PROTO_AGEPP
ID PROTO_AGEPP Reviewed; 12 AA.
AC P69437;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 29-SEP-2021, entry version 31.
DE RecName: Full=Protonectin {ECO:0000303|PubMed:15225564, ECO:0000303|PubMed:23836163};
DE AltName: Full=Agelaia-chemotactic peptide {ECO:0000303|PubMed:15052574};
DE Short=Agelaia-CP {ECO:0000303|PubMed:15052574};
OS Agelaia pallipes pallipes (Neotropical social wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Epiponini; Agelaia.
OX NCBI_TaxID=313352;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT LEU-12, MASS SPECTROMETRY, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=15052574; DOI=10.1002/rcm.1382;
RA Mendes M.A., Monson de Souza B., Delazari dos Santos L., Palma M.S.;
RT "Structural characterization of novel chemotactic and mastoparan peptides
RT from the venom of the social wasp Agelaiapallipes pallipes by high-
RT performance liquid chromatography/electrospray ionization tandem mass
RT spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:636-642(2004).
RN [2]
RP PROTEIN SEQUENCE, AMIDATION AT LEU-12, SYNTHESIS, FUNCTION, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=15225564; DOI=10.1016/j.toxicon.2004.04.009;
RA Mendes M.A., de Souza B.M., Marques M.R., Palma M.S.;
RT "Structural and biological characterization of two novel peptides from the
RT venom of the neotropical social wasp Agelaia pallipes pallipes.";
RL Toxicon 44:67-74(2004).
RN [3]
RP FUNCTION, SYNTHESIS, AND MUTAGENESIS OF LEU-6; GLY-7 AND LEU-8.
RX PubMed=23836163; DOI=10.1128/aac.02311-12;
RA Wang K., Dang W., Yan J., Chen R., Liu X., Yan W., Zhang B., Xie J.,
RA Zhang J., Wang R.;
RT "Membrane perturbation action mode and structure-activity relationships of
RT Protonectin, a novel antimicrobial peptide from the venom of the
RT neotropical social wasp Agelaia pallipes pallipes.";
RL Antimicrob. Agents Chemother. 57:4632-4639(2013).
CC -!- FUNCTION: Shows potent antimicrobial action against both Gram-positive
CC and Gram-negative bacteria (MIC=25 ug/ml or 32-63 uM against E.coli,
CC MIC=1.7 ug/ml against P.aeruginosa, MIC=3.1 ug/ml or 4 uM against
CC B.subtilis, MIC=8 uM against S.epidermis, and MIC=12.5 ug/ml or 8 uM
CC against S.aureus) (PubMed:15225564, PubMed:23836163). Acts by
CC disrupting the integrity of the outer and inner bacterial membranes
CC (Probable). Adopts an amphipathic alpha helical conformation in
CC membrane that is essential for the membrane disrupting activity
CC (PubMed:23836163). Mast cell degranulator that induces a potent
CC chemotaxis in polymorphonucleated leukocyte (PMNL) cells
CC (PubMed:15052574, PubMed:15225564). Shows no or weak hemolytic activity
CC (PubMed:15052574, PubMed:15225564). {ECO:0000269|PubMed:15052574,
CC ECO:0000269|PubMed:15225564, ECO:0000269|PubMed:23836163,
CC ECO:0000305|PubMed:23836163}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15052574,
CC ECO:0000269|PubMed:15225564}. Target cell membrane
CC {ECO:0000269|PubMed:23836163}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15052574, ECO:0000305|PubMed:15225564}.
CC -!- MASS SPECTROMETRY: Mass=1207.8; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:15052574};
CC -!- MASS SPECTROMETRY: Mass=1208.64; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:15225564};
CC -!- SIMILARITY: Belongs to the MCD family. Protonectin subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00521";
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DR PDB; 6N68; NMR; -; A=1-12.
DR PDB; 7JGY; NMR; -; A=1-12.
DR PDBsum; 6N68; -.
DR PDBsum; 7JGY; -.
DR BMRB; P69437; -.
DR SMR; P69437; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial; Chemotaxis;
KW Direct protein sequencing; Membrane; Secreted; Target cell membrane;
KW Target membrane.
FT PEPTIDE 1..12
FT /note="Protonectin"
FT /evidence="ECO:0000269|PubMed:15052574,
FT ECO:0000269|PubMed:15225564"
FT /id="PRO_0000044212"
FT MOD_RES 12
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:15052574,
FT ECO:0000269|PubMed:15225564"
FT MUTAGEN 6
FT /note="L->P: Loss of antibacterial activity, and loss of
FT alpha-helix structure."
FT /evidence="ECO:0000269|PubMed:23836163"
FT MUTAGEN 7
FT /note="G->P: Loss of antibacterial activity, and loss of
FT alpha-helix structure."
FT /evidence="ECO:0000269|PubMed:23836163"
FT MUTAGEN 8
FT /note="L->P: Loss of antibacterial activity, and loss of
FT alpha-helix structure."
FT /evidence="ECO:0000269|PubMed:23836163"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:6N68"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:6N68"
SQ SEQUENCE 12 AA; 1211 MW; 0A7BB6110A287720 CRC64;
ILGTILGLLK GL
