NDB4K_PANIM
ID NDB4K_PANIM Reviewed; 68 AA.
AC R4JQZ0;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Pantinin-2 {ECO:0000303|PubMed:23624072};
DE AltName: Full=Non-disulfide-bridged peptide 4.21 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.21 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 5.22 {ECO:0000303|PubMed:23624072};
DE Short=NDBP-5.22 {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, NOMENCLATURE, AND
RP PROBABLE AMIDATION AT LEU-36.
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 8% of hemolysis). Minimal inhibitory concentration (MIC) are the
CC following: 48 uM against S.aureus, 36 uM against B.magaterium, 18 uM
CC against M.luteus, 36 uM against vancomycin-resistant Enterococci, 28 uM
CC against methicillin-resistant S.aureus, 48 uM against E.coli, >87 uM
CC against P.putida, >87 uM against K.oxytoca, >87 uM against E.cloacae,
CC 68 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.
CC {ECO:0000305|PubMed:23624072}.
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; KC538865; AGK88381.1; -; mRNA.
DR AlphaFoldDB; R4JQZ0; -.
DR SMR; R4JQZ0; -.
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 1: Evidence at protein level;
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-2"
FT /evidence="ECO:0000305|PubMed:23624072"
FT /id="PRO_0000432377"
FT PROPEP 40..68
FT /evidence="ECO:0000305|PubMed:23624072"
FT /id="PRO_0000432378"
FT MOD_RES 36
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:23624072"
SQ SEQUENCE 68 AA; 7745 MW; D4274D57CCD58964 CRC64;
MKAQFAILLI TLVLFQMFSQ SEAIFGAIWK GISSLLGKRG LNNLNDFDEL FDGEITKADL
DFMREIMK
