ID   MKTX1_MESMA             Reviewed;          64 AA.
AC   P56569;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Makatoxin-1;
DE   AltName: Full=Makatoxin I;
DE            Short=MKTXI;
DE            Short=MakatxI;
DE            Short=MkTx I;
OS   Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34649;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=9079654; DOI=10.1074/jbc.272.13.8320;
RA   Gong J., Kini R.M., Gwee M.C.E., Gopalakrishnakone P., Chung M.C.;
RT   "Makatoxin I, a novel toxin isolated from the venom of the scorpion Buthus
RT   martensi Karsch, exhibits nitrergic actions.";
RL   J. Biol. Chem. 272:8320-8324(1997).
CC   -!- FUNCTION: This protein markedly relaxes the rat carbachol-precontracted
CC       anococcygeus muscle. This relaxation is inhibited by the inhibitor of
CC       nitric oxide (NO) synthase, N-nitro-L-arginine methyl ester (L-NAME),
CC       suggesting that the response induced by this protein is NO-mediated.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=7031.71; Mass_error=2.88; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9079654};
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Alpha 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   AlphaFoldDB; P56569; -.
DR   SMR; P56569; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   CDD; cd00107; Knot1; 1.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR018218; Scorpion_toxinL.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   PRINTS; PR00285; SCORPNTOXIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin; Secreted; Toxin.
FT   CHAIN           1..64
FT                   /note="Makatoxin-1"
FT                   /id="PRO_0000066756"
FT   DOMAIN          2..64
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   64 AA;  7047 MW;  C1C2083758AE8143 CRC64;
     GRDAYIADSE NCTYTCALNP YCNDLCTKNG AKSGYCQWAG RYGNACWCID LPDKVPIRIS
     GSCR