ID   NDB23_PANIM             Reviewed;          44 AA.
AC   P83239;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Pandinin-1;
DE            Short=Pin1;
DE   AltName: Full=Non-disulfide-bridged peptide 2.3 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-2.3 {ECO:0000303|PubMed:24184590};
DE   AltName: Full=Non-disulfide-bridged peptide 3.4 {ECO:0000303|PubMed:16036557};
DE            Short=NDBP-3.4 {ECO:0000303|PubMed:16036557};
OS   Pandinus imperator (Emperor scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Pandininae; Pandinus.
OX   NCBI_TaxID=55084 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11563967; DOI=10.1042/0264-6021:3590035;
RA   Corzo G., Escoubas P., Villegas E., Barnham K.J., He W., Norton R.S.,
RA   Nakajima T.;
RT   "Characterization of unique amphipathic antimicrobial peptides from venom
RT   of the scorpion Pandinus imperator.";
RL   Biochem. J. 359:35-45(2001).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=16036557; DOI=10.1080/15216540500058899;
RA   Zeng X.C., Corzo G., Hahin R.;
RT   "Scorpion venom peptides without disulfide bridges.";
RL   IUBMB Life 57:13-21(2005).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
RN   [4]
RP   STRUCTURE BY NMR, AND MUTAGENESIS.
RX   PubMed=16199510; DOI=10.1529/biophysj.105.070292;
RA   Nomura K., Ferrat G., Nakajima T., Darbon H., Iwashita T., Corzo G.;
RT   "Induction of morphological changes in model lipid membranes and the
RT   mechanism of membrane disruption by a large scorpion-derived pore-forming
RT   peptide.";
RL   Biophys. J. 89:4067-4080(2005).
CC   -!- FUNCTION: Disrupts cell membranes through formation of pores. Strong
CC       antimicrobial activity against Gram-positive bacteria B.subtilis,
CC       S.epidermidis, E.faecalis and S.aureus. Less active against Gram-
CC       negative bacteria P.aeruginosa and E.coli. Has no antifungal or
CC       hemolytic activity. {ECO:0000269|PubMed:11563967}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Forms a
CC       helical membrane channel in the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:11563967}.
CC   -!- MASS SPECTROMETRY: Mass=4799.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11563967};
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Long chain multifunctional peptide (group 2) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83239; -.
DR   SMR; P83239; -.
DR   TCDB; 1.C.124.2.1; the antimicrobial pore-forming pandinin (pin) family.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR012526; Antimicrobial_7.
DR   Pfam; PF08102; Antimicrobial_7; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Ion transport;
KW   Membrane; Secreted; Target cell membrane; Target membrane; Transmembrane;
KW   Transport.
FT   CHAIN           1..44
FT                   /note="Pandinin-1"
FT                   /id="PRO_0000152881"
SQ   SEQUENCE   44 AA;  4800 MW;  F0F77D4F1412A17E CRC64;
     GKVWDWIKSA AKKIWSSEPV SQLKGQVLNA AKNYVAEKIG ATPT