ID   MYX1_CROOO              Reviewed;          43 AA.
AC   P12028;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Myotoxin-1 {ECO:0000305};
DE   AltName: Full=Myotoxin I {ECO:0000303|PubMed:3629618};
OS   Crotalus oreganus concolor (Midget faded rattlesnake) (Crotalus viridis
OS   concolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8740;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=3629618; DOI=10.1016/0041-0101(87)90115-2;
RA   Bieber A.L., McParland R.H., Becker R.R.;
RT   "Amino acid sequences of myotoxins from Crotalus viridis concolor venom.";
RL   Toxicon 25:677-680(1987).
CC   -!- FUNCTION: Cationic peptide that possesses multiple functions. It acts
CC       as a cell-penetrating peptide (CPP), and as a potent voltage-gated
CC       potassium channel (Kv) inhibitor. It exhibits antimicrobial activities,
CC       hind limb paralysis, and severe muscle necrosis by a non-enzymatic
CC       mechanism. {ECO:0000250|UniProtKB:Q9PWF3}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3629618}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:3629618}.
CC   -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {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   PIR; A29089; A29089.
DR   AlphaFoldDB; P12028; -.
DR   SMR; P12028; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044564; P:envenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism; ISS:UniProtKB.
DR   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR   InterPro; IPR000881; Myotoxin.
DR   Pfam; PF00819; Myotoxins; 1.
DR   PRINTS; PR00283; MYOTOXIN.
DR   PROSITE; PS00459; MYOTOXINS_1; 1.
DR   PROSITE; PS51345; MYOTOXINS_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Myotoxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..43
FT                   /note="Myotoxin-1"
FT                   /evidence="ECO:0000269|PubMed:3629618"
FT                   /id="PRO_0000221564"
FT   DISULFID        4..36
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   DISULFID        11..30
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   DISULFID        18..37
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
SQ   SEQUENCE   43 AA;  5061 MW;  CD3B5D9B890FCF69 CRC64;
     YKRCHKKEGH CFPKTVICLP PSSDFGKMDC RWKWKCCKKG SVN