AMP2_TITDI
ID AMP2_TITDI Reviewed; 64 AA.
AC P0CF37;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Bactridin-2 {ECO:0000303|PubMed:19540868};
DE Short=Bact2 {ECO:0000303|PubMed:19540868};
DE Short=Bactridine 2 {ECO:0000303|PubMed:19540868};
DE AltName: Full=P-Mice-Antm-beta* NaTx14.8;
OS Tityus discrepans (Venezuelan scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=57059;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19540868; DOI=10.1016/j.toxicon.2009.06.014;
RA Diaz P., D'Suze G., Salazar V., Sevcik C., Shannon J.D., Sherman N.E.,
RA Fox J.W.;
RT "Antibacterial activity of six novel peptides from Tityus discrepans
RT scorpion venom. A fluorescent probe study of microbial membrane Na+
RT permeability changes.";
RL Toxicon 54:802-817(2009).
RN [2]
RP NOMENCLATURE.
RX PubMed=22355312; DOI=10.1371/journal.pone.0030478;
RA Guerrero-Vargas J.A., Mourao C.B., Quintero-Hernandez V., Possani L.D.,
RA Schwartz E.F.;
RT "Identification and phylogenetic analysis of Tityus pachyurus and Tityus
RT obscurus novel putative Na+-channel scorpion toxins.";
RL PLoS ONE 7:E30478-E30478(2012).
CC -!- FUNCTION: Shows antibacterial activity against both Gram-positive
CC bacteria (B.subtilis, M.luteus, E.faecalis) and Gram-negative bacteria
CC (P.aeruginosa, Y.enterocolitica, A.calcoaceticus). Modifies membrane
CC sodium permeability on Y.enterocolitica. Is toxic to mice, but is not
CC to crabs. Induces concentration dependent haemolysis in human
CC erythrocytes (PubMed:19540868). Acts by inhibiting the sodium (Nav)
CC currents (By similarity). {ECO:0000250|UniProtKB:P0C1X7,
CC ECO:0000269|PubMed:19540868}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19540868}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19540868}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=7362; Method=Electrospray; Note=Monoisotopic.;
CC Evidence={ECO:0000269|PubMed:19540868};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CF37; -.
DR SMR; P0CF37; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..64
FT /note="Bactridin-2"
FT /evidence="ECO:0000269|PubMed:19540868"
FT /id="PRO_0000393445"
FT DOMAIN 1..63
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 11..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 15..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 23..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 27..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT UNSURE 64
SQ SEQUENCE 64 AA; 7374 MW; 4E26CA5BF8E88AC9 CRC64;
KDGYLVGNDG CKYSCFTRPG TYCANECSRV KGKDGYCYAW MACYCYSMPN WVKTWNRATN
RCGR