TX1AA_ECTTU
ID TX1AA_ECTTU Reviewed; 37 AA.
AC P49343;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Omega/M-ectatotoxin-Et1a subunit A {ECO:0000303|PubMed:26805882};
DE Short=Omega/M-ECTX-Et1a subunit A {ECO:0000303|PubMed:26805882};
DE AltName: Full=Ectatomin subunit A {ECO:0000303|PubMed:7826413};
DE Short=EA;
DE AltName: Full=Ectatomin-Et1 subunit A {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; S46244; S46244.
DR PDB; 1ECI; NMR; -; A=1-37.
DR PDBsum; 1ECI; -.
DR AlphaFoldDB; P49343; -.
DR SMR; P49343; -.
DR MINT; P49343; -.
DR EvolutionaryTrace; P49343; -.
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..37
FT /note="Omega/M-ectatotoxin-Et1a subunit A"
FT /evidence="ECO:0000269|PubMed:7826413"
FT /id="PRO_0000044887"
FT DISULFID 12..34
FT /evidence="ECO:0000269|PubMed:7826413,
FT ECO:0000269|PubMed:7881269, ECO:0000269|PubMed:8033986,
FT ECO:0000312|PDB:1ECI"
FT DISULFID 22
FT /note="Interchain (with C-20 in subunit B)"
FT /evidence="ECO:0000269|PubMed:7826413,
FT ECO:0000269|PubMed:7881269, ECO:0000269|PubMed:8033986,
FT ECO:0000312|PDB:1ECI"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:1ECI"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1ECI"
SQ SEQUENCE 37 AA; 4149 MW; FCBD410800A1BF3D CRC64;
GVIPKKIWET VCPTVEPWAK KCSGDIATYI KRECGKL
