ID   NDB2S_OPICA             Reviewed;          44 AA.
AC   P83314;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Opistoporin-2 {ECO:0000303|PubMed:12354111};
DE            Short=OP2 {ECO:0000303|PubMed:12354111};
DE   AltName: Full=Non-disulfide-bridged peptide 3.6 {ECO:0000303|PubMed:16036557};
DE            Short=NDBP-3.6 {ECO:0000303|PubMed:16036557};
OS   Opistophthalmus carinatus (African yellow leg scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Opistophthalminae;
OC   Opistophthalmus.
OX   NCBI_TaxID=190115;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12354111; DOI=10.1046/j.1432-1033.2002.03177.x;
RA   Moerman L.F.A., Bosteels S., Noppe W., Willems J., Clynen E., Schoofs L.,
RA   Thevissen K., Tytgat J., Van Eldere J., van der Walt J., Verdonck F.;
RT   "Antibacterial and antifungal properties of alpha-helical, cationic
RT   peptides in the venom of scorpions from southern Africa.";
RL   Eur. J. Biochem. 269:4799-4810(2002).
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).
CC   -!- FUNCTION: At high concentrations, acts as pore former in cellular
CC       membranes and causes the leakage of the cells. At submicromolar
CC       concentrations, degranulates granulocytes and has a weak hemolytic
CC       activity against human erythrocytes. Also strongly inhibits the
CC       production of superoxide anions. Has a strong antibacterial activity
CC       against Gram-negative bacteria but is less active against Gram-positive
CC       bacteria. Also has antifungal activity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12354111}. Target
CC       cell membrane {ECO:0000269|PubMed:12354111}. Note=Forms a helical
CC       membrane channel in the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4870; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12354111};
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; P83314; -.
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; IPR012526; Antimicrobial_7.
DR   Pfam; PF08102; Antimicrobial_7; 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   CHAIN           1..44
FT                   /note="Opistoporin-2"
FT                   /id="PRO_0000152880"
SQ   SEQUENCE   44 AA;  4871 MW;  6117C9B3634373E7 CRC64;
     GKVWDWIKST AKKLWNSEPV KELKNTALNA AKNFVAEKIG ATPS