ANOP_ANOSM
ID ANOP_ANOSM Reviewed; 10 AA.
AC P0C005;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Anoplin {ECO:0000303|PubMed:11738089, ECO:0000303|PubMed:15635634, ECO:0000303|PubMed:17994639};
DE Short=ANP {ECO:0000303|PubMed:17994639};
DE AltName: Full=As-183 {ECO:0000303|PubMed:11006592};
OS Anoplius samariensis (Solitary wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Pompiloidea;
OC Pompilidae; Pompilinae; Anoplius.
OX NCBI_TaxID=200614;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT LEU-10, SUBCELLULAR LOCATION, SYNTHESIS, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=11006592;
RX DOI=10.1002/1097-0231(20001015)14:19<1828::aid-rcm101>3.0.co;2-g;
RA Hisada M., Konno K., Itagaki Y., Naoki H., Nakajima T.;
RT "Advantages of using nested collision induced dissociation/post-source
RT decay with matrix-assisted laser desorption/ionization time-of-flight mass
RT spectrometry: sequencing of novel peptides from wasp venom.";
RL Rapid Commun. Mass Spectrom. 14:1828-1834(2000).
RN [2]
RP PROTEIN SEQUENCE, SYNTHESIS, MASS SPECTROMETRY, FUNCTION, AND MOLECULAR
RP MODELING.
RC TISSUE=Venom;
RX PubMed=11738089; DOI=10.1016/s0167-4838(01)00271-0;
RA Konno K., Hisada M., Fontana R., Lorenzi C.C.B., Naoki H., Itagaki Y.,
RA Miwa A., Kawai N., Nakata Y., Yasuhara T., Ruggiero Neto J.,
RA de Azevedo W.F. Jr., Palma M.S., Nakajima T.;
RT "Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp
RT Anoplius samariensis.";
RL Biochim. Biophys. Acta 1550:70-80(2001).
RN [3]
RP PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, MASS SPECTROMETRY, AND MUTAGENESIS
RP OF GLY-1; LEU-2; LEU-3; LYS-4; ARG-5; ILE-6; LYS-7; THR-8; LEU-9 AND
RP LEU-10.
RC TISSUE=Venom;
RX PubMed=15635634; DOI=10.1002/psc.598;
RA Ifrah D., Doisy X., Ryge T.S., Hansen P.R.;
RT "Structure-activity relationship study of anoplin.";
RL J. Pept. Sci. 11:113-121(2005).
RN [4]
RP SYNTHESIS WITH AND WITHOUT AMIDATION.
RX PubMed=17994639; DOI=10.1002/psc.960;
RA Dos Santos Cabrera M.P., Arcisio-Miranda M., Broggio Costa S.T., Konno K.,
RA Ruggiero J.R., Procopio J., Ruggiero Neto J.;
RT "Study of the mechanism of action of anoplin, a helical antimicrobial
RT decapeptide with ion channel-like activity, and the role of the amidated C-
RT terminus.";
RL J. Pept. Sci. 14:661-669(2008).
RN [5]
RP FUNCTION ON FUNGUS.
RX PubMed=24472551; DOI=10.1016/j.bbrc.2014.01.097;
RA Jindrichova B., Burketova L., Novotna Z.;
RT "Novel properties of antimicrobial peptide anoplin.";
RL Biochem. Biophys. Res. Commun. 444:520-524(2014).
RN [6]
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 [7]
RP STRUCTURE BY NMR OF WILD-TYPE AND MUTANTS, MUTAGENESIS OF ARG-5 AND THR-8,
RP AND FUNCTION.
RX PubMed=25530580; DOI=10.1002/cbic.201402581;
RA Uggerhoej L.E., Poulsen T.J., Munk J.K., Fredborg M., Sondergaard T.E.,
RA Frimodt-Moller N., Hansen P.R., Wimmer R.;
RT "Rational design of alpha-helical antimicrobial peptides: do's and
RT don'ts.";
RL ChemBioChem 16:242-253(2015).
CC -!- FUNCTION: Antimicrobial peptide that exhibits broad-spectrum
CC antimicrobial activity against both Gram-positive and Gram-negative
CC bacteria (PubMed:11738089, PubMed:15635634, PubMed:25530580). Also
CC shows antifungal activities (PubMed:24472551). Exhibits potent activity
CC in stimulating degranulation from rat peritoneal mast cells but not
CC from RBL-2H3 cells (PubMed:11738089). Has little or no hemolytic
CC activity towards human erythrocytes (PubMed:15635634, PubMed:25530580).
