SCX3_ANDMA
ID SCX3_ANDMA Reviewed; 64 AA.
AC P0C910;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Alpha-toxin Amm3;
DE AltName: Full=Amm III;
OS Androctonus mauritanicus mauritanicus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6860;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18243273; DOI=10.1016/j.toxicon.2007.12.012;
RA Oukkache N., Rosso J.-P., Alami M., Ghalim N., Saile R., Hassar M.,
RA Bougis P.E., Martin-Eauclaire M.-F.;
RT "New analysis of the toxic compounds from the Androctonus mauretanicus
RT mauretanicus scorpion venom.";
RL Toxicon 51:835-852(2008).
RN [2]
RP AMINO-ACID COMPOSITION.
RC TISSUE=Venom;
RX PubMed=3992595; DOI=10.1016/0041-0101(85)90114-x;
RA Rosso J.-P., Rochat H.;
RT "Characterization of ten proteins from the venom of the Moroccan scorpion
RT Androctonus mauretanicus mauretanicus, six of which are toxic to the
RT mouse.";
RL Toxicon 23:113-125(1985).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=1949066; DOI=10.1016/0041-0101(91)90078-6;
RA Zerrouk H., Bougis P.E., Ceard B., Benslimane A., Martin-Eauclaire M.-F.;
RT "Analysis by high-performance liquid chromatography of Androctonus
RT mauretanicus mauretanicus (black scorpion) venom.";
RL Toxicon 29:951-960(1991).
CC -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC channels (Nav) and inhibit the inactivation of the activated channels,
CC thereby blocking neuronal transmission. {ECO:0000269|PubMed:1949066}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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=7001.82; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18243273};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C910; -.
DR SMR; P0C910; -.
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:0006952; P:defense response; IEA:InterPro.
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; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..64
FT /note="Alpha-toxin Amm3"
FT /id="PRO_0000368018"
FT DOMAIN 2..63
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 20..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 24..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 64 AA; 7009 MW; C9DF7318E3835115 CRC64;
GRDGYIVDTK NCVYHCYPPC DGLCKKNQAK SGSCGFLYPS GLACWCVALP ENVPIKDPND
DCHK
