the venom of the spider Segestriaflorentina. DRAMP18117 KECMTDGTVCYIHNHNDCCGSCLCSNGPIARPWEMMVGNCMCGPKA 46 U2-segestritoxin-Sf1a (U2-SGTX-Sf1a; F5.6; Toxin SFI 1) P61095 Belongs to the spider toxin SFI family Not found Segestria florentina (Tube-web spider) (Segestria gracilis) Insecticidal Protein level Not found Not found None "Function: Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.5 mg/kg body weight. Orally active against larvae of the tomato moth (Laconobia oleracea), the rice brown planthopper (Nilaparvata lugens), and the peach-potato aphid (Myzus persicae) when fused to snowdrop lectin." Heliothis virescens (LD50=10 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689233##15037094 Toxicon 40:125-130 (2002).##J. Insect Physiol. 50:61-71 (2004). "Lipkin A., Kozlov S. , Nosyreva E., Blake A., Windass J.D., Grishin E.##Fitches E., Edwards M. G., Mee C. , Grishin E., Gatehouse A.M. , Edwards J.P., Gatehouse J.A." Novel insecticidal toxins from the venom of the spider Segestriaflorentina.##Fusion proteins containing insect-specific toxins as pest controlagents: snowdrop lectin delivers fused insecticidal spider venom toxinto insect haemolymph following oral ingestion. DRAMP18118 AECMVDETVCYIHNHNNC 18 U2-segestritoxin-Sf1i (U2-SGTX-Sf1i; Toxin F5.5; Fragment) P61094 Belongs to the spider toxin SFI family Not found Segestria florentina (Tube-web spider) (Segestria gracilis) Insecticidal Protein level Not found Not found None Function: Insecticidal toxin. Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.1 mg/kg body weight. Heliothis virescens (LD50=4 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 11689233 Toxicon 40:125-130 (2002). "Lipkin A., Kozlov S. , Nosyreva E., Blake A., Windass J.D., Grishin E." Novel insecticidal toxins from the venom of the spider Segestriaflorentina. DRAMP18119 ADCVGDGQRCADWAGPYCCSGYYCSCRSMPYCRCRSDS 38 Mu-agatoxin-Aa1c (Mu-AGTX-Aa1c; Mu-agatoxin III; Mu-agatoxin-3) "P60178, P11059" Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." M. sexta (LD50=28?¡À12 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). "Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E." "Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta." DRAMP18121 ADCVGDGQKCADWFGPYCCSGYYCSCRSMPYCRCRSDS 38 Mu-agatoxin-Hc1c (Mu-AGTX-Hc1c; CT-III; Curtatoxin-3) P15968 Belongs to the beta/delta-agatoxin family Not found Hololena curta (Funnel-web spider) (Agelena curta) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces irreversible neuromuscular blockade in the cricket A.domestica. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." A.domestica (LD50=4 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2298738##15066410 J. Biol. CheM. 265:2054-2059 (1990).##Toxicon 43:509-525 (2004). "Stapleton A., Blankenship D.T., Ackermann D.L., Chen T.-M. , Gorder G.W., Manley G.D., Palfreyman M. G., Coutant J.E., Cardin A.D.##Adams M. E." "CurtatoxinS. Neurotoxic insecticidal polypeptides isolated from thefunnel-web spider Hololena curta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta." DRAMP18122 SCVGEYGRCRSAYEDCCDGYYCNCSQPPYCLCRNNN 36 Mu-agatoxin-Hc1a (Mu-AGTX-Hc1a; Curtatoxin-1; CT-I) P15967 Belongs to the beta/delta-agatoxin family Not found Hololena curta (Funnel-web spider) (Agelena curta) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces irreversible neuromuscular blockade in the cricket A.domestica. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." A.domestica (LD50=20 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2298738##15066410 J. Biol. CheM. 265:2054-2059 (1990).##Toxicon 43:509-525 (2004). "Stapleton A., Blankenship D.T., Ackermann D.L., Chen T.-M. , Gorder G.W., Manley G.D., Palfreyman M. G., Coutant J.E., Cardin A.D.##Adams M. E." "CurtatoxinS. Neurotoxic insecticidal polypeptides isolated from thefunnel-web spider Hololena curta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta." DRAMP18123 DCVGESQQCADWAGPHCCDGYYCTCRYFPKCICVNNN 37 Mu-agatoxin-Aa1f (Mu-AGTX-Aa1f; Mu-agatoxin VI; Mu-agatoxin-6) P11062 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." M. sexta (LD50=38?