ID   MYXC2_CRODM             Reviewed;          42 AA.
AC   P86193;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Crotamine-IV-2 {ECO:0000303|PubMed:17828447};
OS   Crotalus durissus cumanensis (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=184542;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, TOXIC DOSE, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=17828447; DOI=10.1007/s10930-007-9094-z;
RA   Ponce-Soto L.A., Martins D., Novello J.C., Marangoni S.;
RT   "Structural and biological characterization of two crotamine isoforms IV-2
RT   and IV-3 isolated from the Crotalus durissus cumanensis venom.";
RL   Protein J. 26:533-540(2007).
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       and hind limb paralysis (By similarity). It also induces potent
CC       blockade of neuromuscular transmission in young chicken biventer
CC       cervicis preparation and potent myotoxic effect. In mice, it induces
CC       myonecrosis, upon intramuscular or subcutaneous injections
CC       (PubMed:17828447). {ECO:0000250|UniProtKB:Q9PWF3,
CC       ECO:0000269|PubMed:17828447}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17828447}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17828447}.
CC   -!- MASS SPECTROMETRY: Mass=4905.95; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17828447};
CC   -!- TOXIC DOSE: LD(50) is 0.07 mg/kg by intracerebroventricular injection
CC       into mice. {ECO:0000269|PubMed:17828447}.
CC   -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR   AlphaFoldDB; P86193; -.
DR   SMR; P86193; -.
DR   TCDB; 1.C.85.2.2; the pore-forming Beta-defensin (Beta-defensin) family.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044534; P:envenomation resulting in modulation of apoptotic process in another organism; IDA:UniProtKB.
DR   GO; GO:0044521; P:envenomation resulting in muscle damage in another organism; IDA:UniProtKB.
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   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..42
FT                   /note="Crotamine-IV-2"
FT                   /evidence="ECO:0000269|PubMed:17828447"
FT                   /id="PRO_0000371460"
FT   DISULFID        4..37
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   DISULFID        11..31
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   DISULFID        19..38
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
SQ   SEQUENCE   42 AA;  4907 MW;  F542A192A9C5B90E CRC64;
     YKRCHIKGGH CFPKEKLICI PPSSDIGKMD CPWKRKCCKK RS