ID   DCRLN_OREDC             Reviewed;          11 AA.
AC   P85870;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Decoralin {ECO:0000303|PubMed:17981364, ECO:0000303|PubMed:28267894};
DE            Short=DEC {ECO:0000303|PubMed:17981364, ECO:0000303|PubMed:28267894};
OS   Oreumenes decoratus (Potter wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Eumeninae; Oreumenes.
OX   NCBI_TaxID=531920;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, CIRCULAR DICHROISM, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17981364; DOI=10.1016/j.peptides.2007.09.017;
RA   Konno K., Rangel M., Oliveira J.S., Dos Santos Cabrera M.P., Fontana R.,
RA   Hirata I.Y., Hide I., Nakata Y., Mori K., Kawano M., Fuchino H., Sekita S.,
RA   Neto J.R.;
RT   "Decoralin, a novel linear cationic alpha-helical peptide from the venom of
RT   the solitary eumenine wasp Oreumenes decoratus.";
RL   Peptides 28:2320-2327(2007).
RN   [2]
RP   REVIEW.
RX   PubMed=27096870; DOI=10.3390/toxins8040114;
RA   Konno K., Kazuma K., Nihei K.;
RT   "Peptide toxins in solitary wasp venoms.";
RL   Toxins 8:114-114(2016).
RN   [3]
RP   STRUCTURE BY NMR OF SYNTHETIC C-TERMINALLY AMIDATED PEPTIDE, AND SYNTHESIS.
RX   PubMed=28267894; DOI=10.1111/cbdd.12970;
RA   Guerra M.E.R., Fadel V., Maltarollo V.G., Baldissera G., Honorio K.M.,
RA   Ruggiero J.R., Dos Santos Cabrera M.P.;
RT   "MD simulations and multivariate studies for modeling the antileishmanial
RT   activity of peptides.";
RL   Chem. Biol. Drug Des. 90:501-510(2017).
CC   -!- FUNCTION: Linear cationic alpha-helical peptide that acts as
CC       antimicrobial peptide (PubMed:17981364). Has antibacterial activity
CC       against the Gram-positive bacteria S.aureus CCT 6538 (MIC=40 uM),
CC       S.saprophyticus (MIC=40 um), B.subtilis CCT 2471 (MIC=40 uM), and
CC       B.thuringiensis (MIC=40 uM), and against the Gram-negative bacteria
CC       E.coli ATCC 25922 (MIC=80), E.coli CCT 1371 (MIC=160), K.pneumonia ATCC
CC       13883 (MIC=80), and A.faecalis ATCC 8750 (MIC=40) (PubMed:17981364).
CC       Has antifungal activity against C.albicans (MIC=40 uM)
CC       (PubMed:17981364). At high concentrations exhibits activity in
CC       stimulating degranulation from rat peritoneal mast cells
CC       (PubMed:17981364). Has very weak hemolytic activity towards human and
CC       mouse erythrocytes (PubMed:17981364). In vitro, inhibits the growth of
CC       L.major promastigotes (IC(50)=72 uM) (PubMed:17981364).
CC       {ECO:0000269|PubMed:17981364}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17981364}. Target
CC       cell membrane {ECO:0000269|PubMed:17981364}. Note=Forms an alpha-
CC       helical membrane channel in the prey. {ECO:0000305|PubMed:28267894}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17981364}.
CC   -!- PTM: The natural peptide is not C-terminally amidated. However,
CC       amidated synthetic analogs show a much more potent activity in all the
CC       biological assays. {ECO:0000269|PubMed:17981364}.
CC   -!- MASS SPECTROMETRY: Mass=1256.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17981364};
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DR   PDB; 2N9A; NMR; -; A=1-11.
DR   PDBsum; 2N9A; -.
DR   BMRB; P85870; -.
DR   SMR; P85870; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0042832; P:defense response to protozoan; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Mast cell degranulation; Membrane;
KW   Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..11
FT                   /note="Decoralin"
FT                   /evidence="ECO:0000269|PubMed:17981364"
FT                   /id="PRO_0000343532"
FT   HELIX           2..4
FT                   /evidence="ECO:0007829|PDB:2N9A"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:2N9A"
SQ   SEQUENCE   11 AA;  1257 MW;  80826DFC24005735 CRC64;
     SLLSLIRKLI T