ID   3NO48_MICCO             Reviewed;          86 AA.
AC   P58370;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Alpha-neurotoxin homolog 8;
DE            Short=NXH8;
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;
RA   Prieto da Silva A.R.B.;
RL   Thesis (2001), University of Sao Paulo, Brazil.
RN   [2]
RP   PROTEIN SEQUENCE OF 22-36, AND 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 and inhibits muscular and neuronal nicotinic
CC       acetylcholine receptors (nAChR). {ECO:0000250|UniProtKB:P81783}.
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 IV sub-subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ344067; CAC50565.1; -; mRNA.
DR   AlphaFoldDB; P58370; -.
DR   SMR; P58370; -.
DR   PRIDE; P58370; -.
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   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
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..86
FT                   /note="Alpha-neurotoxin homolog 8"
FT                   /evidence="ECO:0000305|PubMed:21515432"
FT                   /id="PRO_0000035451"
FT   DISULFID        24..47
FT                   /evidence="ECO:0000250|UniProtKB:P81782"
FT   DISULFID        27..32
FT                   /evidence="ECO:0000250|UniProtKB:P81782"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000250|UniProtKB:P81782"
FT   DISULFID        68..79
FT                   /evidence="ECO:0000250|UniProtKB:P81782"
FT   DISULFID        80..85
FT                   /evidence="ECO:0000250|UniProtKB:P81782"
SQ   SEQUENCE   86 AA;  9591 MW;  7667824BC5382069 CRC64;
     MKTLLLTLVV VTIMCLDLGY TLECKICNFK TCPTDELRHC ASGETICYKT FWNTHRGLRI
     DRGCAATCPT VKPGVNIICC KTDNCN