ID   PISC3_MORCS             Reviewed;          22 AA.
AC   P0C006;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Piscidin-3 {ECO:0000303|PubMed:11713517, ECO:0000303|PubMed:15193922};
OS   Morone chrysops x Morone saxatilis (White bass x Striped bass).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Morone.
OX   NCBI_TaxID=45352;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=11713517; DOI=10.1038/35104690;
RA   Silphaduang U., Noga E.J.;
RT   "Peptide antibiotics in mast cells of fish.";
RL   Nature 414:268-269(2001).
RN   [2]
RP   FUNCTION AS ANTIVIRAL PEPTIDE.
RX   PubMed=15193922; DOI=10.1016/j.virol.2004.02.029;
RA   Chinchar V.G., Bryan L., Silphadaung U., Noga E., Wade D.,
RA   Rollins-Smith L.;
RT   "Inactivation of viruses infecting ectothermic animals by amphibian and
RT   piscine antimicrobial peptides.";
RL   Virology 323:268-275(2004).
RN   [3]
RP   STRUCTURE BY NMR, LIPID-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=24410116; DOI=10.1021/ja411119m;
RA   Perrin B.S. Jr., Tian Y., Fu R., Grant C.V., Chekmenev E.Y.,
RA   Wieczorek W.E., Dao A.E., Hayden R.M., Burzynski C.M., Venable R.M.,
RA   Sharma M., Opella S.J., Pastor R.W., Cotten M.L.;
RT   "High-Resolution structures and orientations of antimicrobial peptides
RT   piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and
RT   bilayer immersion.";
RL   J. Am. Chem. Soc. 136:3491-3504(2014).
CC   -!- FUNCTION: Antimicrobial peptide with broad-spectrum activity against
CC       Gram-positive and Gram-negative bacteria. Rapidly inactivates both
CC       channel catfish herpesvirus (ED(50)=11 uM) and frog virus 3 (ED(50)=16
CC       uM) over a wide temperature range (PubMed:15193922). Has hemolytic
CC       activity. {ECO:0000269|PubMed:15193922}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24410116}. Membrane
CC       {ECO:0000269|PubMed:24410116}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:24410116}. Note=Associates with lipid bilayers via
CC       its amphipathic helix and can insert itself into the lipid bilayer.
CC   -!- TISSUE SPECIFICITY: Mast cells in gill, skin and gut, and in lining
CC       blood vessels in the viscera.
CC   -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR   PDB; 2MCW; NMR; -; A=1-22.
DR   PDB; 2MCX; NMR; -; A=1-22.
DR   PDB; 6PEZ; NMR; -; A=1-22.
DR   PDBsum; 2MCW; -.
DR   PDBsum; 2MCX; -.
DR   PDBsum; 6PEZ; -.
DR   AlphaFoldDB; P0C006; -.
DR   BMRB; P0C006; -.
DR   SMR; P0C006; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR012515; Antimicrobial12.
DR   Pfam; PF08107; Antimicrobial12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial; Antiviral protein;
KW   Cytolysis; Direct protein sequencing; Hemolysis; Immunity; Innate immunity;
KW   Lipid-binding; Membrane; Secreted.
FT   PEPTIDE         1..22
FT                   /note="Piscidin-3"
FT                   /evidence="ECO:0000269|PubMed:11713517"
FT                   /id="PRO_0000043417"
FT   MOD_RES         22
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250"
FT   HELIX           2..20
FT                   /evidence="ECO:0007829|PDB:2MCW"
SQ   SEQUENCE   22 AA;  2492 MW;  3F32E8F800F2FDB9 CRC64;
     FIHHIFRGIV HAGRSIGRFL TG