¡À12 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). "Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E." "Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta." DRAMP18124 ACVGENKQCADWAGPHCCDGYYCTCRYFPKCICRNNN 37 Mu-agatoxin-Aa1e (Mu-AGTX-Aa1e; Mu-agatoxin V; Mu-agatoxin-5) P11061 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." M. sexta (LD50=48?¡À11 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). "Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E." "Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta." DRAMP18125 ACVGENQQCADWAGPHCCDGYYCTCRYFPKCICRNNN 37 Mu-agatoxin-Aa1d (Mu-AGTX-Aa1d; Mu-agatoxin IV; Mu-agatoxin-4) P11060 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." M. sexta (LD50=40?¡À9 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410##8608119 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004).##Biochemistry 35:2836-2844 (1996). "Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E.##Omecinsky D.O., Holub K.E., Adams M. E., Reily M. D." "Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta.##Three-dimensional structure analysis of mu-agatoxins: furtherevidence for common motifs among neurotoxins with diverse ion channelspecificitieS. " DRAMP18126 ECATKNKRCADWAGPWCCDGLYCSCRSYPGCMCRPSS 37 Mu-agatoxin-Aa1b (Mu-AGTX-Aa1b; Mu-agatoxin II; Mu-agatoxin-2) P11058 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level Not found Not found None "Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." M. sexta (LD50=75?¡À27 ??g/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004). "Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E." "Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta." DRAMP18127 ECVPENGHCRDWYDECCEGFYCSCRQPPKCICRNNN 36 Mu-agatoxin-Aa1a (Mu-AGTX-Aa1a; Mu-agatoxin I; Mu-agatoxin-1) P11057 Belongs to the beta/delta-agatoxin family Not found Agelenopsis aperta (North American funnel-web spider) (Agelenopsisgertschi) Insecticidal Protein level beta sheet (4 strands; 15 residues) Not found 1EIT resolved by NMR "Function: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insectS. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neuronS." LD50 of 28?¡À7 ??g/g in M. sexta No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 2914898##15066410##8608119 J. Biol. CheM. 264:2150-2155 (1989).##Toxicon 43:509-525 (2004).##Biochemistry 35:2836-2844 (1996). "Skinner W.S. , Adams M. E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.##Adams M. E.##Omecinsky D.O., Holub K.E., Adams M. E., Reily M. D." "Purification and characterization of two classes of neurotoxins fromthe funnel web spider, Agelenopsis aperta.##Agatoxins: ion channel specific toxins from the American funnel webspider, Agelenopsis aperta.##Three-dimensional structure analysis of mu-agatoxins: furtherevidence for common motifs among neurotoxins with diverse ion channelspecificitieS. " DRAMP18141 PSPPGFSPFR 10 Nephilakinin-3 (Nephilakinin-III) P0DM74 Belongs to the bradykinin-related peptide family Not found Nephila clavipes (Golden silk orbweaver) Insecticidal Protein level Not found Not found None Function: Causes constriction on isolated rat ileum preparations and relaxation on rat duodenum muscle preparations at amounts higher than bradykinin. Is a partial agonist bradykinin receptor B2 (BDKRB2). Has insecticidal propertieS. May be related to the predation of insects by the spider webS. ##Miscellaneous: Has been extracted from the spider web (PubMed: 16202476). Does not target bradykinin receptor B1 (BDKRB1) (PubMed: 16202476). ED50=0.7??M;LD50=70?¡À17pmoles/mg honeybee No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16202476 Peptides 27:690-697 (2006). "Volsi E.C. , Mendes M. A., Marques M. R., dos Santos L.D., Santos K.S. , de Souza B.M. , Babieri E.F., Palma M. S. " "Multiple bradykinin-related peptides from the capture web of thespider Nephila clavipes (Araneae, Tetragnatidae)." DRAMP18142 EAPPGFSPFR 10 Nephilakinin-2 (Nephilakinin-II) P0DM73 Belongs to the bradykinin-related peptide family Not found Nephila clavipes (Golden silk orbweaver) Insecticidal Protein level Not found Not found None Function: Causes constriction on isolated rat ileum preparations and relaxation on rat duodenum muscle preparations at amounts higher than bradykinin. Is a partial agonist bradykinin receptor B2 (BDKRB3). Has insecticidal propertieS. ED50=1.0??M;LD50=72?