ID   NDB31_PANIM             Reviewed;          24 AA.
AC   P83240;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Pandinin-2;
DE            Short=Pin2;
DE   AltName: Full=Non-disulfide-bridged peptide 3.1 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-3.1 {ECO:0000303|PubMed:24184590};
DE   AltName: Full=Non-disulfide-bridged peptide 4.1 {ECO:0000303|PubMed:16036557};
DE            Short=NDBP-4.1 {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;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   STRUCTURE BY NMR.
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   FUNCTION.
RX   PubMed=15328050; DOI=10.1016/j.bbamem.2004.05.007;
RA   Belokoneva O.S., Satake H., Mal'tseva E.L., Pal'mina N.P., Villegas E.,
RA   Nakajima T., Corzo G.;
RT   "Pore formation of phospholipid membranes by the action of two hemolytic
RT   arachnid peptides of different size.";
RL   Biochim. Biophys. Acta 1664:182-188(2004).
RN   [3]
RP   FUNCTION ON E.COLI S.AUREUS AND HUMAN ERYTHROCYTES.
RC   TISSUE=Venom;
RX   PubMed=23093034; DOI=10.1038/ja.2012.87;
RA   Garcia F., Villegas E., Espino-Solis G.P., Rodriguez A.,
RA   Paniagua-Solis J.F., Sandoval-Lopez G., Possani L.D., Corzo G.;
RT   "Antimicrobial peptides from arachnid venoms and their microbicidal
RT   activity in the presence of commercial antibiotics.";
RL   J. Antibiot. 66:3-10(2013).
RN   [4]
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   [5]
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   [6]
RP   STRUCTURE BY NMR, AND PORE FORMATION MECHANISM MODEL.
RX   PubMed=15298871; DOI=10.1529/biophysj.104.043513;
RA   Nomura K., Corzo G., Nakajima T., Iwashita T.;
RT   "Orientation and pore-forming mechanism of a scorpion pore-forming peptide
RT   bound to magnetically oriented lipid bilayers.";
RL   Biophys. J. 87:2497-2507(2004).
CC   -!- FUNCTION: Disrupts cell membranes through formation of pores. Has
CC       strong antimicrobial activity against Gram-positive bacteria
CC       B.subtilis, S.epidermidis, E.faecalis and S.aureus. Is less active
CC       against Gram-negative bacteria P.aeruginosa and E.coli. Also increases
CC       efficacy of antibiotics (ampicillin, chloramphenicol, streptomycin,
CC       kanamycin, novobiocin) when tested against E.coli, probably by
CC       facilitating their incorporation into the bacteria. Possesses
CC       antifungal activity against C.albicans and hemolytic activity against
CC       human, sheep and pig erythrocytes. {ECO:0000269|PubMed:11563967,
CC       ECO:0000269|PubMed:15328050, ECO:0000269|PubMed:23093034}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11563967}. Target
CC       cell membrane. Note=Forms a helical membrane channel in the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2612.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11563967};
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Medium-length antimicrobial peptide (group 3) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83240; -.
DR   TCDB; 1.C.124.1.1; 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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR012523; Antimicrobial_4.
DR   Pfam; PF08024; Antimicrobial_4; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Fungicide;
KW   Hemolysis; Ion transport; Membrane; Secreted; Target cell membrane;
KW   Target membrane; Transmembrane; Transport.
FT   PEPTIDE         1..24
FT                   /note="Pandinin-2"
FT                   /id="PRO_0000043483"
SQ   SEQUENCE   24 AA;  2612 MW;  DD69E407A7C59EDC CRC64;
     FWGALAKGAL KLIPSLFSSF SKKD