ID   3S157_MICAT             Reviewed;          81 AA.
AC   F5CPD8;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Three finger toxin MALT0057C;
DE   AltName: Full=MALT0057C;
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, MASS SPECTROMETRY,
RP   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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21515432}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=6903.9; Method=Electrospray; Note=Average
CC       mass.; Evidence={ECO:0000269|PubMed:21515432};
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; JF754476; AED89565.1; -; mRNA.
DR   AlphaFoldDB; F5CPD8; -.
DR   SMR; F5CPD8; -.
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..81
FT                   /note="Three finger toxin MALT0057C"
FT                   /evidence="ECO:0000305|PubMed:21515432"
FT                   /id="PRO_0000422899"
FT   SITE            52
FT                   /note="May be critical for toxicity"
FT                   /evidence="ECO:0000250"
FT   SITE            55
FT                   /note="May be critical for toxicity"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   81 AA;  9211 MW;  4CA45BD641FD5819 CRC64;
     MKTLLLTLVV VTIVCLDFGH TMICYNQQSS QPPTTTTCSE GQCYKQRWRD HRGWRTERGC
     GCPKAIPEVK LNCCKTDRCN G