NDB41_OPIMA
ID NDB41_OPIMA Reviewed; 68 AA.
AC Q8MMJ7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Cytotoxic linear peptide IsCT {ECO:0000303|PubMed:11520071};
DE AltName: Full=Non-disulfide-bridged peptide 4.1 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.1 {ECO:0000303|PubMed:24184590};
DE AltName: Full=Non-disulfide-bridged peptide 5.2 {ECO:0000303|PubMed:16036557};
DE Short=NDBP-5.2 {ECO:0000303|PubMed:16036557};
DE Contains:
DE RecName: Full=Cytotoxic linear peptide IsCTf {ECO:0000303|PubMed:12054688};
DE Flags: Precursor;
OS Opisthacanthus madagascariensis (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Opisthacanthus.
OX NCBI_TaxID=167108;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-34, MASS SPECTROMETRY,
RP SYNTHESIS, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12054688; DOI=10.1016/s0006-291x(02)00423-0;
RA Dai L., Corzo G., Naoki H., Andriantsiferana M., Nakajima T.;
RT "Purification, structure-function analysis, and molecular characterization
RT of novel linear peptides from scorpion Opisthacanthus madagascariensis.";
RL Biochem. Biophys. Res. Commun. 293:1514-1522(2002).
RN [2]
RP PROTEIN SEQUENCE OF 24-36, MASS SPECTROMETRY, SYNTHESIS, SUBCELLULAR
RP LOCATION, AND AMIDATION AT PHE-36.
RC TISSUE=Venom;
RX PubMed=11520071; DOI=10.1006/bbrc.2001.5472;
RA Dai L., Yasuda A., Naoki H., Corzo G., Andriantsiferana M., Nakajima T.;
RT "IsCT, a novel cytotoxic linear peptide from scorpion Opisthacanthus
RT madagascariensis.";
RL Biochem. Biophys. Res. Commun. 286:820-825(2001).
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).
RN [5]
RP STRUCTURE BY NMR OF 24-36, AND MUTAGENESIS OF TRP-29; GLU-30; GLY-31 AND
RP SER-34.
RX PubMed=15369808; DOI=10.1016/j.bbrc.2004.08.144;
RA Lee K., Shin S.Y., Kim K., Lim S.S., Hahm K.-S., Kim Y.;
RT "Antibiotic activity and structural analysis of the scorpion-derived
RT antimicrobial peptide IsCT and its analogs.";
RL Biochem. Biophys. Res. Commun. 323:712-719(2004).
CC -!- FUNCTION: [Cytotoxic linear peptide IsCT]: Shows weak hemolytic
CC activity and antibacterial activity against both Gram-positive and
CC Gram-negative bacteria probably by forming pores in the cell membrane.
CC IsCT adopts an amphipathic alpha-helical structure.
CC {ECO:0000269|PubMed:11520071}.
CC -!- FUNCTION: [Cytotoxic linear peptide IsCTf]: Shows neither hemolytic,
CC nor antibacterial activities, probably because it cannot adopt
CC amphipathic alpha-helical structure. {ECO:0000269|PubMed:12054688}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11520071,
CC ECO:0000269|PubMed:12054688}. Target cell membrane. Note=Forms a
CC helical membrane channel in the prey.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11520071, ECO:0000305|PubMed:12054688}.
CC -!- PTM: IsCTf is an enzymatic proteolytic cleavage product of IsCT by the
CC proteases present in the venom. {ECO:0000305|PubMed:12054688}.
CC -!- MASS SPECTROMETRY: [Cytotoxic linear peptide IsCT]: Mass=1502.00;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:12054688};
CC -!- MASS SPECTROMETRY: [Cytotoxic linear peptide IsCT]: Mass=1502.9;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:11520071};
CC -!- MASS SPECTROMETRY: [Cytotoxic linear peptide IsCTf]: Mass=1242.80;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:12054688};
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. Short antimicrobial peptide (group 4) family.
CC {ECO:0000305}.
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DR EMBL; AF397895; AAM76913.1; -; mRNA.
DR PDB; 1T51; NMR; -; A=24-36.
DR PDB; 1T52; NMR; -; A=24-36.
DR PDB; 1T54; NMR; -; A=24-36.
DR PDB; 1T55; NMR; -; A=24-36.
DR PDBsum; 1T51; -.
DR PDBsum; 1T52; -.
DR PDBsum; 1T54; -.
DR PDBsum; 1T55; -.
DR AlphaFoldDB; Q8MMJ7; -.
DR BMRB; Q8MMJ7; -.
DR SMR; Q8MMJ7; -.
DR EvolutionaryTrace; Q8MMJ7; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Ion transport; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane; Toxin; Transmembrane; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:11520071,
FT ECO:0000269|PubMed:12054688"
FT PEPTIDE 24..36
FT /note="Cytotoxic linear peptide IsCT"
FT /evidence="ECO:0000269|PubMed:11520071"
FT /id="PRO_0000035356"
FT PEPTIDE 24..34
FT /note="Cytotoxic linear peptide IsCTf"
FT /evidence="ECO:0000269|PubMed:12054688"
FT /id="PRO_0000035357"
FT PROPEP 40..68
FT /evidence="ECO:0000305"
FT /id="PRO_0000035358"
FT SITE 29
FT /note="Important for antibacterial activity, and hemolysis
FT activity"
FT MOD_RES 36
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:11520071"
FT MUTAGEN 29
FT /note="W->A: Drastic reduction in antibacterial activity
FT against both Gram-positive and Gram-negative bacteria, and
FT complete loss of hemolysis activity."
FT /evidence="ECO:0000269|PubMed:15369808"
FT MUTAGEN 29
FT /note="W->L: Drastic reduction in antibacterial activity
FT against both Gram-positive and Gram-negative bacteria, and
FT big loss of hemolysis activity. Similar or 2-fold increase
FT in antibacterial activity against both Gram-positive and
FT Gram-negative bacteria, and big loss of hemolysis activity;
FT when associated with K-34."
FT /evidence="ECO:0000269|PubMed:15369808"
FT MUTAGEN 30
FT /note="E->K: Similar or 2-fold increase in antibacterial
FT activity against both Gram-positive and Gram-negative
FT bacteria, and little loss of hemolysis activity. Similar or
FT 2-fold increase in antibacterial activity against both
FT Gram-positive and Gram-negative bacteria, and complete loss
FT of hemolysis activity; when associated with P-31 and K-34."
FT /evidence="ECO:0000269|PubMed:15369808"
FT MUTAGEN 31
FT /note="G->P: Similar or 2-fold increase in antibacterial
FT activity against both Gram-positive and Gram-negative
FT bacteria, and complete loss of hemolysis activity; when
FT associated with K-30 and K-34."
FT /evidence="ECO:0000269|PubMed:15369808"
FT MUTAGEN 34
FT /note="S->K: Similar or 2-fold increase in antibacterial
FT activity against both Gram-positive and Gram-negative
FT bacteria, and big loss of hemolysis activity; when
FT associated with L-29. Similar or 2-fold increase in
FT antibacterial activity against both Gram-positive and Gram-
FT negative bacteria, and complete loss of hemolysis; when
FT associated with K-30 and P-31."
FT /evidence="ECO:0000269|PubMed:15369808"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:1T51"
SQ SEQUENCE 68 AA; 7722 MW; FAFBC86E52583297 CRC64;
MKTQFAILLV ALVLFQMFAQ SDAILGKIWE GIKSLFGKRG LSDLDGLDEL FDGEISKADR
DFLRELMR
