NDB49_HETPE
ID NDB49_HETPE Reviewed; 68 AA.
AC P0DJ02;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Peptide Hp1090 {ECO:0000303|PubMed:20950663};
DE AltName: Full=Non-disulfide-bridged peptide 4.9 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.9 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 5.9 {ECO:0000303|PubMed:22342498};
DE Short=NDBP-5.9 {ECO:0000303|PubMed:22342498};
DE Flags: Precursor;
OS Heterometrus petersii (Asian forest scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC Heterometrus.
OX NCBI_TaxID=754296;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 24-36, CIRCULAR DICHROISM, AND
RP FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=20950663; DOI=10.1016/j.peptides.2010.10.008;
RA Yan R., Zhao Z., He Y., Wu L., Cai D., Hong W., Wu Y., Cao Z., Zheng C.,
RA Li W.;
RT "A new natural alpha-helical peptide from the venom of the scorpion
RT Heterometrus petersii kills HCV.";
RL Peptides 32:11-19(2011).
RN [2]
RP NOMENCLATURE.
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 [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 which inhibits the growth of Gram-
CC positive bacteria. {ECO:0000269|PubMed:20950663}.
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 -!- MISCELLANEOUS: This peptide has a significant inhibitory effect on
CC hepatitis C virus (HCV) infection (IC(50)=7.62 ug/ml). Furthermore,
CC this peptide potently inhibits HCV before viral entry into cells and
CC kills HCV rapidly in vitro (PubMed:20950663).
CC {ECO:0000305|PubMed:20950663}.
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. Short antimicrobial peptide (group 4) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DJ02; -.
DR SMR; P0DJ02; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Amidation; Antibiotic; Antimicrobial; Antiviral protein;
KW Cleavage on pair of basic residues; Cytolysis; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PEPTIDE 24..36
FT /note="Peptide Hp1090"
FT /id="PRO_0000412875"
FT PROPEP 40..68
FT /evidence="ECO:0000250"
FT /id="PRO_0000412876"
FT MOD_RES 36
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 68 AA; 7741 MW; B7501364F1CE11BB CRC64;
MKTQFAIFLI TLVLFQMFSQ SDAIFKAIWS GIKSLFGKRG LSDLDDLDES FDGEVSQADI
DFLKELMQ
