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