NDB4J_PANIM
ID NDB4J_PANIM Reviewed; 69 AA.
AC R4JNJ5;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Pantinin-1 {ECO:0000303|PubMed:23624072};
DE AltName: Full=Non-disulfide-bridged peptide 4.20 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.20 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 5.21 {ECO:0000303|PubMed:23624072};
DE Short=NDBP-5.21 {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 24-37, 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 very low hemolytic activities against human erythrocytes (64
CC uM induce 21% of hemolysis). Minimal inhibitory concentration (MIC) are
CC the following: 8 uM against S.aureus, 32 uM against B.magaterium, 32 uM
CC against M.luteus, 28 uM against vancomycin-resistant Enterococci, 14 uM
CC against methicillin-resistant S.aureus, 62 uM against E.coli, >87 uM
CC against P.putida, >87 uM against K.oxytoca, 76 uM against E.cloacae, 72
CC uM against S.enterica and 16 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; KC538864; AGK88380.1; -; mRNA.
DR AlphaFoldDB; R4JNJ5; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Fungicide; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PEPTIDE 24..37
FT /note="Pantinin-1"
FT /id="PRO_0000432375"
FT PROPEP 41..69
FT /evidence="ECO:0000250"
FT /id="PRO_0000432376"
FT MOD_RES 37
FT /note="Valine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 69 AA; 7891 MW; F937E27F86055CE2 CRC64;
MKTQFVILMI TVILMQMLVQ TEGGILGKLW EGFKSIVGKR GLNDRDQLDD LFDSDLSDAD
IKLLKEMFK
