ID   NDB2_OPICY              Reviewed;          81 AA.
AC   C7C1L2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Probable antimicrobial peptide Con13 {ECO:0000303|PubMed:19379768};
DE   Flags: Precursor;
OS   Opisthacanthus cayaporum (South American scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Opisthacanthus.
OX   NCBI_TaxID=573324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=19379768; DOI=10.1016/j.toxicon.2009.04.010;
RA   Silva E.C., Camargos T.S., Maranhao A.Q., Silva-Pereira I., Silva L.P.,
RA   Possani L.D., Schwartz E.F.;
RT   "Cloning and characterization of cDNA sequences encoding for new venom
RT   peptides of the Brazilian scorpion Opisthacanthus cayaporum.";
RL   Toxicon 54:252-261(2009).
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|UniProtKB:P83313}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83313}. Target
CC       cell membrane {ECO:0000250|UniProtKB:P83313}. Note=Forms a helical
CC       membrane channel in the prey. {ECO:0000250|UniProtKB:P83313}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19379768}.
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   EMBL; FM998759; CAX51404.1; -; mRNA.
DR   AlphaFoldDB; C7C1L2; -.
DR   PRIDE; C7C1L2; -.
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   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Cytolysis; Fungicide; Hemolysis; Ion transport;
KW   Membrane; Secreted; Signal; Target cell membrane; Target membrane;
KW   Transmembrane; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..65
FT                   /note="Probable antimicrobial peptide Con13"
FT                   /evidence="ECO:0000305|PubMed:19379768"
FT                   /id="PRO_5000502070"
FT   PROPEP          66..81
FT                   /evidence="ECO:0000250|UniProtKB:P83313"
FT                   /id="PRO_5000502071"
SQ   SEQUENCE   81 AA;  9007 MW;  2276D1D87B969663 CRC64;
     MNRKLLLVFL VVAMLVMQPA EAGFWSKIKD FAKKAWNSPL ANELKSKALN AAKNFVSEKI
     GATPSEAGQI PFDEFMDVLY S