3S11_HYDHA
ID 3S11_HYDHA Reviewed; 81 AA.
AC P68416; A3FM51; A3FM52; P01436; P25492;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Short neurotoxin 1;
DE AltName: Full=SN12;
DE AltName: Full=Toxin 4;
DE Flags: Precursor;
OS Hydrophis hardwickii (Hardwick's spine-bellied seasnake) (Lapemis
OS hardwickii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX NCBI_TaxID=8781;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TOXIC DOSE.
RC TISSUE=Venom gland;
RX PubMed=12040423;
RA Zhong X.F., Peng L.S., Wu W.Y., Wei J.W., Yang H., Yang Y.Z., Xu A.L.;
RT "Identification and functional characterization of three postsynaptic
RT short-chain neurotoxins from hydrophiinae, Lapemis hardwickii Gray.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 33:457-462(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Tan T., Bi Q., Xiang X., Zhu S.;
RT "The study of the neurotoxins in sea snake using cDNA phage display
RT technology.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 22-81, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=891966; DOI=10.1016/0014-5793(77)80443-2;
RA Fox J.W., Elzinga M., Tu A.T.;
RT "Amino acid sequence of a snake neurotoxin from the venom of Lapemis
RT hardwickii and the detection of a sulfhydryl group by laser Raman
RT spectroscopy.";
RL FEBS Lett. 80:217-220(1977).
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:891966}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 0.0956 mg/kg by intraperitoneal injection into
CC mice. {ECO:0000269|PubMed:12040423}.
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; EF405869; ABN54804.1; -; mRNA.
DR EMBL; EF405870; ABN54805.1; -; mRNA.
DR AlphaFoldDB; P68416; -.
DR SMR; P68416; -.
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:891966"
FT CHAIN 22..81
FT /note="Short neurotoxin 1"
FT /evidence="ECO:0000269|PubMed:891966"
FT /id="PRO_0000093585"
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 CONFLICT 3
FT /note="T -> L (in Ref. 2; ABN54805)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="P -> S (in Ref. 2; ABN54805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 81 AA; 8988 MW; F3F62372BB2ECF10 CRC64;
MKTLLLTLVV VTIVCLDLGY TMTCCNQQSS QPKTTTNCAE SSCYKKTWSD HRGTRIERGC
GCPQVKPGIK LECCHTNECN N