NDB22_MESMA
ID NDB22_MESMA Reviewed; 72 AA.
AC Q9Y0X4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Bradykinin-potentiating peptide BmKbpp;
DE AltName: Full=Bpp BmK3;
DE AltName: Full=Non-disulfide-bridged peptide 2.2 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-2.2 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 3.3 {ECO:0000303|PubMed:16036557};
DE Short=NDBP-3.3 {ECO:0000303|PubMed:16036557};
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10868911; DOI=10.1080/713803610;
RA Zeng X.-C., Li W.-X., Peng F., Zhu Z.-H.;
RT "Cloning and characterization of a novel cDNA sequence encoding the
RT precursor of a novel venom peptide (BmKbpp) related to a bradykinin-
RT potentiating peptide from Chinese scorpion Buthus martensii Karsch.";
RL IUBMB Life 49:207-210(2000).
RN [2]
RP SYNTHESIS OF 23-69, SYNTHESIS OF C-TERMINAL PEPTIDE, AND FUNCTION.
RX PubMed=22115565; DOI=10.1016/j.peptides.2011.11.012;
RA Zeng X.C., Wang S., Nie Y., Zhang L., Luo X.;
RT "Characterization of BmKbpp, a multifunctional peptide from the Chinese
RT scorpion Mesobuthus martensii Karsch: gaining insight into a new mechanism
RT for the functional diversification of scorpion venom peptides.";
RL Peptides 33:44-51(2012).
RN [3]
RP NOMENCLATURE.
RX PubMed=16036557; DOI=10.1080/15216540500058899;
RA Zeng X.C., Corzo G., Hahin R.;
RT "Scorpion venom peptides without disulfide bridges.";
RL IUBMB Life 57:13-21(2005).
RN [4]
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 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:0000269|PubMed:22115565}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Shows a very weak hemolytic activity (6 uM causes only
CC 3.5 % of hemolysis). {ECO:0000305|PubMed:22115565}.
CC -!- MISCELLANEOUS: Shows a alpha-helical structure.
CC {ECO:0000305|PubMed:22115565}.
CC -!- MISCELLANEOUS: The genomic DNA coding for this protein is not a
CC continuous sequence in the genome. The transcript of this protein may
CC be generated by trans-splicing, by which exons from two independently
CC transcribed pre-mRNAs are joined to form a single mature transcript
CC (PubMed:22115565). {ECO:0000305|PubMed:22115565}.
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; AF146744; AAD39512.1; -; mRNA.
DR EMBL; AF145952; AAF99563.1; -; mRNA.
DR EMBL; AF145953; AAF99564.1; -; mRNA.
DR AlphaFoldDB; Q9Y0X4; -.
DR SMR; Q9Y0X4; -.
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: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.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Fungicide;
KW Hypotensive agent; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..69
FT /note="Bradykinin-potentiating peptide BmKbpp"
FT /id="PRO_0000343194"
FT PROPEP 70..72
FT /evidence="ECO:0000250"
FT /id="PRO_0000343195"
SQ SEQUENCE 72 AA; 8327 MW; C256333D801857C6 CRC64;
MNKKTLLVIF FVTMLIVDEV NSFRFGSFLK KVWKSKLAKK LRSKGKQLLK DYANKVLNGP
EEEAAAPAER RR
