ID   PAP2_PARPV              Reviewed;          33 AA.
AC   P23067;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Pardaxin P-2;
DE   AltName: Full=Pardaxin Pa2;
OS   Pardachirus pavoninus (Peacock sole) (Achirus pavoninus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Pardachirus.
OX   NCBI_TaxID=8286;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=17737623; DOI=10.1126/science.233.4761.341;
RA   Thompson S.A., Tachibana K., Nakanishi K., Kubota I.;
RT   "Melittin-like peptides from the shark-repelling defense secretion of the
RT   sole Pardachirus pavoninus.";
RL   Science 233:341-343(1986).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=1868074; DOI=10.1021/bi00246a019;
RA   Zagorski M.G., Norman D.G., Barrow C.J., Iwashita T., Tachibana K.,
RA   Patel D.J.;
RT   "Solution structure of pardaxin P-2.";
RL   Biochemistry 30:8009-8017(1991).
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.
CC   -!- SUBUNIT: In aqueous solution exists as a tetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Forms a
CC       helical 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   PIR; B60907; B60907.
DR   AlphaFoldDB; P23067; -.
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   Direct protein sequencing; Ion transport; Membrane; Secreted;
KW   Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT   PEPTIDE         1..33
FT                   /note="Pardaxin P-2"
FT                   /id="PRO_0000044783"
SQ   SEQUENCE   33 AA;  3324 MW;  5ABFF96CA04C910D CRC64;
     GFFALIPKII SSPIFKTLLS AVGSALSSSG GQE