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NDB4L_PANIM
ID   NDB4L_PANIM             Reviewed;          68 AA.
AC   R4JJN6;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Pantinin-3;
DE   AltName: Full=Non-disulfide-bridged peptide 4.22 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-4.22 {ECO:0000303|PubMed:24184590};
DE   AltName: Full=Non-disulfide-bridged peptide 5.23 {ECO:0000303|PubMed:23624072};
DE            Short=NDBP-5.23 {ECO:0000303|PubMed:23624072};
DE   Flags: Precursor;
OS   Pandinus imperator (Emperor scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Pandininae; Pandinus.
OX   NCBI_TaxID=55084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 24-36, FUNCTION, AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=23624072; DOI=10.1016/j.peptides.2013.03.026;
RA   Zeng X.C., Zhou L., Shi W., Luo X., Zhang L., Nie Y., Wang J., Wu S.,
RA   Cao B., Cao H.;
RT   "Three new antimicrobial peptides from the scorpion Pandinus imperator.";
RL   Peptides 45:28-34(2013).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
CC   -!- FUNCTION: Amphipathic peptide that possesses relatively strong
CC       activities against Gram-positive bacteria and a fungus, but has very
CC       weak antimicrobial activities against Gram-negative bacteria. Also
CC       exhibits mild hemolytic activities against human erythrocytes (16 uM
CC       induce 70% of hemolysis). Furthermore, this peptide potently inhibits
CC       the growth of vancomycin-resistant Enterococcus (VRE) S13, a pathogen
CC       that can cause a number of human infections. Minimal inhibitory
CC       concentration (MIC) are the following: 16 uM against S.aureus, 6 uM
CC       against B.magaterium, 8 uM against M.luteus, 4 uM against VRE, 12 uM
CC       against methicillin-resistant S.aureus, 36 uM against E.coli, >87 uM
CC       against P.putida, 87 uM against K.oxytoca, >87 uM against E.cloacae, 84
CC       uM against S.enterica and 17 uM against the fungus C.tropicalis.
CC       {ECO:0000269|PubMed:23624072}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms an alpha-helical membrane channel in the
CC       prey. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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; KC538866; AGK88382.1; -; mRNA.
DR   AlphaFoldDB; R4JJN6; -.
DR   SMR; R4JJN6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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.
PE   3: Inferred from homology;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytolysis; Fungicide; Hemolysis; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..36
FT                   /note="Pantinin-3"
FT                   /id="PRO_0000432379"
FT   PROPEP          40..68
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000432380"
FT   MOD_RES         36
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   68 AA;  7674 MW;  3252EE0414CFCA10 CRC64;
     MKTQFAILLI ALVLFQLLSQ SDAFLSTIWN GIKSLLGRRG LNELDNLDEL FDGEISQADI
     DFLKELMS
 
 
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