¡À18pmoles/mg honeybee No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 16202476 Peptides 27:690-697 (2006). "Volsi E.C. , Mendes M. A., Marques M. R., dos Santos L.D., Santos K.S. , de Souza B.M. , Babieri E.F., Palma M. S. " "Multiple bradykinin-related peptides from the capture web of thespider Nephila clavipes (Araneae, Tetragnatidae)." DRAMP18143 EELEAKDVIESKALATLDEER 21 Toxin OAIP 5 P0DM69 Belongs to the huwentoxin-2 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found None Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) "Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F." SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18144 YCQKWMWTCDAERKCCEDMACELWCKKRL 29 Toxin OAIP 4 P0DM68 Belongs to the huwentoxin-1 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found None Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) "Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F." SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18145 ECGGLMTRCDGKTTFCCSGMNCSPTWKWCVYAP 33 Toxin OAIP 3 P0DM67 Belongs to the huwentoxin-1 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found None Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) "Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F." SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18146 DCLGQWASCEPKNSKCCPNYACTWKYPWCRYRA 33 Toxin OAIP 2 P0DM66 Belongs to the huwentoxin-1 family Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level Not found Not found None Function: Probable ion channel inhibitor. Shows insecticidal activity when injected into mealwormS. No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279 PLoS ONE 8:E66279-E66279 (2013) "Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F." SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula. DRAMP18148 ATCAGQDQTCKVTCDCCGERGECVCGGPCICRQGNFLIAWYKLASCKK 48 Delta-ctenitoxin-Pn2c (Delta-CNTX-Pn2c; Neurotoxin Pn2-5A; Neurotoxin Tx2-5; PNTx2-5) "O76199, P29424" Belongs to the spider toxin Tx2 family Not found Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer) Insecticidal Protein level Not found Not found None "Function: Reversible inhibitor of voltage-gated sodium channels (Nav). Delays the fast inactivation kinetics of neuronal-type sodium channelS. Causes scratching, lacrimation, hypersalivation, sweating and agitation followed by spastic paralysis of the anterior and posterior extremities and death at dose levels of 0.24 mg/mouse. Insecticidal to the larval and adult forms of the house fly." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 9839668##1397265##19231838##16278100##1801316 Toxicon 36:1843-1850 (1998).##FEBS Lett. 310:153-156 (1992).##Biochemistry 48:3078-3088 (2009).##Comp. BiocheM. Physiol. 142:173-187 (2006).##Toxicon 29:1225-1233 (1991). "Kalapothakis E., Penaforte C. L., Beirao P.S. L., Romano-Silva M. A., Cruz J.S. , Prado M. A.M. , Guimaraes P.E.M. , Gomez M. V., Prado V.F.##Cordeiro M. N., Diniz C. R., Valentim A.D.C. , von Eickstedt V.R.D., Gilroy J., Richardson M. ##Matavel A., Fleury C. , Oliveira L.C. , Molina F., de Lima M. E., Cruz J.S. , Cordeiro M. N., Richardson M. , Ramos C. H., Beirao P.S. ##Richardson M. , Pimenta A.M. , Bemquerer M. P., Santoro M. M. , Bei" Cloning of cDNAS encoding neurotoxic peptides from the spiderPhoneutria nigriventer.##The purification and amino acid sequences of four Tx2 neurotoxinsfrom the venom of the Brazilian 'armed' spider Phoneutria nigriventer (Keys).##Structure and activity analysis of two spider toxins that alter sodium channel inactivation kineticS. ##Comparison of the partial proteomes of the venoms of Brazilianspiders of the genus Phoneutria.##Isolation of neurotoxic peptides from the venom of the 'armed' spider DRAMP18149 DCGHLHDPCPNDRPGHRTCCIGLQCRYGKCLVRV 34 U1-TRTX-Sp1a (Orally active insecticidal peptide 1; OAIP-1) K7N5K9 Not found Not found Selenotypus plumipes (Australian featherleg tarantula) Insecticidal Protein level beta sheet (7 strands; 13 residues) Not found 2LL1 resolved by NMR Function: Probable ion channel inhibitor. Shows insecticidal activity. Acts synergistically with the neonicotinoid insecticide imidacloprid. Is neither a repellent that repels insects nor an attractant that is preferentially consumed by insectS. Is very stable. Helicoverpa armigera (LD50=104.2?