NDB24_OPICA
ID NDB24_OPICA Reviewed; 82 AA.
AC P83313; Q5VJS8; Q5VJT0;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Opistoporin-1;
DE Short=OP1;
DE AltName: Full=Non-disulfide-bridged peptide 2.4 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-2.4 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 3.5 {ECO:0000303|PubMed:16036557};
DE Short=NDBP-3.5 {ECO:0000303|PubMed:16036557};
DE AltName: Full=Opistoporin-3;
DE Short=OP3;
DE Flags: Precursor;
OS Opistophthalmus carinatus (African yellow leg scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Opistophthalminae;
OC Opistophthalmus.
OX NCBI_TaxID=190115;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Venom gland;
RA Zhu S., Tytgat J.;
RT "Precursor organization and gene structure of scorpion venom antimicrobial
RT peptides.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 23-66, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, CIRCULAR DICHROISM ANALYSIS, AND SYNTHESIS
RP OF 23-66.
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, AND SYNTHESIS OF 23-66.
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 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 [6]
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 erythrocytes. 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. {ECO:0000269|PubMed:12354111,
CC ECO:0000269|PubMed:12457879, ECO:0000269|PubMed:14575699}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12354111}. Target
CC cell membrane {ECO:0000269|PubMed:12354111}. Note=Forms a helical
CC membrane channel in the prey.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:12354111}.
CC -!- MASS SPECTROMETRY: Mass=4836; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12354111};
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; AY427948; AAQ94360.1; -; mRNA.
DR EMBL; AY427950; AAQ94362.1; -; Genomic_DNA.
DR AlphaFoldDB; P83313; -.
DR SMR; P83313; -.
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: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.
DR InterPro; IPR012526; Antimicrobial_7.
DR Pfam; PF08102; Antimicrobial_7; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Fungicide;
KW Hemolysis; Ion transport; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane; Transmembrane; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:12354111"
FT CHAIN 23..66
FT /note="Opistoporin-1"
FT /evidence="ECO:0000269|PubMed:12354111"
FT /id="PRO_0000152879"
FT PROPEP 67..82
FT /evidence="ECO:0000269|PubMed:12354111"
FT /id="PRO_0000356888"
SQ SEQUENCE 82 AA; 9275 MW; A672EF918EA36A44 CRC64;
MNRKLLFVTL MVTMLVMQPS EGGKVWDWIK STAKKLWNSE PVKELKNTAL NAAKNLVAEK
IGATPSEAGQ MPFDEFMDIL YE
