ID   PAP4_PARMA              Reviewed;          33 AA.
AC   P81861;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Pardaxin P-4;
DE   AltName: Full=Pardaxin P1a;
DE   AltName: Full=Pardaxin Pa4;
OS   Pardachirus marmoratus (Finless sole) (Achirus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Pardachirus.
OX   NCBI_TaxID=31087;
RN   [1]
RP   PROTEIN SEQUENCE, AND SYNTHESIS.
RC   TISSUE=Skin secretion;
RX   PubMed=2462511; DOI=10.1016/0014-5793(88)81007-x;
RA   Shai Y., Fox J., Caratsch C., Shih Y.-L., Edwards C., Lazarovici P.;
RT   "Sequencing and synthesis of pardaxin, a polypeptide from the Red sea moses
RT   sole with ionophore activity.";
RL   FEBS Lett. 242:161-166(1988).
RN   [2]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=12124282; DOI=10.1016/s0006-3495(02)75226-0;
RA   Hallock K.J., Lee D.K., Omnaas J., Mosberg H.I., Ramamoorthy A.;
RT   "Membrane composition determines pardaxin's mechanism of lipid bilayer
RT   disruption.";
RL   Biophys. J. 83:1004-1013(2002).
RN   [3]
RP   STRUCTURE BY NMR, AND SYNTHESIS.
RX   PubMed=15292173; DOI=10.1074/jbc.m405454200;
RA   Porcelli F., Buck B., Lee D.-K., Hallock K.J., Ramamoorthy A., Veglia G.;
RT   "Structure and orientation of pardaxin determined by NMR experiments in
RT   model membranes.";
RL   J. Biol. Chem. 279:45815-45823(2004).
RN   [4]
RP   STRUCTURE BY NMR IN COMPLEX WITH LIPOPOLYSACCHARIDE MICELLES, FUNCTION,
RP   SUBCELLULAR LOCATION, AND CIRCULAR DICHROISM.
RX   PubMed=19959835; DOI=10.1074/jbc.m109.065672;
RA   Bhunia A., Domadia P.N., Torres J., Hallock K.J., Ramamoorthy A.,
RA   Bhattacharjya S.;
RT   "NMR structure of pardaxin, a pore-forming antimicrobial peptide, in
RT   lipopolysaccharide micelles: mechanism of outer membrane
RT   permeabilization.";
RL   J. Biol. Chem. 285:3883-3895(2010).
CC   -!- FUNCTION: Exhibits unusual shark repellent and surfactant properties.
CC       Forms voltage-dependent, ion-permeable channels in membranes. At high
CC       concentration causes cell membrane lysis. {ECO:0000269|PubMed:12124282,
CC       ECO:0000269|PubMed:19959835}.
CC   -!- SUBUNIT: Monomer. In aqueous solution exists as a tetramer (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19959835}. Target
CC       cell membrane {ECO:0000269|PubMed:19959835}. Note=Forms a helical
CC       membrane channel in the prey.
CC   -!- DOMAIN: Consists of a C-terminal hydrophilic region and a predominantly
CC       hydrophobic remainder.
CC   -!- SIMILARITY: Belongs to the pardaxin family. {ECO:0000305}.
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DR   PDB; 1XC0; NMR; -; A=1-33.
DR   PDB; 2KNS; NMR; -; A=1-33.
DR   PDBsum; 1XC0; -.
DR   PDBsum; 2KNS; -.
DR   AlphaFoldDB; P81861; -.
DR   SMR; P81861; -.
DR   TCDB; 1.A.66.1.1; the pardaxin (pardaxin) family.
DR   EvolutionaryTrace; P81861; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009990; Pardaxin.
DR   Pfam; PF07425; Pardaxin; 1.
DR   PIRSF; PIRSF037561; Pardaxin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Ion transport; Membrane; Secreted;
KW   Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT   PEPTIDE         1..33
FT                   /note="Pardaxin P-4"
FT                   /id="PRO_0000044785"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:1XC0"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:1XC0"
FT   TURN            10..14
FT                   /evidence="ECO:0007829|PDB:1XC0"
FT   HELIX           15..25
FT                   /evidence="ECO:0007829|PDB:1XC0"
FT   TURN            26..31
FT                   /evidence="ECO:0007829|PDB:1XC0"
SQ   SEQUENCE   33 AA;  3324 MW;  5ABFF96A16FC910D CRC64;
     GFFALIPKII SSPLFKTLLS AVGSALSSSG GQE