PAP1_PARMA
ID PAP1_PARMA Reviewed; 10 AA.
AC P81863;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Pardaxin-1;
DE AltName: Full=Pardaxin I;
DE Short=PXI;
DE Flags: Fragment;
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.
RC TISSUE=Skin secretion;
RX PubMed=3782138; DOI=10.1016/s0021-9258(18)66622-0;
RA Lazarovici P., Primor N., Loew L.M.;
RT "Purification and pore-forming activity of two hydrophobic polypeptides
RT from the secretion of the Red sea moses sole (Pardachirus marmoratus).";
RL J. Biol. Chem. 261:16704-16713(1986).
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. Shown to be 5-10 times more
CC toxic, cytolytic and active in membrane pore formation than pardaxin-2.
CC -!- SUBUNIT: Monomer. 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 -!- SIMILARITY: Belongs to the pardaxin family. {ECO:0000305}.
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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.
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..>10
FT /note="Pardaxin-1"
FT /id="PRO_0000045112"
FT NON_TER 10
SQ SEQUENCE 10 AA; 1063 MW; D399C36760572DD9 CRC64;
GFFALIPGIE