ID   MYX2_CRODU              Reviewed;          64 AA.
AC   P24332;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Myotoxin-2;
DE   AltName: Full=Crotamine-2;
DE   Flags: Precursor; Fragment;
OS   Crotalus durissus terrificus (South American rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=2389256; DOI=10.1016/0041-0101(90)90302-n;
RA   Smith L.A., Schmidt J.J.;
RT   "Cloning and nucleotide sequences of crotamine genes.";
RL   Toxicon 28:575-585(1990).
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:0000305|PubMed:2389256}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:2389256}.
CC   -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR   PIR; B35947; B35947.
DR   AlphaFoldDB; P24332; -.
DR   SMR; P24332; -.
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; PS51345; MYOTOXINS_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Disulfide bond; Ion channel impairing toxin; Myotoxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          <1..21
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   CHAIN           22..63
FT                   /note="Myotoxin-2"
FT                   /id="PRO_0000035180"
FT   DISULFID        32..51
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   NON_TER         1
SQ   SEQUENCE   64 AA;  7306 MW;  C721AA0A51C5918D CRC64;
     KILYLLFAFL FLAFLSEPGN AYKRCHIKGG HCFPKEKICI PPSSDFGKMD CPWRRKSLKK
     GSGK