THAN_PODMA
ID THAN_PODMA Reviewed; 21 AA.
AC P55788;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Thanatin;
OS Podisus maculiventris (Spined soldier bug) (Pentatoma maculiventris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Pentatomomorpha; Pentatomoidea; Pentatomidae; Asopinae; Podisus.
OX NCBI_TaxID=29025;
RN [1]
RP PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Hemolymph;
RX PubMed=8577744; DOI=10.1073/pnas.93.3.1221;
RA Fehlbaum P., Bulet P., Chernysh S., Briand J.-P., Roussel J.-P.,
RA Letellier L., Hetru C., Hoffmann J.A.;
RT "Structure-activity analysis of thanatin, a 21-residue inducible insect
RT defense peptide with sequence homology to frog skin antimicrobial
RT peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1221-1225(1996).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=9760181; DOI=10.1046/j.1432-1327.1998.2560404.x;
RA Mandard N., Sodano P., Labbe H., Bonmatin J.-M., Bulet P., Hetru C.,
RA Ptak M., Vovelle F.;
RT "Solution structure of thanatin, a potent bactericidal and fungicidal
RT insect peptide, determined from proton two-dimensional nuclear magnetic
RT resonance data.";
RL Eur. J. Biochem. 256:404-410(1998).
CC -!- FUNCTION: Insect defense peptide with a broad spectrum of activity
CC against Gram-positive and Gram-negative bacteria and fungi. No activity
CC against S.aureus. Stops respiration in bacteria but does not
CC permeabilize their inner membranes.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: Four regions are important for the activity: the C-terminal
CC loop, the last three C-terminal residues, the stretch of seven N-
CC terminal residues and residues 8-9 are necessary for the antifungal
CC activity and dispensable for antibacterial activity.
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DR PDB; 5XO3; NMR; -; A=1-20.
DR PDB; 5XO4; NMR; -; A=1-21.
DR PDB; 5XO5; NMR; -; A=1-21.
DR PDB; 5XO9; NMR; -; A/B=1-21.
DR PDB; 5XOA; NMR; -; A/B=1-21.
DR PDB; 5XOK; NMR; -; A/B=1-21.
DR PDB; 5XOL; NMR; -; A/B=1-21.
DR PDB; 6AAB; NMR; -; A=1-21.
DR PDB; 6AFQ; NMR; -; A=1-20.
DR PDB; 6GD5; NMR; -; B=1-21.
DR PDB; 8TFV; NMR; -; A=1-21.
DR PDBsum; 5XO3; -.
DR PDBsum; 5XO4; -.
DR PDBsum; 5XO5; -.
DR PDBsum; 5XO9; -.
DR PDBsum; 5XOA; -.
DR PDBsum; 5XOK; -.
DR PDBsum; 5XOL; -.
DR PDBsum; 6AAB; -.
DR PDBsum; 6AFQ; -.
DR PDBsum; 6GD5; -.
DR PDBsum; 8TFV; -.
DR AlphaFoldDB; P55788; -.
DR BMRB; P55788; -.
DR SMR; P55788; -.
DR EvolutionaryTrace; P55788; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Fungicide; Immunity; Innate immunity; Secreted.
FT PEPTIDE 1..21
FT /note="Thanatin"
FT /id="PRO_0000043595"
FT DISULFID 11..18
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5XO9"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5XO3"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:5XO3"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:5XO3"
SQ SEQUENCE 21 AA; 2436 MW; C073A20CF10359E6 CRC64;
GSKKPVPIIY CNRRTGKCQR M
