TX12_ANDCR
ID TX12_ANDCR Reviewed; 80 AA.
AC P0C293;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Toxin Acra I-2;
DE AltName: Full=Acra1;
DE Flags: Precursor;
OS Androctonus crassicauda (Arabian fat-tailed scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=122909;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-80, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16762386; DOI=10.1016/j.toxicon.2006.04.003;
RA Caliskan F., Garcia B.I., Coronas F.I.V., Batista C.V.F., Zamudio F.Z.,
RA Possani L.D.;
RT "Characterization of venom components from the scorpion Androctonus
RT crassicauda of Turkey: peptides and genes.";
RL Toxicon 48:12-22(2006).
CC -!- FUNCTION: Probable neurotoxin that inhibits ion channels (By
CC similarity). Is toxic to mice. Is about 2.8% of the total protein in
CC the venom. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16762386}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16762386}.
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=6496.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16762386};
CC -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC Sodium/Potassium channel inhibitor family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0C293; -.
DR SMR; P0C293; -.
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 Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 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; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:16762386"
FT CHAIN 23..80
FT /note="Toxin Acra I-2"
FT /id="PRO_0000271320"
FT DOMAIN 25..80
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 40..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 49..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 53..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 80 AA; 8889 MW; A8C39AA612AB6C91 CRC64;
MMKLALFSII VILFSLIGSI HGADVPGNYP LDSSGNKYPC TVLGDNQSCI DVCKKHGVKY
GYCYSFKCWC EFLEDKNVSI