ID   NDB4A_ISOMC             Reviewed;          17 AA.
AC   C0HL59;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Peptide Im-4 {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 {ECO:0000303|PubMed:28941793};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT LYS-17.
RC   TISSUE=Venom {ECO:0000303|PubMed:28941793};
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-positive bacteria S.aureus NBRC 13276 (MIC=5-10
CC       uM) and B.subtilis NBRC 3009 (MIC=2.5-5 uM) but not against Gram-
CC       negative bacterium E.coli NBRC 3972. {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=1714.0; Method=MALDI; Note=Amidated.;
CC       Evidence={ECO:0000269|PubMed:28941793};
CC   -!- MASS SPECTROMETRY: Mass=1714.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28941793};
CC   -!- MISCELLANEOUS: Fragments comprising residues 4-17 and 5-17 have been
CC       detected in venom but it is unclear whether they have a physiological
CC       role or are simply due to degradation. {ECO:0000305|PubMed:28941793}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Short antimicrobial peptide (group 4) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HL59; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Membrane;
KW   Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..17
FT                   /note="Peptide Im-4"
FT                   /evidence="ECO:0000269|PubMed:28941793"
FT                   /id="PRO_0000442987"
FT   MOD_RES         17
FT                   /note="Lysine amide; partial"
FT                   /evidence="ECO:0000269|PubMed:28941793"
SQ   SEQUENCE   17 AA;  1700 MW;  6CB4561BFA2546B9 CRC64;
     FIGMIPGLIG GLISAIK