¡À0.6 pmol/g) No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet Not found 23894279##24039872 PLoS ONE 8:E66279-E66279 (2013).##PLoS ONE 8:E73136-E73136 (2013). "Wong E.S. , Hardy M. C. , Wood D., Bailey T., King G.F.##Hardy M. C. , Daly N.L., Mobli M. , Morales R.A., King G.F." SVM-based prediction of propeptide cleavage sites in spider toxinsidentifies toxin innovation in an australian tarantula.##Isolation of an orally active insecticidal toxin from the venom of anAustralian tarantula. DRAMP01272 ATCAGQDQPCKETCDCCGERGECVCGGPCICRQGYFWIAWYKLANCKK 48 Delta-ctenitoxin-Pn2a (Delta-CNTX-Pn2a; Neurotoxin Tx2-6; PnTx2-6) "P29425, Q95UF2" Belongs to the spider toxin Tx2 family Not found Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer) Insecticidal Protein level Not found Not found None "Function: Irreversible inhibitor of voltage-gated sodium channels (Nav). Binds voltage-dependently to sodium channels and inhibits the inactivation of the activated channelS. Also shifts the voltage dependence of the sodium conductance to negative potentials and decrease the peak inward current. Causes scratching, lacrimation, hypersalivation, sweating and agitation followed by spastic paralysis of the anterior and posterior extremities and death at dose levels of 0.79 mg/mouse. Is insecticidal to the larval and adult forms of the house fly. Enhances rat erectile function by increasing NO release in the cavernosum tissue." No MICs found in DRAMP database No hemolysis information or data found in the reference(s) presented in this entry Not included yet Not included yet Not included yet Not included yet Not included yet Not included yet sodium channels 12123835##1397265##16278100##19231838##18397797 FEBS Lett. 523:219-223 (2002).##FEBS Lett. 310:153-156 (1992).##Comp. BiocheM. Physiol. 142:173-187 (2006).##Biochemistry 48:3078-3088 (2009).##Toxicon 51:1197-1206 (2008). "Matavel A., Cruz J.S. , Penaforte C. L., Araujo D.A.M. , Kalapothakis E., Prado V.F., Diniz C. R., Cordeiro M. N., Beirao P.S. L.##;Cordeiro M. N., Diniz C. R., Valentim A.D.C. , von Eickstedt V.R.D., Gilroy J., Richardson M. ##Richardson M. , Pimenta A.M. , Bemquerer M. P., Santoro M. M. , Beirao P.S. , Lima M. E., Figueiredo S. G., Bloch C. Jr., Vasconcelos E.A., Campos F.A., Gomes P.C. , Cordeiro M. N.##Matavel A., Fleury C. , Oliveira" Electrophysiological characterization and molecular identification ofthe Phoneutria nigriventer peptide toxin PnTx2-6.##The purification and amino acid sequences of four Tx2 neurotoxinsfrom the venom of the Brazilian ¡®armed' spider Phoneutria nigriventer (Keys).##Comparison of the partial proteomes of the venoms of Brazilianspiders of the genus Phoneutria.##Structure and activity analysis of two spider toxins that altersodium channel inactivation kineticS. ##Tx2-6 toxin of the Phoneutria nigrive DRAMP00828 GLPTCGETCFGGTCNTPGCTCDPWPVCTHN 30 Cycloviolacin-O24 (Plant defensin) P84637 Belongs to the cyclotide family. Bracelet subfamily. Not found Viola odorata (Sweet violet) "Antiviral,Insecticidal " Protein level Bridge Not found None "Function: Probably participates in a plant defense mechanism. Has hemolytic activity. PTM: This is a cyclic peptide which may contain three disulfide bonds 5-19; 9-21; 14-27." [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=308 nM). [Ref:16872274] It has 75% hemolytic activity at 25.0 ¦ÌM against human type A red blood cells. Cyclic Cyclization (N termini to C termini) Cyclization (N termini to C termini) Disulfide bonds between Cys5 and Cys19; Cys9 and Cys21; Cys14 and Cys27. L [Ref.18008336]CEM-SS cells:IC50=6170 nM. Not found 16872274##18008336 Biochem J. 2006 Nov 15;400(1):1-12.##Biopolymers. 2008;90(1):51-60. "Ireland DC, Colgrave ML, Craik DJ.##Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ. " "A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability.##Cyclotides as natural anti-HIV agents."