3S166_MICAT
ID 3S166_MICAT Reviewed; 83 AA.
AC F5CPE4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Three finger toxin MALT0066C;
DE AltName: Full=MALT0066C;
DE Flags: Precursor;
OS Micrurus altirostris (Uruguayan coral snake) (Elaps altirostris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=129457;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-36, SUBUNIT,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21515432; DOI=10.1016/j.jprot.2011.04.003;
RA Correa-Netto C., Junqueira-de-Azevedo Ide L., Silva D.A., Ho P.L.,
RA Leitao-de-Araujo M., Alves M.L., Sanz L., Foguel D., Zingali R.B.,
RA Calvete J.J.;
RT "Snake venomics and venom gland transcriptomic analysis of Brazilian coral
RT snakes, Micrurus altirostris and M. corallinus.";
RL J. Proteomics 74:1795-1809(2011).
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 -!- SUBUNIT: Dimer. {ECO:0000305|PubMed:21515432}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21515432}.
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 EMBL; JF754482; AED89571.1; -; mRNA.
DR AlphaFoldDB; F5CPE4; -.
DR SMR; F5CPE4; -.
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:21515432"
FT CHAIN 22..83
FT /note="Three finger toxin MALT0066C"
FT /evidence="ECO:0000305|PubMed:21515432"
FT /id="PRO_0000422904"
FT DISULFID 24..45
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 38..62
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 64..75
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 76..81
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ SEQUENCE 83 AA; 9146 MW; 8A2869A64FCB830E CRC64;
MKTLLLTLVV VTIVCLDFGH TLICYNYETP LDKTTECCGN GVTTCFAKSW RDHRGLRTDR
GCGCPNVKPG VTINCCKTDR CNG