3S1C_LATLA
ID 3S1C_LATLA Reviewed; 62 AA.
AC P10460;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Short neurotoxin C;
OS Laticauda laticaudata (Blue-ringed sea krait) (Blue-lipped sea krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX NCBI_TaxID=8630;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=3955004; DOI=10.1021/bi00350a019;
RA Endo T., Nakanishi M., Furukawa S., Joubert F.J., Tamiya N., Hayashi K.;
RT "Stopped-flow fluorescence studies on binding kinetics of neurotoxins with
RT acetylcholine receptor.";
RL Biochemistry 25:395-404(1986).
CC -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC inhibit acetylcholine from binding to the receptor, thereby impairing
CC neuromuscular transmission.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3955004}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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 PIR; E25866; E25866.
DR AlphaFoldDB; P10460; -.
DR SMR; P10460; -.
DR Proteomes; UP000694406; Unplaced.
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; Reference proteome; Secreted; Toxin.
FT CHAIN 1..62
FT /note="Short neurotoxin C"
FT /evidence="ECO:0000269|PubMed:3955004"
FT /id="PRO_0000093586"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 3..24
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 17..41
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 43..54
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 55..60
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ SEQUENCE 62 AA; 7087 MW; AD75239110256BCE CRC64;
RRCFNQQSSQ PQTNKSCPPG ENSCYRKQWR DHRGTIIERG CGCPTVKPGV KLRCCQSEDC
NN