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TX1AB_ECTTU
ID   TX1AB_ECTTU             Reviewed;          34 AA.
AC   P49344;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Omega/M-ectatotoxin-Et1a subunit B {ECO:0000303|PubMed:26805882};
DE            Short=Omega/M-ECTX-Et1a subunit B {ECO:0000303|PubMed:26805882};
DE   AltName: Full=Ectatomin subunit B {ECO:0000303|PubMed:7826413};
DE            Short=EA;
DE   AltName: Full=Ectatomin-Et1 subunit B {ECO:0000303|PubMed:26805882};
OS   Ectatomma tuberculatum (Selva ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ectatomminae; Ectatommini; Ectatomma.
OX   NCBI_TaxID=39300;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, TOXIC DOSE, STRUCTURE BY NMR, DISULFIDE BOND,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=7826413;
RA   Pluzhnikov K.A., Nolde D.E., Tertishnikova S.M., Sukhanov S.V., Sobol A.G.,
RA   Torgov M.Y., Filippov A.K., Arseniev A.S., Grishin E.V.;
RT   "Structure-activity study of the basic toxic component of venom from the
RT   ant Ectatomma tuberculatum.";
RL   Bioorg. Khim. 20:857-871(1994).
RN   [2]
RP   FUNCTION, AND EFFECT ON CARDIAC L-TYPE CALCIUM CURRENT.
RX   PubMed=10336635; DOI=10.1046/j.1432-1327.1999.00426.x;
RA   Pluzhnikov K., Nosyreva E., Shevchenko L., Kokoz Y., Schmalz D., Hucho F.,
RA   Grishin E.;
RT   "Analysis of ectatomin action on cell membranes.";
RL   Eur. J. Biochem. 262:501-506(1999).
RN   [3]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=26805882; DOI=10.3390/toxins8010030;
RA   Touchard A., Aili S.R., Fox E.G., Escoubas P., Orivel J., Nicholson G.M.,
RA   Dejean A.;
RT   "The biochemical toxin arsenal from ant venoms.";
RL   Toxins 8:1-28(2016).
RN   [4]
RP   STRUCTURE BY NMR, AND DISULFIDE BOND.
RX   PubMed=8033986; DOI=10.1016/0014-5793(94)00518-4;
RA   Arseniev A.S., Pluzhnikov K.A., Nolde D.E., Sobol A.G., Torgov M.Y.,
RA   Sukhanov S.V., Grishin E.V.;
RT   "Toxic principle of selva ant venom is a pore-forming protein
RT   transformer.";
RL   FEBS Lett. 347:112-116(1994).
RN   [5]
RP   STRUCTURE BY NMR, AND DISULFIDE BOND.
RX   PubMed=7881269; DOI=10.1007/bf00227465;
RA   Nolde D.E., Sobol A.G., Pluzhnikov K.A., Grishin E.V., Arseniev A.S.;
RT   "Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant
RT   venom.";
RL   J. Biomol. NMR 5:1-13(1995).
CC   -!- FUNCTION: Algogenic for animals, human and insects (PubMed:7826413). At
CC       high concentrations (0.5-1 uM), it acts as a pore-forming protein that
CC       forms nonselective cation channels both in cell and artificial
CC       membranes (PubMed:7826413). It is weakly selective for cation over
CC       anions channel conductance is identical in both directions. At lower
CC       concentrations (1-10 nM), this heterodimer inhibits cardiac L-type
CC       calcium currents in isolated rat cardiac ventricular myocytes
CC       (PubMed:10336635). {ECO:0000269|PubMed:10336635,
CC       ECO:0000269|PubMed:7826413}.
CC   -!- SUBUNIT: Heterodimer of an A and a B chain; disulfide-linked.
CC       {ECO:0000269|PubMed:7826413}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7826413}. Target
CC       cell membrane {ECO:0000305|PubMed:7826413}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:7826413}.
CC   -!- TOXIC DOSE: LD(50) is 6.8 ug/kg by intracerebroventricular injection
CC       into mice. {ECO:0000269|PubMed:7826413}.
CC   -!- SIMILARITY: Belongs to the ectatomin family. Ectatomin-Et subfamily.
CC       {ECO:0000305}.
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DR   PIR; S77895; S77895.
DR   PDB; 1ECI; NMR; -; B=1-34.
DR   PDBsum; 1ECI; -.
DR   AlphaFoldDB; P49344; -.
DR   SMR; P49344; -.
DR   MINT; P49344; -.
DR   EvolutionaryTrace; P49344; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009458; Ectatomin.
DR   InterPro; IPR036261; Ectatomin_sf.
DR   Pfam; PF06457; Ectatomin; 1.
DR   PIRSF; PIRSF005989; Ectatomin; 1.
DR   SUPFAM; SSF47401; SSF47401; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel; Ion channel impairing toxin; Ion transport;
KW   Membrane; Secreted; Target cell membrane; Target membrane; Toxin;
KW   Transport; Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..34
FT                   /note="Omega/M-ectatotoxin-Et1a subunit B"
FT                   /evidence="ECO:0000269|PubMed:7826413"
FT                   /id="PRO_0000044888"
FT   DISULFID        10..32
FT                   /evidence="ECO:0000269|PubMed:7826413,
FT                   ECO:0000269|PubMed:7881269, ECO:0000269|PubMed:8033986,
FT                   ECO:0000312|PDB:1ECI"
FT   DISULFID        20
FT                   /note="Interchain (with C-22 in subunit A)"
FT                   /evidence="ECO:0000269|PubMed:7826413,
FT                   ECO:0000269|PubMed:7881269, ECO:0000269|PubMed:8033986,
FT                   ECO:0000312|PDB:1ECI"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:1ECI"
FT   HELIX           24..31
FT                   /evidence="ECO:0007829|PDB:1ECI"
SQ   SEQUENCE   34 AA;  3786 MW;  36E9E0367813B65F CRC64;
     WSTIVKLTIC PTLKSMAKKC EGSIATMIKK KCDK
 
 
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