ID   NDB4B_ISOMC             Reviewed;          25 AA.
AC   C0HL58;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Peptide Im-5 {ECO:0000303|PubMed:28941793};
OS   Isometrus maculatus (Lesser brown scorpion) (Scorpio maculatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Isometrus.
OX   NCBI_TaxID=497827;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC
RP   DOSE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=28941793; DOI=10.1016/j.toxicon.2017.09.010;
RA   Miyashita M., Kitanaka A., Yakio M., Yamazaki Y., Nakagawa Y., Miyagawa H.;
RT   "Complete de novo sequencing of antimicrobial peptides in the venom of the
RT   scorpion Isometrus maculatus.";
RL   Toxicon 139:1-12(2017).
CC   -!- FUNCTION: Probably forms pores in target membranes. Has antibacterial
CC       activity against Gram-negative bacterium E.coli NBRC 3972 (MIC=10 uM)
CC       and against Gram-positive bacteria S.aureus NBRC 13276 (MIC=2.5-5 uM)
CC       and B.subtilis NBRC 3009 (MIC=0.5-1 uM). Toxic to cricket A.domestica.
CC       Has hemolytic activity against sheep erythrocytes.
CC       {ECO:0000269|PubMed:28941793}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28941793}. Target
CC       cell membrane {ECO:0000305|PubMed:28941793}. Note=Probably forms a
CC       helical membrane channel in the prey. {ECO:0000305|PubMed:28941793}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:28941793}.
CC   -!- MASS SPECTROMETRY: Mass=2803.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28941793};
CC   -!- TOXIC DOSE: LD(50) is 61 nmol/g by intraabdominal injection into
CC       cricket A.domestica. {ECO:0000269|PubMed:28941793}.
CC   -!- MISCELLANEOUS: Fragments comprising residues 10-25, 1-19, 7-25, 1-22,
CC       4-25 and 1-23 have been detected in venom but it is unclear whether
CC       they have a physiological role or are simply due to degradation.
CC       {ECO:0000305|PubMed:28941793}.
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; C0HL58; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0051715; P:cytolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   InterPro; IPR012523; Antimicrobial_4.
DR   Pfam; PF08024; Antimicrobial_4; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Membrane; Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..25
FT                   /note="Peptide Im-5"
FT                   /evidence="ECO:0000269|PubMed:28941793"
FT                   /id="PRO_0000442986"
SQ   SEQUENCE   25 AA;  2805 MW;  EF61297EB0D8D6F1 CRC64;
     FLGSLFSIGS KLLPGVIKLF QRKKQ