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MYC1_CRODU
ID   MYC1_CRODU              Reviewed;          65 AA.
AC   O57540;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Crotamine CRO1 {ECO:0000303|PubMed:10484745};
DE   Flags: Precursor;
GN   Name=CRO1;
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   STRAIN=Martinopolis; TISSUE=Venom gland;
RX   PubMed=10484745; DOI=10.1016/s0041-0101(98)00226-8;
RA   Radis-Baptista G., Oguiura N., Hayashi M.A.F., Camargo M.E., Grego K.F.,
RA   Oliveira E.B., Yamane T.;
RT   "Nucleotide sequence of crotamine isoform precursors from a single South
RT   American rattlesnake (Crotalus durissus terrificus).";
RL   Toxicon 37:973-984(1999).
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:10484745}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:10484745}.
CC   -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR   EMBL; AF044674; AAC02995.1; -; mRNA.
DR   AlphaFoldDB; O57540; -.
DR   BMRB; O57540; -.
DR   SMR; O57540; -.
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   3: Inferred from homology;
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..22
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   CHAIN           23..65
FT                   /note="Crotamine CRO1"
FT                   /id="PRO_0000035183"
FT   DISULFID        26..58
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   DISULFID        33..52
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT   DISULFID        40..59
FT                   /evidence="ECO:0000250|UniProtKB:Q9PWF3"
SQ   SEQUENCE   65 AA;  7519 MW;  F840C453C5BCCE33 CRC64;
     MKILYLLFAF LFLAFLSEPG NAYKQCHKKG GHCFPKEKIC IPPSSDFGKM DCRWRWKCCK
     KGSGK
 
 
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