NDB25_PARSC
ID NDB25_PARSC Reviewed; 45 AA.
AC P83312;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Parabutoporin {ECO:0000303|PubMed:12354111, ECO:0000303|PubMed:15245865};
DE Short=PP {ECO:0000303|PubMed:15245865};
DE AltName: Full=Non-disulfide-bridged peptide 2.5 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-2.5 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 3.2 {ECO:0000303|PubMed:16036557};
DE Short=NDBP-3.2 {ECO:0000303|PubMed:16036557};
OS Parabuthus schlechteri (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Parabuthus.
OX NCBI_TaxID=190110;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RA Verdonck F., Bosteels S., Desmet J., Moerman L.F.A., Noppe W., Willems J.,
RA Tytgat J., van der Walt J.;
RT "A novel class of pore-forming peptides in the venom of Parabuthus
RT schlechteri Purcell (Scorpions: Buthidae).";
RL Cimbebasia 16:247-260(2000).
RN [2]
RP FUNCTION, CIRCULAR DICHROISM ANALYSIS, AND SYNTHESIS.
RC TISSUE=Venom;
RX PubMed=12354111; DOI=10.1046/j.1432-1033.2002.03177.x;
RA Moerman L.F.A., Bosteels S., Noppe W., Willems J., Clynen E., Schoofs L.,
RA Thevissen K., Tytgat J., Van Eldere J., van der Walt J., Verdonck F.;
RT "Antibacterial and antifungal properties of alpha-helical, cationic
RT peptides in the venom of scorpions from southern Africa.";
RL Eur. J. Biochem. 269:4799-4810(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SYNTHESIS, AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Venom;
RX PubMed=12457879; DOI=10.1016/s0041-0101(02)00183-6;
RA Willems J., Noppe W., Moerman L., van der Walt J., Verdonck F.;
RT "Cationic peptides from scorpion venom can stimulate and inhibit
RT polymorphonuclear granulocytes.";
RL Toxicon 40:1679-1683(2002).
RN [4]
RP FUNCTION.
RX PubMed=14575699; DOI=10.1016/j.bbrc.2003.09.175;
RA Moerman L., Verdonck F., Willems J., Tytgat J., Bosteels S.;
RT "Antimicrobial peptides from scorpion venom induce Ca(2+) signaling in HL-
RT 60 cells.";
RL Biochem. Biophys. Res. Commun. 311:90-97(2003).
RN [5]
RP FUNCTION.
RX PubMed=15245865; DOI=10.1016/j.peptides.2004.04.008;
RA Willems J., Moerman L., Bosteels S., Bruyneel E., Ryniers F., Verdonck F.;
RT "Parabutoporin -- an antibiotic peptide from scorpion venom -- can both
RT induce activation and inhibition of granulocyte cell functions.";
RL Peptides 25:1079-1084(2004).
RN [6]
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 [7]
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: At high concentrations, acts as pore former in cellular
CC membranes and causes the leakage of the cells. At submicromolar
CC concentrations, degranulates granulocytes and has a weak hemolytic
CC activity against human red blood cells. Also strongly inhibits the
CC production of superoxide anions. Has a strong antibacterial activity
CC against Gram-negative bacteria but is less active against Gram-positive
CC bacteria. Also has antifungal activity. Induces reversible G-protein
CC dependent Ca(2+) release from intracellular stores and increase Ca(2+)
CC influx in HL-60 cells. Induces the activation of the Rac pathway in
CC granulocytes. Synergistically enhances the excitatory effects of short
CC and long chain ion-channel-specific neurotoxins by interaction with the
CC neuronal membranes. {ECO:0000269|PubMed:12354111,
CC ECO:0000269|PubMed:12457879, ECO:0000269|PubMed:14575699,
CC ECO:0000269|PubMed:15245865, ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. Target cell
CC membrane {ECO:0000269|PubMed:12354111, ECO:0000269|PubMed:12457879}.
CC Note=Forms a helical membrane channel in the prey.
CC {ECO:0000269|PubMed:12354111, ECO:0000269|PubMed:12457879}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=5030.3; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
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 AlphaFoldDB; P83312; -.
DR SMR; P83312; -.
DR IntAct; P83312; 4.
DR MINT; P83312; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; 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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Fungicide;
KW Hemolysis; Ion transport; Membrane; Secreted; Target cell membrane;
KW Target membrane; Toxin; Transmembrane; Transport.
FT CHAIN 1..45
FT /note="Parabutoporin"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000066839"
FT UNSURE 11
FT /evidence="ECO:0000269|Ref.1"
FT UNSURE 44
FT /evidence="ECO:0000269|Ref.1"
FT UNSURE 45
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 45 AA; 4995 MW; 3EEFF71425FA14FA CRC64;
FKLGSFLKKA WKSKLAKKLR AKGKEMLKDY AKGLLEGGSE EVPGQ
