SCX5_ANDMA
ID SCX5_ANDMA Reviewed; 64 AA.
AC P01482;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-toxin Amm5;
DE AltName: Full=Amm V;
DE Short=AmmV;
DE AltName: Full=Neurotoxin 5;
DE AltName: Full=Neurotoxin V;
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 AMIDATION AT ASN-64.
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 [2]
RP PARTIAL 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).
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:0000250}.
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=7280; 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 PIR; A01742; NTSR5M.
DR AlphaFoldDB; P01482; -.
DR SMR; P01482; -.
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 CDD; cd00107; Knot1; 1.
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 Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..64
FT /note="Alpha-toxin Amm5"
FT /id="PRO_0000066723"
FT DOMAIN 2..64
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 64
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:3992595"
FT DISULFID 12..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 22..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 26..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 64 AA; 7301 MW; 3D03A733534CD866 CRC64;
LKDGYIIDDL NCTFFCGRNA YCDDECKKKG GESGYCQWAS PYGNACWCYK LPDRVSIKEK
GRCN
