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3S11_HYDPR
ID   3S11_HYDPR              Reviewed;          81 AA.
AC   Q5UFR8; P01438; P10461; P19005; P68414;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Short neurotoxin 1;
DE   AltName: Full=Major/minor neurotoxin;
DE   Flags: Precursor;
OS   Hydrophis peronii (Spiny-headed seasnake) (Acalyptophis peronii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX   NCBI_TaxID=8676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Kini R.M., Pahari S.;
RT   "Acalyptophis peronii neurotoxin.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 22-81, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=3341735; DOI=10.1016/0003-9861(88)90418-3;
RA   Mori N., Tu A.T.;
RT   "Isolation and primary structure of the major toxin from sea snake,
RT   Acalyptophis peronii, venom.";
RL   Arch. Biochem. Biophys. 260:10-17(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-81, VARIANT GLU-64, AND TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=3202959; DOI=10.1515/bchm3.1988.369.1.521;
RA   Mori N., Tu A.T.;
RT   "Amino-acid sequence of the minor neurotoxin from Acalyptophis peronii
RT   venom.";
RL   Biol. Chem. Hoppe-Seyler 369:521-526(1988).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission. {ECO:0000250|UniProtKB:P60775}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3341735}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 0.170 mg/kg by intravenous injection into mice
CC       for the minor toxin, and 0.125 mg/kg for the major toxin.
CC       {ECO:0000269|PubMed:3202959, ECO:0000269|PubMed:3341735}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY742210; AAV33393.1; -; mRNA.
DR   PIR; A27580; A27580.
DR   AlphaFoldDB; Q5UFR8; -.
DR   SMR; Q5UFR8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:3202959,
FT                   ECO:0000269|PubMed:3341735"
FT   CHAIN           22..81
FT                   /note="Short neurotoxin 1"
FT                   /evidence="ECO:0000269|PubMed:3202959,
FT                   ECO:0000269|PubMed:3341735"
FT                   /id="PRO_5000094110"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        38..60
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        62..73
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        74..79
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   VARIANT         64
FT                   /note="Q -> E (in minor variant)"
FT                   /evidence="ECO:0000269|PubMed:3202959"
SQ   SEQUENCE   81 AA;  8860 MW;  E865C241FA5F7D04 CRC64;
     MKTLLLSPVV VTIVCLDLGY TMTCCNQQSS QPKTTTNCAG NSCYKKTWSD HRGTIIERGC
     GCPQVKSGIK LECCHTNECN N
 
 
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