NDB4E_VAEMS
ID NDB4E_VAEMS Reviewed; 69 AA.
AC I0DEB4;
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 CT2 {ECO:0000303|PubMed:22342498};
DE Short=VmCT2 {ECO:0000303|PubMed:22342498};
DE AltName: Full=Non-disulfide-bridged peptide 4.14 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.14 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 5.14 {ECO:0000303|PubMed:23624072};
DE Short=NDBP-5.14 {ECO:0000303|PubMed:23624072};
DE Flags: Precursor;
OS Vaejovis mexicanus smithi (Mexican scorpion) (Vaejovis smithi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Chactoidea; Vaejovidae; Vaejovis.
OX NCBI_TaxID=1562928;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 24-36, FUNCTION, AND CIRCULAR
RP DICHROISM ANALYSIS.
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).
RN [2]
RP NOMENCLATURE.
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 [3]
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 shows antibacterial activities
CC against both Gram-positive (MIC=10 uM, 20 uM and 20 uM against
CC S.aureus, B.subtilis and S.agalactiae, respectively) and Gram-negative
CC bacteria (MIC=20 uM, 10 uM, and 10 uM against E.coli, S.typhi, and
CC P.aeruginosa, respectively). Is mildly hemolytic at its MIC range, but
CC shows a strong cytotoxic activity at higher concentrations, reaching
CC 84% lysis at 50 uM. {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; JQ086326; AFH87945.1; -; mRNA.
DR AlphaFoldDB; I0DEB4; -.
DR SMR; I0DEB4; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Cytolysis; Hemolysis; 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 CT2"
FT /id="PRO_0000418783"
FT PROPEP 40..69
FT /evidence="ECO:0000250"
FT /id="PRO_0000418784"
FT SITE 29
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 69 AA; 7897 MW; 89CFB2C242DF28BB CRC64;
MKTQFVILIV AVVLLQLIAN SEAFLSTLWN AAKSIFGKRG LRNLDNLDDD IFEPEMSEAD
LRYLQDLLR