CC {ECO:0000269|PubMed:11738089, ECO:0000269|PubMed:15635634,
CC ECO:0000269|PubMed:25530580}.
CC -!- SUBUNIT: A n-merization is probable.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11006592}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11006592}.
CC -!- PTM: The C-terminal amidation is crucial for activity, since the
CC carboxylated peptide has antimicrobial and mast cell degranulation
CC activities drastically reduced compared to amidated peptide. However,
CC the carboxylated peptide has no hemolytic activity, like the amidated
CC peptide. {ECO:0000269|PubMed:17994639}.
CC -!- MASS SPECTROMETRY: Mass=1153.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11738089};
CC -!- MASS SPECTROMETRY: Mass=1153.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15635634};
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DR PDB; 2MJQ; NMR; -; A=1-10.
DR PDB; 2MJR; NMR; -; A=1-10.
DR PDB; 2MJS; NMR; -; A=1-10.
DR PDB; 2MJT; NMR; -; A=1-10.
DR PDBsum; 2MJQ; -.
DR PDBsum; 2MJR; -.
DR PDBsum; 2MJS; -.
DR PDBsum; 2MJT; -.
DR BMRB; P0C005; -.
DR SMR; P0C005; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Fungicide; Secreted.
FT PEPTIDE 1..10
FT /note="Anoplin"
FT /evidence="ECO:0000269|PubMed:11006592"
FT /id="PRO_0000044108"
FT MOD_RES 10
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:11006592"
FT MUTAGEN 1
FT /note="G->A: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 1
FT /note="G->K: Decrease in antimicrobial activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 2
FT /note="L->A: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 3
FT /note="L->A: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 4
FT /note="K->A: Decrease in antimicrobial activity against
FT S.aureus and better against E.coli and no change in
FT hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 5
FT /note="R->A,I,L: Increase in antimicrobial activity and
FT gain in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 5
FT /note="R->F: Increase in antimicrobial activity and gain in
FT hemolytic activity. In R5F/T8W; gain in hemolytic activity
FT (EC(50)=2 uM)."
FT /evidence="ECO:0000269|PubMed:15635634,
FT ECO:0000269|PubMed:25530580"
FT MUTAGEN 5
FT /note="R->K: Decrease in antimicrobial activity, but no
FT change in hemolytic activity. In R5K/T8W; In R5K/T8W;
FT Increase in antimicrobial activity and gain in hemolytic
FT activity (EC(50)=130 uM)."
FT /evidence="ECO:0000269|PubMed:15635634,
FT ECO:0000269|PubMed:25530580"
FT MUTAGEN 5
FT /note="R->N: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 5
FT /note="R->W: Increase in antimicrobial activity and gain in
FT hemolytic activity (EC(50)=20 uM)."
FT /evidence="ECO:0000269|PubMed:15635634,
FT ECO:0000269|PubMed:25530580"
FT MUTAGEN 6
FT /note="I->A: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 7
FT /note="K->A: Increase in antimicrobial activity and gain in
FT hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 8
FT /note="T->A,F,I,L: Increase in antimicrobial activity and
FT gain in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 8
FT /note="T->K: Increase in antimicrobial activity and gain of
FT low hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 8
FT /note="T->N: Increase in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 8
FT /note="T->V: Decrease in antimicrobial activity against
FT S.aureus and better against E.coli and gain in hemolytic
FT activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 8
FT /note="T->W: Increase in antimicrobial activity and gain in
FT hemolytic activity. In R5F/T8W; gain in hemolytic activity
FT (EC(50)=2 uM). In R5K/T8W; Increase in antimicrobial
FT activity and gain in hemolytic activity (EC(50)=130 uM)."
FT /evidence="ECO:0000269|PubMed:15635634,
FT ECO:0000269|PubMed:25530580"
FT MUTAGEN 9
FT /note="L->A: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT MUTAGEN 10
FT /note="L->A: Decrease in antimicrobial activity, but no
FT change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:15635634"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:2MJQ"
SQ SEQUENCE 10 AA; 1155 MW; 550CAAA330440337 CRC64;
GLLKRIKTLL
