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