ID   NDBM_LYCMC              Reviewed;          72 AA.
AC   D9U2B5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Bradykinin-potentiating peptide NDBP6;
DE            Short=BPP-6;
DE   Flags: Precursor;
OS   Lychas mucronatus (Chinese swimming scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX   NCBI_TaxID=172552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hainan; TISSUE=Venom gland;
RX   PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA   Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT   "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT   mucronatus reveals intraspecific toxic gene diversity and new venomous
RT   components.";
RL   BMC Genomics 11:452-452(2010).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=23731212; DOI=10.1021/pr4003068;
RA   Verano-Braga T., Dutra A.A., Leon I.R., Melo-Braga M.N., Roepstorff P.,
RA   Pimenta A.M., Kjeldsen F.;
RT   "Moving pieces in a venomic puzzle: unveiling post-translationally modified
RT   toxins from Tityus serrulatus.";
RL   J. Proteome Res. 12:3460-3470(2013).
CC   -!- FUNCTION: Amphipathic peptide that shows bradykinin potentiating
CC       activity and antimicrobial activities against bacteria and fungi. Has
CC       higher antibacterial activities against Gram-negative than against
CC       Gram-positive bacteria. Also inhibits NADPH oxidase-dependent
CC       superoxide production (IC(50) is 0.4 uM on granulocytes stimulated with
CC       PMA, IC(50) is 0.51 uM on HL-60 cells undifferentiated and IC(50) is
CC       0.53 uM on HL-60 cells treated with DMSO). The C-terminal peptide shows
CC       a higher bradykinin potentiating activity than the complete peptide.
CC       {ECO:0000250|UniProtKB:Q9Y0X4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20663230}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Long chain multifunctional peptide (group 2) family.
CC       {ECO:0000305}.
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DR   EMBL; EU163889; ABY26698.1; -; mRNA.
DR   AlphaFoldDB; D9U2B5; -.
DR   SMR; D9U2B5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Hypotensive agent;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..69
FT                   /note="Bradykinin-potentiating peptide NDBP6"
FT                   /id="PRO_0000403870"
FT   PROPEP          70..72
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000403871"
SQ   SEQUENCE   72 AA;  8355 MW;  C24484CD801857C6 CRC64;
     MNKKTLLVIF FVTMLIVDEV NSFRFGSFLK KVWKSKLAKK LRSKGKQLLK DYANRVLNGP
     EEEAAAPAER RR