ID   3NO22_MICCO             Reviewed;          88 AA.
AC   C6JUP2;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Three-finger toxin 3FTx-2;
DE            Short=3FTx;
DE   Flags: Precursor;
OS   Micrurus corallinus (Brazilian coral snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX   NCBI_TaxID=54390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=19291316; DOI=10.1186/1471-2164-10-112;
RA   Leao L.I., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RT   "Transcriptomic basis for an antiserum against Micrurus corallinus (coral
RT   snake) venom.";
RL   BMC Genomics 10:112-112(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-36, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
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 with low affinity to muscular (alpha-1-beta-1-delta-
CC       epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal
CC       (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).
CC       {ECO:0000250|UniProtKB:O42255}.
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. Ancestral
CC       subfamily. Orphan group II sub-subfamily. {ECO:0000305}.
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DR   EMBL; GQ139602; ACS74996.1; -; mRNA.
DR   AlphaFoldDB; C6JUP2; -.
DR   SMR; C6JUP2; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.60.10; -; 1.
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; Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:21515432"
FT   CHAIN           22..88
FT                   /note="Three-finger toxin 3FTx-2"
FT                   /evidence="ECO:0000305|PubMed:21515432"
FT                   /id="PRO_0000422893"
FT   DISULFID        27..48
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        41..66
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        70..81
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        82..87
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
SQ   SEQUENCE   88 AA;  9984 MW;  24E45E0E6FC8B5F9 CRC64;
     MKTLLLTLVV VTIVCLDLGN TANTLFCDNS NVPSIRTRKR CLKNQKLCYK MTFFTPGFGW
     TQIKGCIHRC PESTPNEKYQ CCSTDNCI