ID   NDB4S_MESSU             Reviewed;          68 AA.
AC   I0DEB5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Amphipathic peptide CT1 {ECO:0000303|PubMed:22342498};
DE            Short=VsCT1 {ECO:0000303|PubMed:22342498};
DE   AltName: Full=Non-disulfide-bridged peptide 5.11 {ECO:0000303|PubMed:22342498};
DE            Short=NDBP-5.11 {ECO:0000303|PubMed:22342498};
DE   Flags: Precursor;
OS   Mesomexovis subcristatus (Scorpion) (Vaejovis subcristatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Vaejovidae; Mesomexovis.
OX   NCBI_TaxID=1532995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 24-36, FUNCTION, CIRCULAR
RP   DICHROISM ANALYSIS, AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=22342498; DOI=10.1016/j.peptides.2012.02.002;
RA   Ramirez-Carreto S., Quintero-Hernandez V., Jimenez-Vargas J.M., Corzo G.,
RA   Possani L.D., Becerril B., Ortiz E.;
RT   "Gene cloning and functional characterization of four novel antimicrobial-
RT   like peptides from scorpions of the family Vaejovidae.";
RL   Peptides 34:290-295(2012).
CC   -!- FUNCTION: Amphipathic peptide that shows no antibacterial activity even
CC       at 50 uM but shows a low hemolytic activity against human erythrocytes.
CC       {ECO:0000269|PubMed:22342498}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms a helical membrane channel in the prey.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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   EMBL; JQ086327; AFH87946.1; -; mRNA.
DR   AlphaFoldDB; I0DEB5; -.
DR   SMR; I0DEB5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytolysis; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..36
FT                   /note="Amphipathic peptide CT1"
FT                   /id="PRO_0000418777"
FT   PROPEP          40..68
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418778"
FT   MOD_RES         36
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   68 AA;  7729 MW;  AC2A3912C0718786 CRC64;
     MKTQIVILIV AVLFLQLVSQ SDAFLKGIID TVSNWLGKRG LKNLDQYNDL FDGEISDADI
     KFLKDLMR